{"title":"High-Quality Cytokines for Advanced Research","description":"\u003cp dir=\"ltr\"\u003e\u003cspan\u003eCytokines are small proteins that play a central role in cell signaling, immune response, and inflammation. Whether you're investigating immune pathways, designing therapeutic interventions, or seeking to understand the delicate balance of the body’s defense system, cytokines are essential to your work. At Beta LifeScience, we offer a curated selection of recombinant cytokines with verified bioactivity and purity—ready to support your research from start to finish.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eExplore our premium-grade inflammatory and proinflammatory cytokines, including cytokine Th1 Th2 options, all available for immediate shipment. From basic science to drug development, our catalog is designed for researchers who demand precision, consistency, and performance.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eWhat Are Cytokines and Why Do They Matter?\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eCytokines are defined as signaling proteins that facilitate communication between cells. They are secreted by various immune cells and act as messengers to regulate immunity, inflammation, and hematopoiesis. Cytokines operate through specific receptors on target cells, triggering a cascade of intracellular events that shape immune responses.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eUnderstanding \u003c\/span\u003e\u003cspan\u003ewhat cytokines are\u003c\/span\u003e\u003cspan\u003e helps unlock the mechanisms behind immune activation, suppression, and dysregulation. Whether you're studying autoimmune diseases, infectious diseases, or cancer, cytokines serve as both biomarkers and therapeutic targets.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eCytokines Definition and Functional Role\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eCytokines are a broad class of small proteins that play a vital role in regulating immune responses, inflammation, and cellular communication. The standard \u003c\/span\u003e\u003cspan\u003ecytokines definition\u003c\/span\u003e\u003cspan\u003e includes various types such as interleukins (ILs), interferons (IFNs), tumor necrosis factors (TNFs), growth factors, and chemokines. These proteins affect processes like cell differentiation, proliferation, apoptosis, and migration.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eDepending on their type, \u003c\/span\u003e\u003cspan\u003ecytokines\u003c\/span\u003e\u003cspan\u003e can either enhance or suppress immune function. Some initiate inflammation to combat infection, while others regulate the immune system to prevent overreactions. This dual behavior makes them valuable in immunology research, chronic inflammation studies, and regenerative medicine.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch3 dir=\"ltr\"\u003e\u003cspan\u003eTypes of Cytokines\u003c\/span\u003e\u003c\/h3\u003e\n\u003cul\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eInterleukins (ILs):\u003c\/strong\u003e\u003cspan\u003e Mediate communication between immune cells.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eInterferons (IFNs):\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e \u003c\/strong\u003eDefend against viral infections and modulate immune activity.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eTumor Necrosis Factors (TNFs):\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e \u003c\/strong\u003ePromote apoptosis and inflammation.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eGrowth Factors:\u003c\/strong\u003e\u003cspan\u003e Stimulate cell growth and tissue repair.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eChemokines:\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e \u003c\/strong\u003eDirect the movement of immune cells to infection or injury sites.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eInflammatory Cytokines in Disease Research\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eInflammatory cytokines\u003c\/span\u003e\u003cspan\u003e are a group of cytokines that amplify immune responses, especially during infections, injuries, or autoimmune reactions. Examples include IL-1β, IL-6, and TNF-α. These molecules are essential for initiating inflammation, attracting white blood cells, and activating endothelial cells.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eIn conditions like rheumatoid arthritis, psoriasis, and Crohn’s disease, these cytokines are overproduced, contributing to chronic inflammation and tissue damage. Researchers targeting immune-related diseases depend on high-purity \u003c\/span\u003e\u003cspan\u003ecytokines\u003c\/span\u003e\u003cspan\u003e to test experimental treatments and immune-modulating drugs.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eProinflammatory Cytokines and Their Applications\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eProinflammatory cytokines\u003c\/span\u003e\u003cspan\u003e form a critical part of the body’s early immune defense. These include IL-12, IFN-γ, and TNF-α. Their primary role is to trigger inflammation, helping to eliminate pathogens or abnormal cells quickly.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eIn the lab, \u003c\/span\u003e\u003cspan\u003eproinflammatory cytokines\u003c\/span\u003e\u003cspan\u003e are widely used in vaccine development, cancer research, and infectious disease studies. They also serve as drug targets in modern biologics that aim to reduce unwanted inflammation. Access to reliable, bioactive \u003c\/span\u003e\u003cspan\u003ecytokines\u003c\/span\u003e\u003cspan\u003e enables scientists to recreate disease conditions and evaluate potential therapies in vitro or in vivo.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eCytokine Th1 and Th2 Pathways\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eCytokines Th1 Th2\u003c\/span\u003e\u003cspan\u003e pathways represent two key branches of the immune system. Th1 cytokines like IL-2, IFN-γ, and TNF-β support cell-mediated immunity, targeting viruses and intracellular pathogens. Th2 cytokines such as IL-4, IL-5, IL-10, and IL-13 promote antibody responses and are linked to allergies and parasitic infections.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eShifts in the Th1\/Th2 balance can contribute to immune disorders, including asthma, multiple sclerosis, and autoimmune diseases. With Beta LifeScience’s catalog of recombinant cytokines, researchers can study these pathways with precision and consistency.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eWhy Researchers Choose Beta LifeScience to Buy Cytokines?\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eWhen you \u003c\/span\u003e\u003cspan\u003ebuy cytokines\u003c\/span\u003e\u003cspan\u003e from Beta LifeScience, you’re investing in confidence. Our collection features recombinant proteins expressed in mammalian systems to ensure proper folding, glycosylation, and bioactivity. Each batch undergoes rigorous testing, including SDS-PAGE, HPLC, and functional assays.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eWe serve a global community of immunologists, pharmacologists, biotechnologists, and diagnostic developers who rely on our products to deliver accurate and reliable results. From academic labs to pharmaceutical R\u0026amp;D pipelines, our cytokines are trusted for quality and reproducibility.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eDesigned for Your Workflow\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eWe understand the demands of modern research. That’s why our cytokines are:\u003c\/span\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eReady-to-ship\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e: \u003c\/strong\u003eMost cytokines are in-stock and available for same-day dispatch.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eFlexible formats\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e: \u003c\/strong\u003eChoose from various sizes to match your experimental needs.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003ePerformance-tested\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e: \u003c\/strong\u003eVerified through bioassays and purity tests.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eSpecies variety\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e:\u003c\/strong\u003e Available across human, mouse, rat, and other species.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eCustom support\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e:\u003c\/strong\u003e Need something specific? Ask about our custom cytokine services.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eWhether you're doing ELISA, flow cytometry, Western blotting, or cell-based assays, we provide the tools you need to succeed.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eApplications of Recombinant Cytokines\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eOur cytokine collection supports a wide range of applications:\u003c\/span\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eImmunotherapy development\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e: \u003c\/strong\u003eStudy cytokine interactions with immune cells or design targeted therapies for diseases like cancer.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eInflammatory disease research\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e: \u003c\/strong\u003eInvestigate chronic inflammation pathways and test anti-cytokine therapies.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eVaccine and adjuvant studies\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e: \u003c\/strong\u003eMimic immune stimulation to evaluate new vaccine candidates.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eCell culture\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e: \u003c\/strong\u003eUse cytokines to differentiate or activate immune cells like macrophages, dendritic cells, or T cells.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eRegenerative medicine\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e: \u003c\/strong\u003eExplore cytokines’ role in tissue repair and stem cell differentiation.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eLooking for recombinant IL-2, IFN-γ, or TNF-α? Our cytokines are performance-verified and ideal for sensitive applications.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eStreamline Your Research—Buy Cytokines Online\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eReady to move your project forward? Beta LifeScience makes it easy to \u003c\/span\u003e\u003cspan\u003ebuy cytokines online\u003c\/span\u003e\u003cspan\u003e with confidence. Our platform is designed for simplicity, speed, and transparency. Browse cytokines by name, function, or application, and enjoy real-time stock availability and technical support.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eWhen purchasing critical reagents, quality and consistency matter. That’s why researchers worldwide choose us—not just for the products, but for the partnership.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eRelated Protein Collections\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eMany researchers working with cytokines also explore related protein families to get a full picture of immune signaling. Consider browsing our \u003c\/span\u003e\u003ca href=\"https:\/\/www.betalifesci.com\/collections\/interleukins-and-receptors\" target=\"_blank\" rel=\"noopener\"\u003e\u003cspan\u003eInterleukins Collection\u003c\/span\u003e\u003c\/a\u003e\u003cspan\u003e for more targeted immune proteins or \u003c\/span\u003e\u003ca href=\"https:\/\/www.betalifesci.com\/collections\/growth-factors-and-receptors\" target=\"_blank\" rel=\"noopener\"\u003e\u003cspan\u003eGrowth Factors\u003c\/span\u003e\u003c\/a\u003e\u003cspan\u003e to support cellular proliferation and repair.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eWe also offer a \u003c\/span\u003e\u003ca href=\"https:\/\/www.betalifesci.com\/collections\/in-stock-recombinant-proteins\"\u003e\u003cspan\u003eRecombinant Protein Inventory\u003c\/span\u003e\u003c\/a\u003e\u003cspan\u003e for ready-to-ship solutions and\u003c\/span\u003e\u003cspan\u003e \u003c\/span\u003e\u003ca href=\"https:\/\/www.betalifesci.com\/collections\/phycobiliproteins\"\u003e\u003cspan\u003ePhycobiliproteins\u003c\/span\u003e\u003c\/a\u003e\u003cspan\u003e for advanced detection and imaging needs.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eDiscover the Power of Cytokines with Beta LifeScience\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eCytokines are at the center of immune regulation, and your research deserves tools that match your ambition. Whether you’re dissecting inflammation pathways, studying immune dysfunction, or designing the next breakthrough therapy, Beta LifeScience provides cytokines you can trust.\u003c\/span\u003e\u003c\/p\u003e","products":[{"product_id":"recombinant-human-rgma-protein-his-tag-bl-1562np","title":"Recombinant Human RGMA Protein (N-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Repulsive Guidance Molecule A is produced by our E.coli expression system and the target gene encoding Pro169-Gly422 is expressed with a 6His tag at the N-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"AAI51133.1\" target=\"_blank\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/protein\/AAI51133.1\"\u003eAAI51133.1\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepulsive guidance molecule A; RGM domain family member A; RGM\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRepulsive guidance molecule A（RGMA） is a cell membrane protein and belongs to the repulsive guidance molecule (RGM) family. It interacts with NEO1, BMP2 and BMP4. RGMA is a glycosylphosphatidylinositol-anchored glycoprotein that functions as an axon guidance protein in the developing and adult central nervous system. It helps guide Retinal Ganglion Cell (RGC) axons to the tectum in the midbrain. RGMa has been implicated to play an important role in the developing brain and in the scar tissue that forms after a brain injury. This protein may also function as a tumor suppressor in some cancers.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e29.8 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e30 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSupplied as a 0.2 μm filtered solution of 20mM PB, 10% Trehalose, 50% Glycerol, 1mM DTT, 0.05% Tween80, pH 7.8.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eStore at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped on dry ice\/polar packs.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915104485601,"sku":"BL-1562NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYOAKPoyAAB-M1r4AiQ511_8ea461f7-ed96-4075-b14c-cf1cc14bdf36.jpg?v=1685853416"},{"product_id":"recombinant-mouse-hcfc2-protein-his-tag-bl-1576np","title":"Recombinant Mouse HCFc2 Protein (N-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Host Cell Factor 2 is produced by our E.coli expression system and the target gene encoding Met1-Glu486 is expressed with a 6His tag at the N-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"G5E837\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/G5E837\/entry\"\u003eG5E837\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHost cell factor 2 ;HCF-2;C2 factor;Hcfc2\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHost cell factor 2(HCFC2) is a cytoplasmic protein. It contains 2 fibronectin type-III domains.HCFC2 binds KMT2A\/MLL1, as component of the MLL1\/MLL complex.Hcfc2 negative regulation of transcription from RNA polymerase II promoter.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e55.2 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e55 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSupplied as a 0.2 μm filtered solution of PBS, 2M Urea, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eStore at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped on dry ice\/polar packs.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915106484449,"sku":"BL-1576NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYaAANFXAAC1G2WNtTc685_0d796b66-4951-43ad-99cc-e74f4571fa37.jpg?v=1685853492"},{"product_id":"recombinant-human-nrg1-beta-protein-bl-1688np","title":"Recombinant Human NRG1Beta Protein (65AA)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Neuregulin-1 Beta is produced by our E.coli expression system and the target gene encoding Ser177-Glu241 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"Q02297-6\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/Q02297\/entry#Q02297-6\"\u003eQ02297-6\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePro-neuregulin-1; Neuregulin-1 beta 1; NRG1-beta 1; HRG1-beta 1; EGF;NRG1; GGF; HGL; HRGA; NDF; SMDF\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eneuregulin-1 (heregulin-1，NRG1) is a member of  neuregulin family, which is comprised of four genes that encode a large number of secreted or membrane-bound isoforms. All family members share an EGF-like domain that interacts with the ErbB family of tyrosine kinase receptors. NRG1 isoforms can be classified into type I, type II and type III isoforms. NRG1 directs ligand for ERBB3 and ERBB4 tyrosine kinase receptors, concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. NRG proteins show distinct spatial and temporal expression patterns and play important roles during development of both the nervous system and the heart.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e7.5 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e8-10 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915101700321,"sku":"BL-1688NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYaAYFKwAACiO_luCd4828_8e5156a0-1a04-4d27-84ee-cdf62839dd98.jpg?v=1685853310"},{"product_id":"recombinant-mouse-ngf-ngfb-protein-bl-1697np","title":"Recombinant Mouse Beta-NGF Protein (110AA)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Beta-Nerve Growth Factor is produced by our E.coli expression system and the target gene encoding Met130-Arg239 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP01139\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBeta-Nerve Growth Factor; Beta-NGF; NGF; NGFB;β-NGF\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNGF is the first member discovered in the Neurotrophin family, which includes brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4). These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Mouse beta -NGF is a homodimer of two 120 amino acid polypeptides. It shares approximately 90% homology at the amino acid level with human beta -NGF and 95.8% with rat beta -NGF. NGF signaling has been shown to play an important role in neuroprotection and repair. β-NGF acts as a growth and differentiation factor for B lymphocytes, and enhances B-cell survival. It is a potent neurotrophic factor that signals through its receptor β-NGFR, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e12.4 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 200mM NaCl, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBiologically active. Please contact us to obtain bioactivity data.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival. The immature NGF precursor (proNGF) functions as ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and\/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse. In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI. Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer. The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted. Endosome lumen.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            mmu:18049           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            10090.ENSMUSP00000102538           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29875237            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Mechanoinsensitive ''silent'' nociceptors are characterized by the expression of the nicotinic acetylcholine receptor subunit alpha-3 (CHRNA3); the mechanically gated ion channel PIEZO2 mediates NGF-induced mechanosensitivity in these neurons.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29241539            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            antibodies raised against NGF, TrkA, and p75 (also known as CD271) were used to explore the expression of these antigens in the non-decalcified young mouse femur.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29166838            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            An inducible mouse model that can dissect the contribution of autocrine direct action of cleavage-resistant proNGF on systemic microvascular abnormalities in both retina and kidney, major targets for microvascular complication.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29253516            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            both in vivo mechanical loading and in vitro mechanical stretch were shown to induce the profound up-regulation of NGF in osteoblasts within 1 h of loading.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28416686            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Nerve growth factor negatively regulates bone marrow granulopoiesis during small intestinal inflammation            \u003ca rel=\"nofollow\"\u003e             PMID:                        26683342            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study may represent a common mechanism for selective follicular activation induced by a localized increase in NGF in interstitial cells and mediated via the mTOR signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28542147            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            nerve growth factor (NGF) signaling through neurotrophic tyrosine kinase receptor type 1 (TrkA) directs innervation of the developing mouse femur to promote vascularization and osteoprogenitor lineage progression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27568565            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mechanical stress-induced upregulation of NGF in colon SMC underlies the visceral hypersensitivity in bowel obstruction through increased gene expression and activity of tetrodotoxin-resistant Na channels in sensory neurons.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28079757            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results suggest that perivascular nerves innervate neovessels as neovasculatures mature and that NGF accelerates the innervation of perivascular nerves in neovessels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27493098            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings reveal a non-neuronal role for neurotrophins and identify a new regulatory pathway in insulin secretion that can be targeted to ameliorate beta cell dysfunction.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27825441            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF signalling directly controls basal APP phosphorylation, subcellular localization and BACE cleavage.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27076121            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF facilitates OVA with lowLPS-induced maturation of mouse BMDCs through LPS-up-regulated p75 NTR via activation of NF-kappaB pathways, providing another mechanism for the involvement of NGF in the Th2 response            \u003ca rel=\"nofollow\"\u003e             PMID:                        27437725            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF-OE mice exhibit age-dependent increases in Substance P and CGRP in the urothelium and hyperinnervation of the bladder.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27342083            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TNF-alpha upregulated Nerve Growth Factor [NGF] expression in synovial fibroblasts and macrophages and IL-1beta upregulated NGF expression in synovial fibroblasts. IL-1beta and TNF-alpha may regulate NGF signaling in Osteoarthritic joints and be suitable therapeutic targets for treating Osteoarthritis pain            \u003ca rel=\"nofollow\"\u003e             PMID:                        27635406            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            functional PAP(thorn) neurons are essential for the analgesic effect, which is mediated by NGF-trkA signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27306411            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF negatively regulates growth cone retrograde actin flow on laminin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26631553            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In E-Reeler retinas, NGF was significantly increased in retinal ganglion cells and glial cells. E-Reeler retinal bipolar cells and RGCs overexpress NGF and p75(NTR) as a protective endogenous response to Reelin deprivation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26066836            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The NGF-induced up-regulation of TRPV1 via the increased synthesis and release of endogenous CGRP leads to improved cardiac performance in I\/R-injured diabetic heart.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25650182            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF effects on parasympathetic nerves may regulate airway smooth muscle.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25647301            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ginger extract has a synaptogenic effect via NGF-induced ERK\/CREB activation, resulting in memory enhancement.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25049196            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Proinflammatory cytokines in osteoarthritis (OA) joints and the increased mechanical loading of cartilage may mediate OA pain via the stimulation of NGF expression and release by chondrocytes            \u003ca rel=\"nofollow\"\u003e             PMID:                        24438745            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Despite being highly conserved, NGF and proNGF of mouse and human origins show distinct properties.Special care must be taken in performing experiments with cross-species systems.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25496838            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF exhibits anti-oxidative and hepatoprotective effects and is suggested to be therapeutically applicable in treating cholestatic liver diseases.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25397406            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate that analgesic effect of CB1 activation may in part be due to inhibition of NGF-induced sensitization of TRPV1 and also that the effect of CB1 activation is at least partly mediated by attenuation of NGF-induced increased PI3 signaling            \u003ca rel=\"nofollow\"\u003e             PMID:                        25088915            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF induces removal of active caspase-3 in a lysosome-dependent manner.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24787014            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results indicate that NGF exerts antileishmanial effect by stimulating hydrogen peroxide production in macrophages.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24937592            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            iron accumulation induces NGF expression in hepatocytes, which in turn leads to LSEC defenestration via TrkA            \u003ca rel=\"nofollow\"\u003e             PMID:                        25460199            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings suggest that overexpression of NGF in the ovary may suffice to cause both reproductive and metabolic alterations characteristic of polycystic ovary-like syndrome (PCOS) and support the hypothesis that sympathetic hyperactivity may contribute to the development and\/or progression of PCOS.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25211588            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The increased NGF concentrations abolish Sema3A-induced inhibitory effect on axon outgrowth, while they have no effect on Sema3A-induced collapse rate.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24338202            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that proNGF may appeal a new pathway or possible mechanism underlying microglial toxicity in the neuroinflammation and a potential target for therapeutic manipulation of the neurodegenerative diseases.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24040063            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            beta-NGF gene transfection promotes the differentiation of bone marrow stromal stem cells into neurons through regulation of AKT and MAPKs signaling pathways.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23934089            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            mechanical stimulation may attenuate NGFbeta signaling through Rac1            \u003ca rel=\"nofollow\"\u003e             PMID:                        23989259            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Independent of genotype, folate deficiency affects NGF levels in the frontal cortex, amygdala and hippocampus.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23623989            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            calcineurin\/NFAT pathway mediates the upregulation of PAI-1 by NGF            \u003ca rel=\"nofollow\"\u003e             PMID:                        23825664            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ProNGF\\NGF imbalance triggers learning and memory deficits, neurodegeneration and spontaneous epileptic-like discharges in transgenic mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23538417            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            elevated levels of NGF in target tissues stimulate sympathetic and sensory axonal sprouting            \u003ca rel=\"nofollow\"\u003e             PMID:                        23322532            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PIP5Kalpha acts as a negative regulator of nerve growth factor-induced neurite outgrowth by inhibiting PI3K\/Akt signaling pathway in PC12 cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23538529            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that diet factors (i.e., olive pomace polyphenols) up-regulate NGF\/TrkA (proto-oncogene trk) and BDNF\/TrkB (brain derived neurotrophic factor\/receptor) in hippocampus\/olfactory bulb and down-regulate NGF\/BDNF in frontal cortex\/striatum.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23466052            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that expression of NGF is down-regulated in wounded skin (epidermis) in diabetes; among the growth factors investigated, only expression of NGF was down-regulated in healing skin wounds of diabetic mice as compared to nondiabetic mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23426701            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            proNGF selectively promotes the growth of neurites from a subset of NGF-responsive neurons by a p75(NTR)-dependent mechanism during postnatal development when the axons of these neurons are ramifying within their targets in vivo            \u003ca rel=\"nofollow\"\u003e             PMID:                        23633509            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Overexpression of mouse NGF in urothelium \u0026amp; detrusor affected transcription of PAC1, VPAC1, VPAC2, PAPCAP, VIP \u0026amp; other peptides normally \u0026amp; in cyclophosphamide-induced cystitis. The changes were tissue- and disease-duration dependent.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22700375            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The HTM1 heterodimer of 2 NGF muteins binds p75 and TrkA on opposite sides of the heterodimer, but not 2 TrkA receptors, supporting the ligand passing of NGF from p75 to TrkA via a transient heteroreceptor complex of p75-NGF-TrkA.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22903500            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our results suggest that BDNF-TrkB but not NGF-TrkA signaling is involved in the brain repair after ICH, and early proper treadmill exercise might promote this repair process.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22999926            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of NGF in hippocampus, cortex, and adrenal gland of wild type animal tended to decrease following spaceflight.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22808101            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrated that both TrkA and NGF support the survival of only a subset of basal forebrain cholinergic neuron during brain development.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23100411            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Letter: NGF-p75 and neuropsin\/KLK8 pathways may cooperate in regulation of epidermal homeostasis in inflamed skin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22520925            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            that NGF derived from bronchial and alveolar epithelium plays an important role in airway hyperresponsiveness after chronic exposure to mite antigen            \u003ca rel=\"nofollow\"\u003e             PMID:                        22168511            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Therapeutic potential of NGF for the prevention of cardiomyopathy in diabetic subjects.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22187379            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF exerts profibrotic activities in the airways by inducing type III collagen production in fibroblasts            \u003ca rel=\"nofollow\"\u003e             PMID:                        21816457            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915102257377,"sku":"BL-1697NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLVqAb-UOAADAjuU8JvM359_c447bbe5-a0dd-4511-8908-084faf3df6c5.jpg?v=1685853334"},{"product_id":"recombinant-human-ngf-ngfb-protein-bl-1701np","title":"Recombinant Human Beta-NGF Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Beta-Nerve Growth Factor is produced by our E.coli expression system and the target gene encoding Ser122-Ala241 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP01138\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBeta-Nerve Growth Factor; Beta-NGF; NGF; NGFB;β-NGF\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHuman β-Nerve Growth Factor (β-NGF) was initially isolated in the mouse submandibular gland. It is composed of three non-covalently linked subunits α, β, and γ; it exhibits all the biological activities ascribed to NGF. It is structurally related to BDNF, NT-3 and NT-4 and belongs to the cysteine-knot family of growth factors that assume stable dimeric structures. Β-NGF is a neurotrophic factor that signals through its receptor β-NGF, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems. Β-NGF also acts as a growth and differentiation factor for B lymphocytes and enhances B-cell survival. These results suggest that β-NGF is a pleiotropic cytokine, which in addition to its neurotropic activities may have an important role in the regulation of the immune system. Human β-NGF shares 90% sequence similarity with mouse protein and shows cross-species reactivity.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13.4 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e14 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (Probable). The immature NGF precursor (proNGF) functions as ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and\/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse. In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI. Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer. The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted. Endosome lumen.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            7808           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            162030           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4803           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000358525           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29527653            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Single nucleotide polymorphisms in NGF gene (rs6330) and NGFR gene (rs2072446 and rs734194) are associated with ischemic stroke. The NGF rs6330*T and NGFR rs2072446*T minor alleles might be nominated as a risk factor for developing ischemic stroke and NGFR rs734194*G minor allele as a protective against this disease at least in Armenian population            \u003ca rel=\"nofollow\"\u003e             PMID:                        29499660            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Neurotrophic factors and hippocampal activity in PTSD            \u003ca rel=\"nofollow\"\u003e             PMID:                        29799860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SNRPA may contribute to GC progression via NGF and could be a prognostic biomarker for GC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30039889            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that NGF signalling is strongly linked to pathological and regenerative processes in human teeth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28465581            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggest an interaction between NGF, GDNF and MMP-9 during the transition to malignancy in prostate cancer (PC). Also this interaction may involve in regulating PC cell differentiation, tumor invasion, progression, and the agressiveness of PC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28237042            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the anti-tumor activity of oleuropein against hepatocellular carcinoma could be attributed to influencing the pro-NGF\/NGF balance via affecting MMP-7 activity without affecting the gene expression of NGF            \u003ca rel=\"nofollow\"\u003e             PMID:                        29476769            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            co-expression patterns of NGF and heme oxygenase-1 might be used as prognostic indicators for gastric carcinoma patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        28679437            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This review will briefly address the peripheral and central sensitization mechanisms of airway neurons and will then focus on NGF signaling and its role in cough hypersensitivity.[review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        28494216            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            First-trimester plasma nerve growth factor is lower in patients who subsequently develop preeclampsia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27513943            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study show evidence of variation in plasmatic beta-NGF expression during the progression of dementia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27802234            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF is functionally linked to beta-catenin, promoting the migration of human ovarian cancer cells via the WNT\/beta-catenin pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27835587            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Varicella zoster virus DNA replication is regulated in part by an NGF pathway that is PI3-kinase-independent.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27683235            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Many studies indicate that the only presence of NGF is unable to generate cell carcinogenesis, both in normal neuronal and non-neuronal cells\/tissues. However, it cannot be excluded the possibility that the co-expression of NGF and pro-carcinogenic molecules might open to different consequence. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27439311            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the effect and underlying mechanisms of NGF\/BDNF on the production of NPW in PC12 cells and hypothalamus, is reported.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28249734            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data support a role for islet NGF in fine-tuning insulin secretion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27424144            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study indicated that dysmenorrhea pain severity is partly genetically determined by the chromosome 1p13.2, near the nerve growth factor locu.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27454463            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings suggest that IL-1beta and TNF-alpha regulate Nerve Growth Factor expression and production in synovial macrophages and fibroblasts in osteoarthritic joints.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28677145            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results advance our knowledge of the conformational properties of proNGF and NGF and help provide a rationale for the diverse biological effects of NGF and proNGF at the molecular level.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28798232            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study suggest that proNGF protein levels may augment the diagnostic accuracy of currently used CSF biomarker panels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26825093            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Neuroimmune-endocrine events may lead to overactivity of sympathetic nervous system that triggers cascade of pathologic conditions in ovary in polycystic ovary syndrome (PCOS). Data suggest women with PCOS exhibit reduction of CRH and NGF; reduction of CRH\/NGF may be under influence of sympathetic nervous system and may reflect deficit of neuronal stress-adaptation in PCOS patients. (CRH = corticotropin releasing hormone)            \u003ca rel=\"nofollow\"\u003e             PMID:                        27908212            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The rare nerve growth factor-beta (NGFB) mutation R221W causes a selective loss of thinly myelinated fibers and especially unmyelinated C-fibers. Carriers of this mutation show altered pain sensation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27146986            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF expression was positively correlated with disease severity and visceral hypersensitivity in irritable bowel syndrome patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27862119            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a stage-related modulation of beta-NGF and its receptors in the inflammatory process of OA            \u003ca rel=\"nofollow\"\u003e             PMID:                        28253191            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BDNF and NGF serum levels are reduced in the early and moderate glaucoma stages, suggesting the possibility that both factors could be further investigated as potential circulating biomarkers for the early detection of glaucoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28068360            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            overexpression of ARMS blocked NGF-mediated secretion, without affecting basal secretion, a decrease in ARMS resulted in potentiation. Similar effects were observed with synembryn-B, a protein that interacts directly with ARMS. Downstream of ARMS and synembryn-B are Galphaq and Trio proteins, which modulate the activity of Rac1 in response to NGF            \u003ca rel=\"nofollow\"\u003e             PMID:                        26966186            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that the standardized nerve growth factor (NGF) concentration was negatively correlated with continuous pain, neuropathic pain and total score, and the standardized S100 proteins S100A8\/A9 concentration was positively correlated with present pain intensity and continuous pain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27936243            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate that NGF inhibited CRT translocation induced by mitoxantrone. NGF effect on CRT translocation could have consequences in immunotherapy, potentially lessening the effectiveness of this type of treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28260038            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF stimulates generation of neurons, but not neuronal progenitors from embryonic stem cells and affects the proportion of specific types of neurons in cultures of differentiating embryonic stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28364186            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF attenuates these responses-both in vivo and in vitro. Therefore, NGF therapy may represent a novel approach for the management of diabetic keratopathy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27978558            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF signaling pathway provides a potential target for developing molecularly targeted therapies            \u003ca rel=\"nofollow\"\u003e             PMID:                        27792755            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these data suggest a positive feedback loop through which NGF-mediated upregulation of p75(NTR) can contribute to the chemo-resistance of Triple negative breast cancer cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27577679            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Based on these current developments, the present review provides not only a broad overview of the biological effects of NGF-TrkA-p75NTR on cancer cells and their microenvironment, but also explains why NGF and its receptors are going to evoke major interest as promising therapeutic anti-cancer targets in the coming decade.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27264679            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF\/CD133 might be an effective and potent therapeutic target for pancreatic cancer metastasis, particularly in perineural invasion            \u003ca rel=\"nofollow\"\u003e             PMID:                        27654574            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The analysis of covariance (ANCOVA) indicated that the mean serum GDNF and NTF3 levels of ADHD patients were significantly higher than that of controls. However, serum BDNF and NGF levels did not show any significant differences between groups.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27561780            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            All patients had serum neurotrophin (NT-3, BDNF, NGF) concentrations determined.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27367919            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum NGF does not differentiate between recurrent acute pancreatitis and chronic pancreatitis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27020638            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF FLIPs TrkA onto the death TRAIL in neuroblastoma cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        26962689            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Major depression patients had similar serum NGF to controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27008247            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data demonstrate the involvement and modulation of nerve growth factor and its receptors in chronic obstructive pulmonary disease and in its staging            \u003ca rel=\"nofollow\"\u003e             PMID:                        26408608            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study showed that IL-17, in addition to stimulating an inflammatory response, negatively regulates the action of NGF and NGF R in the polar forms of the leprosy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26616164            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Locally increased estrogen levels and inflammation may cause increased NGF production in the uterus of patients with adenomyosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25519715            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study is the first to thoroughly assess the enhancement of neural differentiation of bone marrow mesenchymal stem cells following transfection with bFGF and NGF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26572749            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest MMP7 (matrix metalloproteinase 7) in follicular fluid cleaves proNGF (pro-nerve growth factor) in ovarian follicle; both MMP7 and proNGF appear to be products of granulosa cells; processing of proNGF to NGF appears to regulate apoptosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26457789            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF promotes renal fibrosis via TGF-beta1-signaling activation, suggesting that in kidney diseases high NGF serum levels could contribute to worsen renal fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26066770            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study suggests that the circadian rhythm in the esophagus may be important for the mediation of and\/or the response to erosive damage in GERD patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26337663            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Intratumoral nerve growth factor expression is not associated with perineural invasion in patients with resected extrahepatic cholangiocarcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26547754            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF has a role in modulating trkANGFR\/p75NTR in alphaSMA-expressing conjunctival fibroblasts from human ocular cicatricial pemphigoid            \u003ca rel=\"nofollow\"\u003e             PMID:                        26569118            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF-induced tyrosine kinase independent TrkA signaling through CD44 is sufficient to maintain tumor aggressiveness in breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        25840418            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Urinary NGF, but not BDNF, levels decreased significantly after hyaluronic acid therapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24614892            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915099439329,"sku":"BL-1701NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLSGAWtdsAACfla_PP38662_6a4bfe57-137c-4180-b700-1e7b0e34f79f.jpg?v=1685853214"},{"product_id":"recombinant-human-ngf-ngfb-protein-bl-1705np","title":"Recombinant Human Beta-NGF Protein (Mammalian)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Beta-Nerve Growth Factor is produced by our Mammalian expression system and the target gene encoding Ser122-Arg239 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP01138\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBeta-Nerve Growth Factor; Beta-NGF; NGF; NGFB;β-NGF\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHuman β-Nerve Growth Factor (β-NGF) was initially isolated in the mouse submandibular gland. It is composed of three non-covalently linked subunits α, β, and γ; it exhibits all the biological activities ascribed to NGF. It is structurally related to BDNF, NT-3 and NT-4 and belongs to the cysteine-knot family of growth factors that assume stable dimeric structures. Β-NGF is a neurotrophic factor that signals through its receptor β-NGF, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems. Β-NGF also acts as a growth and differentiation factor for B lymphocytes and enhances B-cell survival. These results suggest that β-NGF is a pleiotropic cytokine, which in addition to its neurotropic activities may have an important role in the regulation of the immune system. Human β-NGF shares 90% sequence similarity with mouse protein and shows cross-species reactivity.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13.3 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e14 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 250mM NaCl, pH 7.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by SEC-HPLC. (Regularly tested)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBiologically active. Please contact us to obtain bioactivity data.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (Probable). The immature NGF precursor (proNGF) functions as ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and\/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse. In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI. Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer. The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted. Endosome lumen.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            7808           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            162030           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4803           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000358525           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29527653            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Single nucleotide polymorphisms in NGF gene (rs6330) and NGFR gene (rs2072446 and rs734194) are associated with ischemic stroke. The NGF rs6330*T and NGFR rs2072446*T minor alleles might be nominated as a risk factor for developing ischemic stroke and NGFR rs734194*G minor allele as a protective against this disease at least in Armenian population            \u003ca rel=\"nofollow\"\u003e             PMID:                        29499660            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Neurotrophic factors and hippocampal activity in PTSD            \u003ca rel=\"nofollow\"\u003e             PMID:                        29799860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SNRPA may contribute to GC progression via NGF and could be a prognostic biomarker for GC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30039889            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that NGF signalling is strongly linked to pathological and regenerative processes in human teeth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28465581            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggest an interaction between NGF, GDNF and MMP-9 during the transition to malignancy in prostate cancer (PC). Also this interaction may involve in regulating PC cell differentiation, tumor invasion, progression, and the agressiveness of PC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28237042            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the anti-tumor activity of oleuropein against hepatocellular carcinoma could be attributed to influencing the pro-NGF\/NGF balance via affecting MMP-7 activity without affecting the gene expression of NGF            \u003ca rel=\"nofollow\"\u003e             PMID:                        29476769            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            co-expression patterns of NGF and heme oxygenase-1 might be used as prognostic indicators for gastric carcinoma patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        28679437            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This review will briefly address the peripheral and central sensitization mechanisms of airway neurons and will then focus on NGF signaling and its role in cough hypersensitivity.[review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        28494216            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            First-trimester plasma nerve growth factor is lower in patients who subsequently develop preeclampsia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27513943            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study show evidence of variation in plasmatic beta-NGF expression during the progression of dementia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27802234            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF is functionally linked to beta-catenin, promoting the migration of human ovarian cancer cells via the WNT\/beta-catenin pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27835587            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Varicella zoster virus DNA replication is regulated in part by an NGF pathway that is PI3-kinase-independent.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27683235            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Many studies indicate that the only presence of NGF is unable to generate cell carcinogenesis, both in normal neuronal and non-neuronal cells\/tissues. However, it cannot be excluded the possibility that the co-expression of NGF and pro-carcinogenic molecules might open to different consequence. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27439311            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the effect and underlying mechanisms of NGF\/BDNF on the production of NPW in PC12 cells and hypothalamus, is reported.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28249734            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data support a role for islet NGF in fine-tuning insulin secretion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27424144            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study indicated that dysmenorrhea pain severity is partly genetically determined by the chromosome 1p13.2, near the nerve growth factor locu.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27454463            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings suggest that IL-1beta and TNF-alpha regulate Nerve Growth Factor expression and production in synovial macrophages and fibroblasts in osteoarthritic joints.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28677145            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results advance our knowledge of the conformational properties of proNGF and NGF and help provide a rationale for the diverse biological effects of NGF and proNGF at the molecular level.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28798232            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study suggest that proNGF protein levels may augment the diagnostic accuracy of currently used CSF biomarker panels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26825093            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Neuroimmune-endocrine events may lead to overactivity of sympathetic nervous system that triggers cascade of pathologic conditions in ovary in polycystic ovary syndrome (PCOS). Data suggest women with PCOS exhibit reduction of CRH and NGF; reduction of CRH\/NGF may be under influence of sympathetic nervous system and may reflect deficit of neuronal stress-adaptation in PCOS patients. (CRH = corticotropin releasing hormone)            \u003ca rel=\"nofollow\"\u003e             PMID:                        27908212            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The rare nerve growth factor-beta (NGFB) mutation R221W causes a selective loss of thinly myelinated fibers and especially unmyelinated C-fibers. Carriers of this mutation show altered pain sensation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27146986            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF expression was positively correlated with disease severity and visceral hypersensitivity in irritable bowel syndrome patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27862119            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a stage-related modulation of beta-NGF and its receptors in the inflammatory process of OA            \u003ca rel=\"nofollow\"\u003e             PMID:                        28253191            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BDNF and NGF serum levels are reduced in the early and moderate glaucoma stages, suggesting the possibility that both factors could be further investigated as potential circulating biomarkers for the early detection of glaucoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28068360            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            overexpression of ARMS blocked NGF-mediated secretion, without affecting basal secretion, a decrease in ARMS resulted in potentiation. Similar effects were observed with synembryn-B, a protein that interacts directly with ARMS. Downstream of ARMS and synembryn-B are Galphaq and Trio proteins, which modulate the activity of Rac1 in response to NGF            \u003ca rel=\"nofollow\"\u003e             PMID:                        26966186            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that the standardized nerve growth factor (NGF) concentration was negatively correlated with continuous pain, neuropathic pain and total score, and the standardized S100 proteins S100A8\/A9 concentration was positively correlated with present pain intensity and continuous pain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27936243            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate that NGF inhibited CRT translocation induced by mitoxantrone. NGF effect on CRT translocation could have consequences in immunotherapy, potentially lessening the effectiveness of this type of treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28260038            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF stimulates generation of neurons, but not neuronal progenitors from embryonic stem cells and affects the proportion of specific types of neurons in cultures of differentiating embryonic stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28364186            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF attenuates these responses-both in vivo and in vitro. Therefore, NGF therapy may represent a novel approach for the management of diabetic keratopathy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27978558            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF signaling pathway provides a potential target for developing molecularly targeted therapies            \u003ca rel=\"nofollow\"\u003e             PMID:                        27792755            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these data suggest a positive feedback loop through which NGF-mediated upregulation of p75(NTR) can contribute to the chemo-resistance of Triple negative breast cancer cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27577679            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Based on these current developments, the present review provides not only a broad overview of the biological effects of NGF-TrkA-p75NTR on cancer cells and their microenvironment, but also explains why NGF and its receptors are going to evoke major interest as promising therapeutic anti-cancer targets in the coming decade.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27264679            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF\/CD133 might be an effective and potent therapeutic target for pancreatic cancer metastasis, particularly in perineural invasion            \u003ca rel=\"nofollow\"\u003e             PMID:                        27654574            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The analysis of covariance (ANCOVA) indicated that the mean serum GDNF and NTF3 levels of ADHD patients were significantly higher than that of controls. However, serum BDNF and NGF levels did not show any significant differences between groups.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27561780            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            All patients had serum neurotrophin (NT-3, BDNF, NGF) concentrations determined.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27367919            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum NGF does not differentiate between recurrent acute pancreatitis and chronic pancreatitis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27020638            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF FLIPs TrkA onto the death TRAIL in neuroblastoma cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        26962689            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Major depression patients had similar serum NGF to controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27008247            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data demonstrate the involvement and modulation of nerve growth factor and its receptors in chronic obstructive pulmonary disease and in its staging            \u003ca rel=\"nofollow\"\u003e             PMID:                        26408608            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study showed that IL-17, in addition to stimulating an inflammatory response, negatively regulates the action of NGF and NGF R in the polar forms of the leprosy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26616164            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Locally increased estrogen levels and inflammation may cause increased NGF production in the uterus of patients with adenomyosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25519715            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study is the first to thoroughly assess the enhancement of neural differentiation of bone marrow mesenchymal stem cells following transfection with bFGF and NGF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26572749            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest MMP7 (matrix metalloproteinase 7) in follicular fluid cleaves proNGF (pro-nerve growth factor) in ovarian follicle; both MMP7 and proNGF appear to be products of granulosa cells; processing of proNGF to NGF appears to regulate apoptosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26457789            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF promotes renal fibrosis via TGF-beta1-signaling activation, suggesting that in kidney diseases high NGF serum levels could contribute to worsen renal fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26066770            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study suggests that the circadian rhythm in the esophagus may be important for the mediation of and\/or the response to erosive damage in GERD patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26337663            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Intratumoral nerve growth factor expression is not associated with perineural invasion in patients with resected extrahepatic cholangiocarcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26547754            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF has a role in modulating trkANGFR\/p75NTR in alphaSMA-expressing conjunctival fibroblasts from human ocular cicatricial pemphigoid            \u003ca rel=\"nofollow\"\u003e             PMID:                        26569118            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF-induced tyrosine kinase independent TrkA signaling through CD44 is sufficient to maintain tumor aggressiveness in breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        25840418            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Urinary NGF, but not BDNF, levels decreased significantly after hyaluronic acid therapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24614892            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915099603169,"sku":"BL-1705NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYmAAMvJAAChZ5lbdyc990_c75d6eb2-746d-4e4e-9680-d17026bbf8dc.jpg?v=1685853222"},{"product_id":"recombinant-human-lif-protein-bl-1730np","title":"Recombinant Human LIF Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Leukemia Inhibitory Factor is produced by our E.coli expression system and the target gene encoding Ser23-Phe202 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP15018\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLeukemia Inhibitory Factor; LIF; Differentiation-Stimulating Factor; D Factor; Melanoma-Derived LPL Inhibitor; MLPLI; Emfilermin; LIF; HILDA\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLeukemia Inhibitory Factor (LIF) is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. LIF has a number of other activities including cholinergic neuron differentiation, control of stem cell pluripotency, bone and fat metabolism, mitogenesis of certain factor dependent cell lines and promotion of megakaryocyte production in vivo. Human and murine mature LIF exhibit a 78% sequence identity at the amino acid level. Human LIF is equally active on human and mouse cells. Murine LIF is approximately 1000 fold less active on human cells than human LIF.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e19.7 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e18 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLIF\/OSM family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            6596           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            159540           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:3976           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000249075           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29605252            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            The findings indicate that low LIF concentrations in serum and follicular fluid may contribute to disordered folliculogenesis in polycystic ovary syndrome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29397316            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study uses LIF to activate the PI3K\/ AKT signal and induce the anti-inflammatory effect during the neuron differentiation from human induced pluripotent stem cell-derived neural precursor cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29393372            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings implicate ZEB1 as a stem cell regulator in glioma via LIF repression which when deleted leads to increased stemness, tumorigenicity and shortened patient survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28246407            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Decreased serum LIF levels may be associated with vasculopathy in systemic sclerosis (SSc) and that Fli1 deficiency may contribute to the inhibition of LIF-dependent biological effects on SSc endothelial cells by suppressing the expression of LIF, LIF receptor, and gp130.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29038846            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The endometrial expression of LIF and CD34 in the pathogenesis of non-developing pregnancy can be used for evaluating the pregnancy prognosis in women of young and old reproductive age.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29063331            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This report describes the involvement of proteins responsible for cell growth and progression and defines the LIF-mediated novel autocrine-paracrine signaling loop for cell growth arrest.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28755912            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The expression of LIF was associated with tumor size and a poorer overall survival. Microarray and quantitative real-time polymerase chain reaction assessments suggest that LIF can facilitate tumor-promoting inflammation. Results indicate that LIF plays a role in maintaining cancer stem cells in chordomas.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28247842            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study indicated impaired LIF expression levels only in women with unexplained infertility, while LIF-R expression was impaired in all sub-groups of infertile women.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28432985            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings illustrate that DeltaNp63alpha can inhibit the levels of LIF mRNA by direct transcription regulation and decrease LIF mRNA stability by suppressing the expression of Lnc-LIF-AS. An inverse interaction of LIF and DeltaNp63alpha expression was as well validated in clinical samples of cervical cancer, and high level of LIF in cervical cancers was related with poor patient survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28391028            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ATF3 plays a significant role in regulating human endometrial receptivity and embryo attachment in vitro via up-regulation of leukemia inhibitory factor.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28577574            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Although further studies would be required to deconvolute the targets involved in LIF induction and to confirm activity of hits in more disease-relevant assays, our results have demonstrated the potential of the phenotypic approach to identify specific and chemically tractable small molecules that trigger the production of LIF in relevant cell lines            \u003ca rel=\"nofollow\"\u003e             PMID:                        26984928            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SNP 3951C\/T of LIF may not be associated with in vitro fertilization and embryo transfer outcome in Iranian population.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28466814            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In summary, this study has shown that LIF is implicated in the HG-mediated inhibition of osteoblast differentiation, via promoting STAT3\/SOCS3 signaling. This study may provide insights into the signal pathway of HG-induced bone loss or delayed injured joint healing.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28064096            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Cytokines of the LIF\/CNTF family and metabolism            \u003ca rel=\"nofollow\"\u003e             PMID:                        26817395            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results demonstrate the involvement of PIM kinases in LIF-induced regulation in different trophoblastic cell lines which may indicate similar functions in primary cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28729093            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest a 216-nucleotide proximal cis-element in LIF mRNA exhibits mRNA destabilizing potential; on exposure to carcinogen PMA (phorbol-12-myristate-13-acetate), this cis-element exhibits mRNA stabilizing activity. PMA induces nucleo-cytoplasmic translocation of both nucleolin and PCBP1, 2 trans-acting factors that bind to and stabilize LIF mRNA. [LIF = leukemia inhibitory factor; PCBP1 = poly(rC) binding protein 1]            \u003ca rel=\"nofollow\"\u003e             PMID:                        28512205            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Leukemia inhibitory factor (LIF) - STAT3 transcription factor (STAT3) signaling pathway is systemically dysregulated in in the endometrium of patients with recurrent\/repeated implantation failure (RIFE).            \u003ca rel=\"nofollow\"\u003e             PMID:                        27304912            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Endometrial expression of LIF and LIFR is significantly reduced in the epithelial cells of infertile women.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27082016            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LIF SNP T\/G (rs929271) seems to be a susceptibility biomarker capable of predicting implantation efficiency and pregnancy outcomes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26615902            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Overexpression of LIF promotes Epithelial-mesenchymal transition and results in cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26716902            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This review discusses the role of LIF and the recent analysis of its action on the uterine LE in regulating endometrial receptivity and implantation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26817565            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Women with dormant genital tuberculosis were found to have decreased endometrial LIF-STAT3 signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26776907            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that leukemia inhibitory factor (LIF) signaling promote chemoresistance in cholangiocarcinoma by up-regulating myeloid cell factor-1 (Mcl-1) via phosphatidylinositol 3-kinase (PI3K)\/c-akt protein (AKT)-dependent pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26296968            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Despite common signal transduction mechanisms (JAK\/STAT, MAPK and PI3K) LIF can have paradoxically opposite effects in different cell types including stimulating or inhibiting each of cell proliferation, differentiation and survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26187859            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Taken together, we firstly demonstrate that LIF enhances the adhesion of trophoblastic cells to endometrial cells by up-regulating expression of integrin heterodimer alphaVbeta3 and alphaVbeta5.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26723254            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LIF has a role in negatively regulating tumour-suppressor p53 through Stat3\/ID1\/MDM2 in colorectal cancers            \u003ca rel=\"nofollow\"\u003e             PMID:                        25323535            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LIF\/p21 signaling cascade as a novel tumor suppressive-like pathway in melanoma, acting downstream of TGFbeta to regulate cell cycle arrest and cell death, further highlight new potential therapeutic strategies for the treatment of cutaneous melanoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        25885043            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LIF was frequently overexpressed in osteosarcoma, which could promote the growth and invasion through activating the STAT3 pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26271643            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LIF structure, signaling pathway, and primary roles in the development and function of an organism are reviewed--{REVIEW}            \u003ca rel=\"nofollow\"\u003e             PMID:                        25879318            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LIF downregulates the autoimmune response by enhancing Treg numbers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25514345            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LIF mediates fibroblast activation to promote invasive tumor microenvironment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24857661            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that NanoLuc-fusion strategy provided an efficient approach for preparation of recombinant leukemia inhibitory factor (LIF) protein            \u003ca rel=\"nofollow\"\u003e             PMID:                        25179300            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of LIF protects the lung from lung injury and enhanced pathology during respiratory syncytial virus infection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25277705            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studied the association of tubal pregnancy with leukemia inhibitory factor (LIF) and leukemia inhibitory factor receptor (LIFR) expression in oviduct tissues.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25790555            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            an essential function of Foxm1 in the LIF\/Stat3-mediated mESC self-renewal and the generation of iPSCs            \u003ca rel=\"nofollow\"\u003e             PMID:                        24743237            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that endogenous levels of Pkig reciprocally regulate osteoblast and adipocyte differentiation and that this reciprocal regulation is mediated in part by LIF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23963683            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            An increased mRNA expression of PROK1 and LIF could be one of the several abnormalities characterizing the endometrium in women recurrent pregnancy loss.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25128195            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Addition of leukemia inhibitory factor (LIF) neutralizing antibodies inhibited oligodendrocyte differentiation, indicating a crucial role of TNFR2-induced astrocyte derived LIF for oligodendrocyte maturation            \u003ca rel=\"nofollow\"\u003e             PMID:                        24310780            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data from 3-year-old girl and other reported cases support model in which abundance of LIF in B-cell acute lymphoblastic leukemia results in leukemic infiltration of central nervous system and development of Cushing syndrome. [CASE STUDY; REVIEW]            \u003ca rel=\"nofollow\"\u003e             PMID:                        23729555            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This mini review will summarize the findings that are related to LIF signaling and discuss the neuroprotective effects of LIF in different models.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24664722            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest LIF\/LIF receptor (alpha subunit) signal transduction facilitates blastocyst implantation or development of tubal pregnancy by stimulating blastocyst adhesion and outgrowth\/proliferation of placenta or Fallopian tube epithelial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24074901            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Polyethylene glycated leukemia inhibitory factor antagonist inhibits human blastocyst implantation and triggers apoptosis by down-regulating embryonic AKT1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23876532            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NPC patients had increased serum levels of LIF. Higher LIF levels correlated with local tumor recurrence. Xenograft mouse studies showed that LIF critically contributes to NPC tumor growth \u0026amp; radioresistance.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24270418            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study found lower expression of LIF in the edndometrium in unexplained infertile women with multiple implantation failures compared to fertile women; data suggest that the initial lower expression of LIF in proliferative phase may be one of the causes for multiple failure of implantation            \u003ca rel=\"nofollow\"\u003e             PMID:                        23541977            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            novel expression and purification protocol for the production of recombinant hLIF            \u003ca rel=\"nofollow\"\u003e             PMID:                        23628981            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In summary, we can show that LIF is an important factor in melanoma progression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23831429            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that the expressions of ER-alpha, PR, LIF, VEGF, iNOS and CB1 in fallopian tube and chorionic villi of tubal pregnancy were not altered by exposure to levonorgestrel emergency contraception.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23687977            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LIF is a contraction-induced myokine, potentially acting in an autocrine or paracrine fashion to promote skeletal muscle satellite cell proliferation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21527666            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            No correlation was found between pinopodes development stage and LIF expressions in endometrium.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22252755            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915098095841,"sku":"BL-1730NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLRGAGkmDAAChKRsmdis654_6ddc93bb-cea2-4b56-9e2e-af4722ed7a81.jpg?v=1685853164"},{"product_id":"recombinant-human-mouse-rat-bmp2-protein-bl-1735np","title":"Recombinant Human\/Mouse\/Rat BMP-2 Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human\/Mouse\/Rat Bone Morphogenetic Protein 2 is produced by our E.coli expression system and the target gene encoding Gln283-Arg396 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP12643\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBone Morphogenetic Protein 2; BMP-2; Bone Morphogenetic Protein 2A; BMP-2A; BMP2; BMP2A\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBone Morphogenetic Protein-2 (BMP-2) is one of the bone-growth regulatory factors that belong to the transforming growth factor-beta (TGF-beta) superfamily of proteins. BMPs are synthesized as large precursor molecules, which are cleaved by proteolytic enzymes. The active form of BMP-2 can consist of a dimer of two identical proteins or a heterodimer of two related bone morphogenetic proteins.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13.3 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 10mM HAc-NH4Ac, 4% D-Mannitol, pH 4.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in 50mM Acetic Acid.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGrowth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cardiogenesis, neurogenesis, and osteogenesis. Induces cartilage and bone formation. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1\/5\/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical pathways such as ERK\/MAP kinase signaling cascade that regulates osteoblast differentiation. Stimulates also the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A-ATF4 pathway by stimulating EIF2A phosphorylation which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            1069           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            112261           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:650           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000368104           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29386057            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            This work indicates that NELL-1, HMGB1, and CCN2 might enhance bone defect healing via the recruitment of endogenous cells and induction of vascularization and act via different processes than BMP2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28463604            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum BMP2 and Smad4 levels in patients with senile osteoporotic fracture were significantly lower than those in normal controls            \u003ca rel=\"nofollow\"\u003e             PMID:                        29938690            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            conclude that SUMO3-tagged hBMP2 is more suited for generation of soluble form of the protein and addition of SUMO3 tag does not affect the functional activity of hBMP2            \u003ca rel=\"nofollow\"\u003e             PMID:                        29574511            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study identified a change in miR-22, miR-140, and BMP-2 expression in the synovial fluid of patients with osteoarthritis before and after arthroscopic debridement.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29429984            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The study revealed an enhanced sensitivity of aortic valve interstitial cells to osteogenic inductors in aortic stenosis patients, which indicates probable implication of OPN, OPG, and BMP2 genes in pathogenesis of aortic valve calcification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29308559            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The rhBMP2 monomer and dimer were eluted at 0.9 M and 0.6 M NaCl, respectively. The alkaline phosphatase assay of rhBMP2 (0, 50, 100, 200, and 400 ng\/ml) was analyzed on C2C12 cells and maximum 200 ng\/ml activity was observed in dose dependent manner            \u003ca rel=\"nofollow\"\u003e             PMID:                        29333457            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In contrast to BMP-2, BMP-7 concomitantly inhibited the expression of profibrotic genes            \u003ca rel=\"nofollow\"\u003e             PMID:                        28102712            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The binding free energies indicate that ALK-3 preferably binds to BMP-2 instead of BMP-9. The structural analysis shows that ALK-3 binding with BMP-2 occurs in a perfectly symmetry pathway, whereas this symmetry is lost for possible ALK-3 interactions with BMP-9            \u003ca rel=\"nofollow\"\u003e             PMID:                        28869862            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results demonstrate the efficacy of HPP-GC hydrogel in minimizing the diffusive loss of rhBMP-2 from the implantation site, compared to the collagen hydroxyapatite scaffold.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28847606            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The in vitro results suggest that altered BMP2 regulatory function at rs1884302 may contribute to the etiology of sagittal nonsyndromic craniosynostosis. The in vivo results indicate that differences in regulatory activity depend on the presence of a C or T allele at rs1884302.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28985029            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Collectively, according to our study, rhIL-6 could induce the extracellular calcification and osteogenic differentiation of human artery smooth muscle cells through upregulating endogenous BMP2 in vitro. This may be one of the underlying mechanisms of the overwhelming vascular calcification in rheumartoid arthritis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28134597            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HUCB-MSC transfected with mTAT\/PEI were shown to express more BMP-2 protein and mRNA.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28951869            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results showed that BMP2 activated SMAD1\/5\/8 phosphorylation and up-regulated BAMBI mRNA in human granulosa-lutein cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28578012            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BMP-2 can enhance HUVEC proliferation, migration and angiogenesis through P38, ERK and Akt\/m-TOR pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27886213            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study shows that recombinant human bone morphogenetic protein-2 activates hippo signaling through RASSF1 in esophageal cancer cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27230238            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SNPs in BMP2 can predict grade \u0026gt;\/= 2 or 3 RP after radiotherapy for NSCLC and improve the predictive power of MLD model.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28574846            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CTGF and BMP2 are induced following myocardial ischemia in mice and humans.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28460577            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Missense mutations in COL6A1, COL11A2, FGFR1, and BMP2 genetically predispose patients to ossification of posterior longitudinal ligaments.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27246988            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Computational analysis on conformational dynamics of BMP-2 has been presented.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27426435            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            there was a significant association in men between BMP2 genetic variant (rs235756) and hypertension in the genetically homogeneous Finnish population; no significant association between BMP2 rs235768 (A\u0026gt;T) and hypertension was found            \u003ca rel=\"nofollow\"\u003e             PMID:                        29390526            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Adding NMP as an adjunct to rhBMP-2-coated BCP produced inconsistent effects on bone regeneration, resulting in no significant benefit compared to controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28680881            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            observations regarding the dysregulation of these gatekeepers of neuronal viability may have important implications in understanding the iAbeta1-42 mediated effects observed in AD            \u003ca rel=\"nofollow\"\u003e             PMID:                        29470488            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrates that viscous collagen gel can be an effective carrier for rhBMP-2 delivery into surgical sites, and that the injectable rhBMP-2-containing collagen gel may be applied for the enhancement of tendon-bone interface healing            \u003ca rel=\"nofollow\"\u003e             PMID:                        26177709            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Synergistic effects of BMP-2, BMP-6 or BMP-7 with human plasma fibronectin onto hydroxyapatite coatings.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28434979            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High-dose recombinant human bone morphogenetic protein-2 impacts histological and biomechanical properties of a cervical spine fusion segment: results from a sheep model.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26053675            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Report osteoblast-like transformation of epithelial breast cancer cells that have undergone epithelial-mesenchymal transition followed by bone morphogenetic protein-2 stimulation. RUNX2 functions as a master mediator of this process.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27806311            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Taken together, our results suggest that DHCA may be developed as an efficient therapeutic for osteoporosis by regulating osteoblastogenesis through its estrogenic effects.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29253565            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BMP2-transduced BMSCs can maintain the chondrocyte-like phenotype in PRP gel in vitro, and the combined use of these two agents can significantly promote repair of the degenerated discs in vivo            \u003ca rel=\"nofollow\"\u003e             PMID:                        26169838            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these results suggest that the BMP2 gene polymorphism may be related to the development of allograft rejection and graft dysfunction in kidney transplant recipients            \u003ca rel=\"nofollow\"\u003e             PMID:                        28583517            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that the GREMLIN 2 (GREM2) expression during Induced Pluripotent Stem Cell (hiPS) cell cardiac differentiation follows the expression pattern of cardiac-specific genes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28125926            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results identify a novel 4671-bp tandem duplication downstream of BMP2, which is associated with brachydactyly type A2 . The duplication highly overlaps the sequences reported previously but has a different breakpoint and a different flanking microhomology.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29129813            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-106b inhibited osteoblastic differentiation and bone formation partly through directly targeting bone morphogenetic protein 2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28108317            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BMP2 decreases gap junction intercellular communication of luteinized human granulosa cells by downregulating Cx43 expression through an ALK2\/ALK3-mediated SMAD-dependent signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27986931            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BMP2 also requires Src for filamentous actin polymerization in Tgfbr3(-\/-) epicardial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26645362            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The deletion contained 17 protein coding genes including PROKR2 and BMP2, both of which are expressed during embryological development of the pituitary gland. PROKR2 mutations have been associated with hypopituitarism but a heterozygous deletion of this gene with hypopituitarism is a novel observation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28586151            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            both bone morphogenetic protein 2 (BMP2) and BMP6 are proangiogenic in vitro and ex vivo and that the BMP type I receptors, activin receptor-like kinase 3 (ALK3) and ALK2, play crucial and distinct roles in this process.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28733457            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            sequential presentation of PDGF to BMP-2 led to increased tubule formation over simultaneous delivery of these growth factors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27650131            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Bone Morphogenetic Protein-2, But Not Mesenchymal Stromal Cells, Exert Regenerative Effects on Canine and Human Nucleus Pulposus Cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27829314            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The structure of Grem2-GDF5 complex has revealed a number of key findings for DAN-family mediated BMP2 inhibition.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27524626            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Bioluminescence imaging reveals increased MSC survival when implanted in BMP-2 PAHs.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27581621            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Bone morphogenetic protein 2 promotes osteogenesis of bone marrow stromal cells in type 2 diabetic rats via the Wnt signaling pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        27702654            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            monocytes interact specifically with Chitosan-Fibrinogen (Ch-Fg) via TLR-4, triggering particular intracellular signalling pathways (ERK and JNK, but not p38), downstream of TLR-4. Functionally, Ch-Fg induced monocytes to produce the osteogenic mediator BMP-2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27856281            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study showed that si-Grem2 increased the BMP-2-induced osteogenic differentiation of hBMSCs via the BMP-2\/Smad\/Runx2 pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27335248            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Low doses of IL1B activate the BMP\/Smad signaling pathway to promote the osteogenesis of periodontal ligament stem cells, but higher doses of IL1B inhibit BMP\/Smad signaling through the activation of NF-kappaB and MAPK signaling, inhibiting osteogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27415426            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Increased miR-93-5p in trauma-induced osteonecrosis of the femoral head patients inhibited osteogenic differentiation, which may be associated with BMP-2 reduction.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28797104            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RANKL promotes VC by inducing BMP-2 release from HAECs            \u003ca rel=\"nofollow\"\u003e             PMID:                        27339040            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            KDM5A-mediated H3K4me3 modification participated in the etiology of osteoporosis and may provide new strategies to improve the clinical efficacy of BMP2 in osteoporotic conditions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27512956            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            fabricated scaffolds were well coated with DOPA as well as grafted with rhBMP2 at a quantity of 22.7+\/-5ng when treatment with 100ng\/ml rhBMP2 and 153.3+\/-2.4ng when treated with 500ng\/ml rhBMP2. This grafting enables rhBMP2 to be released in a sustained pattern.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26868173            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest pituitary cells secrete factor (TSP1) that binds to and inhibits action of BMP2 and BMP4; von Willebrand type C domain of TSP1 is likely responsible for this BMP2\/4-binding activity. These studies were initially conducted using cultured cells from ovine pituitary gland and mouse cell line; interactions were confirmed using recombinant human proteins. (TSP1 = thrombospondin-1; BMP = bone morphogenetic protein)            \u003ca rel=\"nofollow\"\u003e             PMID:                        28747434            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915097473249,"sku":"BL-1735NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLRCALMHuAACU0OpiwKU856_6860bfbb-e830-4f52-816d-7e158765249a.jpg?v=1685853139"},{"product_id":"recombinant-human-fibronectin-protein-bl-1736np","title":"Recombinant Human NovoNectin Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Fibronectin Fragment is produced by our E.coli expression system and the target gene encoding Pro1270-Ser1546\u0026amp;Ala1721-Thr2016 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP02751\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNovoNectin; Fibronectin; FN; Cold-insoluble globulin; CIG; FN; Fibronectin 1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFibronectin1(FN1) is a secreted protein and contains 12 fibronectin type-I domains,fibronectin type-II domains and 16 fibronectin type-III domains.Recombinant human fibronectin fragment, is a protein of ~63 kDa containing a central cell-binding domain, a high affinity heparin-binding domain II,and CS1 site within the alternatively spliced III CS region of human fibronectin. Cells bind to a VLA-4 ligand, a CS-I site, and a VLA-5 ligand, a cell attachment domain, and virus vectors binds to a heparin binding domain II, which co-locates the cell and the virus vector on NovoNectin. This process enhances the density of both cells and vectors, and facilitates the gene transduction in the result.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e62.7 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e60-80 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 12.5 mM Citric acid, 1.25% Sucrose, 0.1% Tween80, pH 5.5 .\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBiologically active. Please contact us to obtain bioactivity data.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.; Binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted, extracellular space, extracellular matrix.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            3778           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            135600           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:2335           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30237127            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Depletion of FN1 by siRNA knockdown markedly reduced the invasive capacity of prostate cancer cells in vitro.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29391407            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Human IL-7 binds more strongly to stretched than to relaxed Fibronectin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28845674            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGFB1-mediated PI3K\/Akt and p38 MAP kinase dependent alternative splicing of fibronectin extra domain A in human podocyte culture has been reported.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29729706            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings of this study provide evidence highlighting the prominent role played by FN1 in stimulating glioma growth, invasion, and survival through the activation of the PI3K\/AKT signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30048971            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The simultaneous delivery of multiple proinflammatory payloads to the cancer site conferred protective immunity against subsequent tumor challenges. A fully human homolog of IL2-F8-TNF(mut), which retained selectivity similar to its murine counterpart when tested on human material, may open new clinical applications for the immunotherapy of cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28716814            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Under the same condition, p53 protein expression, but not mRNA expression, was reversed by MG132. Taken together, our data demonstrate that the level of FN expression is associated with the status and expression of p53 in breast cancer cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        28765903            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our study thus demonstrates the dual roles of PTHrP on TGF-b1 signaling and FN up-regulation for the first time in glomerular mesangial cells . These data also provided new insights to guide development of therapy for diabetic kidney disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        28954822            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data suggest that miR-200b regulates EMT of chemo-resistant breast cancer cells by targeting FN1. miR-200b-based therapy may be an effective strategy in treating advanced breast cancer patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28972876            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Identification of novel integrin-binding domain mutations in FN1 in patients with glomerulopathy with fibronectin deposits.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27056061            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fibronectin fragments (FNFr) function as matrikines driving the chemotactic affinity of prostate cancer cells via the alpha5beta1 integrin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27715399            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fn with its inactive compact structure requires unfolding to assemble into active fibrils. Shear stress could induce conformational changes of plasma Fn.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29470988            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            B. burgdorferi does not primarily target insoluble matrix Fn deposited on endothelial surfaces but, instead, recruits and induces polymerization of soluble plasma Fn (pFn), an abundant protein in blood plasma that is normally soluble and nonadhesive.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28396443            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR1271 inhibited glioma cell growth by targeting FN1, and a low level of miR1271 in glioma tumor tissues was associated with lower survival rates in patients with glioma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28535003            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There is a significant association between a positive fetal fibronectin result and underlying inflammatory pathology of the placenta, even more so than the recognized relationship with short cervical length.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28535404            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The article focuses on summarizing the many binding partners for fibronectin such as extracellular matrix proteins, growth factors, and synthetic binding partners with a particular interest in binding partners whose adhesiveness is impacted by the molecular conformation of the fibronectin fibers. (Review)            \u003ca rel=\"nofollow\"\u003e             PMID:                        27496349            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FN1 fibrils regulate TGFB1-induced epithelial-mesenchymal transition.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28109697            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Breast cancer cells alter the dynamics of stromal fibronectin-collagen interactions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27503584            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study suggested that high a1-antitrypsin (AAT)expression might be a negative prognostic marker for lung adenocarcinoma. AAT promoted lung adenocarcinoma metastasis, whose functional target may be fibronectin . Our findings provide new insight into the mechanisms of lung adenocarcinoma metastasis            \u003ca rel=\"nofollow\"\u003e             PMID:                        28440399            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show the expression of ED-B fibronectin was much higher in mesenchymal than prostate cancer cells even after the epithelial to mesenchymal transition. Epithelial to mesenchymal transition is a key step for tumor progression contributing to the metastatic spread. Therefore, circulating cancer cells could seed into the metastatic niche taking advantage from the ED-B fibronectin that secrete their own.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27902486            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Thrombomodulin (TM) promotes angiogenesis by enhancing cell adhesion, migration, and FAK activation through interaction with fibronectin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27602495            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            thyroid nodule stiffness is correlated with fibrosis and expression of Gal-3 and FN-1            \u003ca rel=\"nofollow\"\u003e             PMID:                        27809694            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EGF and TNFalpha cooperatively promoted the motility of HCC cells mainly through NF-kappaB\/p65 mediated synergistic induction of FN in vitro. These findings highlight the crosstalk between EGF and TNFalpha in promoting HCC, and provide potential targets for HCC prevention and treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28844984            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            analysis of FN in breast cancer reveals its role and diagnostic potential            \u003ca rel=\"nofollow\"\u003e             PMID:                        27250024            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RT-PCR together with Sanger sequencing verified the presence of the FN1-ALK fusion transcripts            \u003ca rel=\"nofollow\"\u003e             PMID:                        27469327            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fibronectin is readily modified by ONOOH at low (physiologically-relevant) molar ratios of oxidant to protein.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27396946            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The 45 kDa gelatin-binding domain of fibronectin is responsible for the binding to TGM2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27394141            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Proteomics study showed a strong association of FN1, A2M, C4BPA and CFB in molecular subtypes of breast cancer. The findings also revealed the altered level expressions of these selected proteins could classify BC subtypes through plasma and tissue based expression analysis            \u003ca rel=\"nofollow\"\u003e             PMID:                        27498393            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FN1\/CCL2 levels are elevated in the bronchoalveolar lavage fluid from pulmonary sarcoidosis patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27259755            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Cancer-associated fibroblasts organize the fibronectin matrix and promote directional prostate cancer cell migration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29021221            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FN1 mutations that cause defective fibronectin secretion are found in SMD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29100092            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FN1 overexpression is an important determinant of thyroid cancer aggressiveness.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27173027            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Thyroid hormone T3 induces fibronectin and HIF-1alpha synthesis via PI3K\/AKT signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28974422            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mutations in FN are associated with glomerulopathy, but when we studied mutant proteins, the single-nucleotide mutations had only minor effects on conformation and matrix assembly. The mutations may destabilize their FNIII domains or generate dimers of dimers by disulfide cross-linking.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28745050            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fibronectin and Hepatocyte Growth Factor were shown to be produced by lung fibroblasts and, furthermore, to enhance malignant pleural mesothelioma cell migration and invasion            \u003ca rel=\"nofollow\"\u003e             PMID:                        28476806            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study identifies four likely Tourette disorder risk genes with multiple de novo damaging variants in unrelated probands: WWC1 (WW and C2 domain containing 1), CELSR3 (Cadherin EGF LAG seven-pass G-type receptor 3), NIPBL (Nipped-B-like), and FN1 (fibronectin 1).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28472652            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            fibrillar fibronectin on this polymer, but not a globular conformation obtained on control polymers, promotes synergistic presentation of integrin-binding sites and bound bone morphogenetic protein 2 (BMP-2), which enhances mesenchymal stem cell osteogenesis in vitro and drives full regeneration of a nonhealing bone defect in vivo at low GF concentrations.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27574702            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fn plays a critical role in inflammasome-activated cells by amplifying caspase-1 activation and inducing inflammatory cell death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27870323            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            If the expression of Capon is decreased, myeloma cells are adhered to fibronectin or bone marrow stromal cells (bone marrow mesenchymal stem cells). In addition, the sensitivity of the cell line to chemotherapeutic agents was reduced after silencing Capon in the myeloma cell line which was adhered to bone marrow mesenchymal stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28671047            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Protease sensitivity resulting from mutations in the Fn-binding sequence could lead to degradation of type I collagen, early embryonic lethality            \u003ca rel=\"nofollow\"\u003e             PMID:                        27799304            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            C-terminal truncation of transglutaminase 2 (TG2) reduces binding to the small intestinal extracellular matrix (ECM) despite retained fibronectin (FN)-binding capacity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27685605            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            analysis of novel functions for two fibronectin isoforms and the mediating receptors in osteoblast differentiation            \u003ca rel=\"nofollow\"\u003e             PMID:                        28325836            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In vitro binding assays with purified components reveal that Tie-integrin recognition is direct, and further demonstrate that the receptor binding domain of the Tie2 ligand Ang-1, but not the receptor binding domain of Ang-2, can independently associate with a5b1 or aVb3. cooperative Tie\/integrin interactions selectively stimulate ERK\/MAPK signaling in the presence of both Ang-1 and fibronectin            \u003ca rel=\"nofollow\"\u003e             PMID:                        27695111            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results directly implicate the heparin-binding sequence of the first type III repeat of fibrillar fibronectin (FNIII1) in realignment of stress fibers in HUVECs and, importantly, show that the matricryptic heparin-binding RWRPK sequence located in FNIII1 is required for the response.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27521419            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGFbeta elevated the expression of CamK IIbeta and CamK IIdelta, while siRNA silencing of those two subtypes significantly reduced TGFbeta-mediated expression of collagen A1 and fibronectin 1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28130256            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings suggest that the up-regulated level of EDA+ FN is associated with liver damage in nonalcoholic fatty liver disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28397039            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In vitro binding studies support a previously unreported two-state \"catch-clamp\" mechanism of Fn binding by CshA, in which the disordered N-terminal domain of CshA acts to \"catch\" Fn, via formation of a rapidly assembled but also readily dissociable pre-complex, enabling its neighboring ligand binding domain to tightly clamp the two polypeptides together.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27920201            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data add new evidence that thermodynamic stability correlates primarily with unfolding rate rather than folding rate. The study also has implications for the question of whether opening of FNIII domains contributes to the stretching of fibronectin matrix fibrils.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27909052            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A positive fFN was associate with preterm birth \u0026lt;32 weeks (15.6% versus 4.2%, p = 0.043), \u0026lt;35 weeks (37.5% versus 11.1%, p = 0.002), \u0026lt;37 weeks (65.6% versus 20.8%, p \u0026lt; 0.001), and earlier gestational ages at delivery (35.2 +\/- 3.9 versus 37.4 +\/- 2.9, p = 0.001).            \u003ca rel=\"nofollow\"\u003e             PMID:                        26782923            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FN1 plays a role in the development of cisplatin resistance in non-small cell lung cancer (NSCLC), possibly by modulation of beta-catenin signaling through interaction with integrin-beta1 in NSCLC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27207836            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"Default Title","offer_id":42876480159969,"sku":"BL-1736NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYOAKuORAABjlnuZNDE057_e5059931-2af3-484d-85a6-2165a9cddbf8.jpg?v=1685853165"},{"product_id":"recombinant-human-tgfb2-protein-bl-1740np","title":"Recombinant Human TGF-beta 2 Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Transforming Growth Factor Beta 2 is produced by our Mammalian expression system and the target gene encoding Ala303-Ser414 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP61812\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTransforming growth factor beta-2; TGFB2; Polyergin; G-TSF; Glioblastoma-derived T-cell suppressor factor; Cetermin; BSC-1 cell growth inhibitor; TGF-beta-2\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTransforming growth factor beta-2 (TGF-β2)  is a secreted protein which belongs to the TGF-beta family. It is known as a cytokine that performs many cellular functions and has a vital role during embryonic development. The precursor is cleaved into mature TGF-beta-2 and LAP, which remains non-covalently linked to mature TGF-beta-2 rendering it inactive. It is an extracellular glycosylated protein. It is known to suppress the effects of interleukin dependent T-cell tumors. Defects in TGFB2 may be a cause of non-syndromic aortic disease (NSAD).\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e12.7 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e12 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 4mM HCl.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBiologically active. Please contact us to obtain bioactivity data.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTransforming growth factor beta-2 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively.; Required to maintain the Transforming growth factor beta-2 (TGF-beta-2) chain in a latent state during storage in extracellular matrix. Associates non-covalently with TGF-beta-2 and regulates its activation via interaction with 'milieu molecules', such as LTBP1 and LRRC32\/GARP, that control activation of TGF-beta-2.; Transforming growth factor beta-2: Multifunctional protein that regulates various processes such as angiogenesis and heart development. Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains remain non-covalently linked rendering TGF-beta-2 inactive during storage in extracellular matrix. At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1 and LRRC32\/GARP, that control activation of TGF-beta-2 and maintain it in a latent state during storage in extracellular milieus. Once activated following release of LAP, TGF-beta-2 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e[Latency-associated peptide]: Secreted, extracellular space, extracellular matrix.; [Transforming growth factor beta-2]: Secreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            11768           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            190220           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:7042           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30160133            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Importantly, high expression levels of HIF-1alpha\/TGF-beta2\/GLI2 correlated robustly with the patient relapse following chemotherapy, highlighting a potential biomarker and therapeutic target for chemoresistance in colorectal cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29891662            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these data suggest that miR-592 may exert it suppressive role in breast cancer, at least in part, by targeting TGFbeta-2, and that miR-592 may be a novel target for breast cancer treatment            \u003ca rel=\"nofollow\"\u003e             PMID:                        29039599            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MicroRNA-486-5p suppresses TGFB2-induced proliferation, invasion and epithelial-mesenchymal transition of lens epithelial cells by targeting Smad2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29229876            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that TGF-beta2 is highly expressed in glioma and correlated with poor prognosis in glioma patients. Further findings elucidate a potential mechanism of autophagy-associated glioma invasion that TGF-beta2 could initiate autophagy via Smad and non-Smad pathway to promote glioma cells' invasion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29145888            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Up-regulation of TGF-beta2 showed a strong association with muscle invasion in bladder cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28261684            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Report early adaptive drug-escape in EGFR-mutant lung tumor cells dependent on TGFbeta2-bioenergetics-mitochondrial priming.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27852038            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The expression of TGFB2 obtained by microarray analysis was consistent with that of RT-PCR. Ion transport could be affected promptly after ANP treatment, and subsequently, the cytolysis of vein endothelial cells may be promoted and endothelial permeability would be enhanced, followed by activated immune responses.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29279524            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            4.7 Mb deletion encompassing TGFB2 is associated with features of Loeys-Dietz syndrome and osteoporosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28544325            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results imply that the interaction of matrix AGEs with RAGE plays a role in the TGFbeta2-mediated EMT of lens epithelial cells and suggest that the blockade of RAGE could be a strategy to prevent PCO and other age-associated fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27263094            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results support that the regulation of miR-30b by VEGF in HUVEC is important for capillary morphogenesis, as increased miR-30b expression inhibits capillary morphogenesis through enhanced expression of TGFbeta2            \u003ca rel=\"nofollow\"\u003e             PMID:                        28977001            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that TGFB2 (the most abundant growth factor in human milk) binding to Tgfb2r elicits robust\/rapid response in small intestinal mucosal cells leading to stimulation of Egr1 transport to nucleus and cell differentiation; more than 15 Wnt signaling pathway genes have Egr1 binding sites\/response elements; Egr1 binds to Axin1 promoter and functionally activates gene expression. (Axin1 = axis inhibition protein 1)            \u003ca rel=\"nofollow\"\u003e             PMID:                        27697743            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RUNX1T1 serves as a common angiogenic driver for vaculogenesis and functionality of endothelial lineage cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        28640846            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High TGFbeta2 expression is associated with oral cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27803052            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGF-beta2 is a new regulatory factor for KCC2 functional activation and membrane trafficking.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27505893            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our data expand the phenotype of Loeys-Dietz syndrome type 4 : we confirm that TGFb2 mutations are responsible for true Loeys-Dietz (LDS) syndrome with non-specific features of connective tissue disorders and diffuse vascular lesions            \u003ca rel=\"nofollow\"\u003e             PMID:                        27440102            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGF-beta signaling regulated cell growth of cancer associated fibroblasts.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27880067            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Localized constitutive expression and release of TGF-beta2 by TM cells may promote or exacerbate elevation of IOP in POAG.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26743044            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Advanced glycation endproduct in the lens capsule promote the TGFbeta2-mediated fibrosis of lens epithelial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26853893            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our study suggests that lnc-ATB promotes tumor progression by interacting with miR-141-3p and that Lnc-ATB may be a valuable prognostic predictor for GC. In conclusion, the positive feedback loop of lnc-ATB\/miR-141-3p\/TGF-beta2 may be a potential therapeutic target for the treatment of GC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28115163            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            decorin can alter the bioactivity of TGF-beta2 on human myoblast migration            \u003ca rel=\"nofollow\"\u003e             PMID:                        27644884            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings indicate that lncRNA-ATB governs the autocrine secretion of TGF-beta2 in KFs, at least in part, by downregulating the expression level of ZNF217 via miR-200c, suggesting a signaling axis consisting of lncRNA-ATB\/miR-200c\/ZNF217\/TGF-beta2            \u003ca rel=\"nofollow\"\u003e             PMID:                        27090737            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            association between SNP rs6658835 in TGF-beta2 and conotruncal heart defects            \u003ca rel=\"nofollow\"\u003e             PMID:                        27564654            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-422a directly targeted TGFbeta2 and regulated its expression and the activation of downstream molecules, smad2 and smad3 in osteosarcoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27779704            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-378a expression is associated with its methylation status in TGF-beta1-treated cells, and epigenetically-regulated miR-378a inhibits TGF-beta1-induced hepatic stellate cells activation, at least in part, via TGF-beta2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27855367            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we detected and verified a list of differentially expressed microRNAs in PE placentas by HTS and qRT-PCR, and provided preliminary evidence for the role of miR-193b-3p in the pathogenesis of preeclampsia by targeting TGF-beta2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26822621            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Likely pathogenic variants included a TGFB2 variant in one patient and a SMAD3 variant in another. These variants have been reported previously in individuals with similar phenotypes. Variants of uncertain significance of particular interest included novel variants in MYLK and MFAP5, which were identified in a third patient            \u003ca rel=\"nofollow\"\u003e             PMID:                        26854089            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results provide evidence that miR-148a decreases the expression of TGFbeta2 and SMAD2 in gastric cancer cells through binding to their 3'UTRs.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26983401            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGF-beta2 induces epithelial-mesenchymal transition by activating the PI3K\/Akt\/mTOR signaling pathway in cultured human lens epithelial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26647778            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Human retinal pigment epithelial cells were cultured in the presence or absence of TGF-beta2, and reverse-transcription quantitative PCR was performed to determine the mRNA expression of IDO and Nrf2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26676103            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGF-beta2 induces Grb2 to recruit PI3-K to TGF-RII that activates JNK\/AP-1-signaling and augments invasiveness of Theileria-transformed macrophages.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26511382            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In conclusion, each of the DPP-4 inhibitors may have unique drug-specific effects.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26826382            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Active CREB1 promotes a malignant TGFbeta2 autocrine loop in glioblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25084773            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Comparison of the aqueous humor TGF-beta2 level between patients with open-angle glaucoma (OAG) and controls provides direct evidence for the role of TGF-beta2 in the etiology of OAG. (meta-analysis)            \u003ca rel=\"nofollow\"\u003e             PMID:                        26019480            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            there is a borderline significant association between higher mean TGF-beta2 levels in breast milk and more severe pathologic diagnoses            \u003ca rel=\"nofollow\"\u003e             PMID:                        25604865            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results suggest that miR-200a suppresses RCC development via directly targeting TGFB2, indicating that miR-200a may present a novel target for diagnostic and therapeutic strategies in renal cell carcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        25813153            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGFbeta2 is a key growth promoter of CD44(hi) cells that survived chemotherapy and also is a growth inhibitor of cells that survived hypoxia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26340918            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MicroRNA-153 inhibits osteosarcoma cells proliferation and invasion by targeting TGF-beta2            \u003ca rel=\"nofollow\"\u003e             PMID:                        25793604            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression of TGFB2 is associated with melanoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25743834            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that the intrinsic transforming growth factor beta 2-triggered stromal cell-derived factor-1-C-X-C chemokine receptor-4 signaling is crucial for drug resistance in bone marrow (BM)-slow-cycling disseminated tumor cells (DTCs).            \u003ca rel=\"nofollow\"\u003e             PMID:                        25504440            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Here, we show that increased TGF-beta2 signaling through ALK5 plays a role in hypoxia-induced redifferentiation of chondrocytes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25621374            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGF-beta2 secretion from retinal pigmented epithelium decreases with polarization and becomes apically oriented            \u003ca rel=\"nofollow\"\u003e             PMID:                        25496702            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            glycated collagen in the cardiac interstitium triggers an autocrine TGF-beta2 signaling pathway that stimulates alpha11 integrin expression through Smad2\/3 binding elements in the alpha11 integrin promoter            \u003ca rel=\"nofollow\"\u003e             PMID:                        24962729            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these results revealed no correlation between the normalized expression of TGF-beta2, TGF-betaRI, or TGF-betaRII and EDSS scores            \u003ca rel=\"nofollow\"\u003e             PMID:                        26037400            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these data shed light on previously unrecognized roles of Mkx in tendinopathy, tenogenesis, and tendon repair as well as in regulating the TGFbeta pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25332192            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High levels of furin, TNF-alpha and TGF-beta2 may be the reason of proceeding decidualization, placentation, and prevention from abortion, in spite of terminating the fetal life.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26065233            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGF-beta2 therefore promotes the adhesion and invasiveness of virulent macrophages by modulating COX2, EP4, and PKIG transcription to initiate a prostaglandin E2 (PGE2)-driven autostimulatory loop that augments PKA and EPAC activities.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25690101            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGF-beta2 induced MYOC expression and secretion in human primary cultured trabecular meshwork cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        25197353            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that TGF-beta2 (TGFB2) and TGF beta type III receptor (TGFBR3) are target genes of miR-193b in chondrogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25728278            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ALDH1 and TGFbeta2 play important roles in the development of breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25120797            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915097440481,"sku":"BL-1740NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/rB9Eh2Pczt-AJgsjAACwWolseRo109_7227e88a-58c6-4379-82e9-8302329bcede.jpg?v=1685853138"},{"product_id":"recombinant-human-pro-bdnf-protein-bl-1757np","title":"Recombinant Human pro-BDNF Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Pro-Brain-Derived Neurotrophic Factor is produced by our E.coli expression system and the target gene encoding Ala19-Arg247(R125A,R127A,R128A) is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP23560\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBrain-Derived Neurotrophic Factor; BDNF; Abrineurin\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe precursor form of Brain-Derived Neurotrophic Factor (pro-BDNF) interacts preferentially with the pan-neurotrophin receptor p75 (p75NTR) and vps10p domain-containing receptor sortilin and induces neuronal apoptosis, whereas mature BDNF selectively binds with high affinity to the TrkB kinase receptor and promotes the survival, growth and differentiation of neurons. As proneurotrophins and mature neurotrophins elicit opposite biological effects, Pro-BDNF cleavage in the neuronal system is regulated in a specific and cell-context dependent manner. Pro-BDNF plays important role in negative regulation of neurotrophic actions in the brain.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e25.6 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e28 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eImportant signaling molecule that activates signaling cascades downstream of NTRK2. During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.; Important signaling molecule that activates signaling cascades downstream of NTRK2. Activates signaling cascades via the heterodimeric receptor formed by NGFR and SORCS2. Signaling via NGFR and SORCS2 plays a role in synaptic plasticity and long-term depression (LTD). Binding to NGFR and SORCS2 promotes neuronal apoptosis. Promotes neuronal growth cone collapse.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.; [BDNF precursor form]: Secreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            1033           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            113505           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:627           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000414303           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29734216            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Low brain derived neurotrophic factor may contribute to the pathogenesis of schizophrenia, but maybe not to its cognitive impairments.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29482040            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In a 12-year longitudinal population-based sample of older adults (n = 2,218), we used growth curve modeling to investigate whether the benefits of physical activity on cognitive preservation differed by BDNF genotype and sex across multiple cognitive domains including processing speed, attention, working memory, and episodic verbal memory.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29402782            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mn-SOD V allele carries a worse outcome profile after stroke, relating to nitrosative stress, inflammatory, and apoptotic response and associated with a BDNF reduction.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30150066            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            while the BDNF Val66Met Megroup displayed significant SICI reduction in the bilateral M1 in response to motor training, short-interval intracortical inhibition (SICI) remained unchanged in the BDNF Val66Met group.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29856758            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our study provides evidence for the correlation between the BDNF variant rs6265 and emotional symptoms in the early phase after mild traumatic brain injury.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29357818            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results indicate that genetic variant Met66 decreased the serum BDNF levels in combination with self-reported risk-taking propensity among heroin users.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30134233            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            serum BDNF levels and the BDNF Val66Met polymorphism in healthy young adults were associated with the sleep pattern on weekends but not with that on weekdays, suggesting that the systems involved in BDNF control may be linked to endogenous sleep characteristics rather than the socially constrained sleep schedule in healthy young adults.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29944703            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Neurotrophic factors and hippocampal activity in PTSD            \u003ca rel=\"nofollow\"\u003e             PMID:                        29799860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            upregulation of PAI-1 may be a critical mechanism underlying insufficient neurotrophic support and increased neurodegeneration associated with AD. Thus, targeting BDNF maturation through pharmacological inhibition of PAI-1 might become a potential treatment for AD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28132883            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study shows the genetic correlates of early trauma in a group of schizophrenia patients (BDNF Met carriers).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28711474            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrated significant differences in the blood levels of BDNF between people with epilepsy and healthy subjects.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30140987            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study shows that brain-derived neurotrophic factor concentrations in serum and peritoneal fluid were significantly higher in women with endometriosis with pain compared to women with endometriosis without pain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28954602            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Met allele of the Val66Met polymorphism in brain derived neurotrophic factor is associated with lower BMI-SDS in children            \u003ca rel=\"nofollow\"\u003e             PMID:                        28960774            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            platelet BDNF and SERT do not specifically underlie psychosocial deficits in stage Huntington's Disease, while higher BDNF storage in delayed mild symptoms            \u003ca rel=\"nofollow\"\u003e             PMID:                        30039833            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Direct within family analysis showed that fathers with the Met allele were more likely than Val\/Val carriers to exhibit differential parenting toward twins who differed in their prosocial behavior. The same pattern of findings was found with mother-rated and experimentally assessed prosociality.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28523227            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study suggest that the Val66Met polymorphism does not predict long-term, functional mobility following stroke.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29480080            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            polymorphisms in BDNF gene including rs925946, rs10501087, rs6265 and rs988712 can be considered as genetic determinants of obesity (systematic review and meta-analysis).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28818748            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Single nucleotide polymorphism found in the BDNF-AS (BDNF antisense RNA [nonprotein coding]) gene may be related to the decreased plasma brain derived neurotrophic factor levels found in frail elderly people.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27449141            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The pattern of low BDNF and high inflammation in MDD may be influenced by the Val66Met polymorphism; the association of a polymorphism in the BDNF gene with inflammatory markers in addition to BDNF levels suggests an interaction between these systems.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28656803            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Angiogenin contributes to angiogenesis induced by Brain-derived neurotrophic factor (BDNF).            \u003ca rel=\"nofollow\"\u003e             PMID:                        29573867            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings demonstrated that polymorphism Val66Met is not associated with temporal lobe epilepsy caused by hippocampal sclerosis, epilepsy-related factors and psychiatric comorbidities in this selected group of patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30015148            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study suggested that BDNF 196 G\u0026gt;A polymorphism may be a genetic marker for predicting insulin resistance before initiating risperidone treatment in autism spectrum disorder patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29369497            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            No significant difference was found in the BDNF Val66Met polymorphism between patients with GAD and healthy controls, nor was this polymorphism significantly associated with antidepressant drug efficacy for GAD            \u003ca rel=\"nofollow\"\u003e             PMID:                        29446659            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Its single-nucleotide polymorphisms involves in dopaminergic metabolism and motor and cognitive function in older adults.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29525179            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BDNF rs11030101 and BDNF rs61888800are associated with change of temperament scores in a clinical sample of subjects with major depression (MDD), who received selective serotonin reuptake inhibitor treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29310728            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We found that harsh parenting predicted an increased error-related negativity only among children with a methionine allele of the BDNF genotype, and evidence of moderated mediation: the ERN mediated the relationship between parenting and internalizing diagnoses and dimensional symptoms only if children had a methionine allele.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28427482            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings presented here suggest a strong influence of seasonality on depression outcome and BDNF expression in atopic dermatitis and psoriasis            \u003ca rel=\"nofollow\"\u003e             PMID:                        27409526            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum BDNF was significantly lower in patients with Parkinson's disease than in patients with essential tremor and controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29350074            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The purpose of this systematic review was to provide a comprehensive analysis of the available clinical trials analyzing, in seniors, the effect of interval aerobic training (IAT) and continuous aerobic training (CAT) on peripheral brain-derived neurotrophic factor (BDNF) concentration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28498065            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings suggested that BDNF modulates graunlosa cell functions and the action probably mediated by FSHR-coupled signaling pathway, to affect aromatase-mediated steroidogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28282971            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The functional Val66Met BDNF polymorphism is not associated with BDNF serum levels in acute episode of schizophrenia and depression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29331787            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrated that a significantly higher incidence of defective BDNF expression in granule layers of the cerebellar cortex.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29174061            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            combining cognitive and physical exercise had no additional or synergistic effect on peripheral BDNF levels compared with physical exercise alone            \u003ca rel=\"nofollow\"\u003e             PMID:                        29842831            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Review\/Meta-analysis: suggests a lower risk of ischemic stroke for the GG genotype of BDNF rs6265.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29449128            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            that the BDNF SNP rs1157659 interacted with mild traumatic brain injury to predict hippocampal volume            \u003ca rel=\"nofollow\"\u003e             PMID:                        28755387            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            found that though there was no significantly difference in peripheral BDNF levels between ADHD patients and control groups overall, BDNF levels were significantly higher in males with ADHD compared with controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29132072            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            found evidence that supported the hypothesis that BDNF Val66Met polymorphism moderated the relationship between stress and depression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29102837            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the BDNF Val66Met polymorphism is associated with functional tuning of behaviorally-relevant frontolimbic circuitry, particularly involving the ventromedial prefrontal cortex, during higher-order learning.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28867340            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MicroRNA-103 suppresses glioma cell proliferation and invasion by targeting BDNF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29257320            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression levels of BDNF was observed in cervical cancer.BDNF role in epithelial-mesenchymal transition, migration and invasion of cervical cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29345295            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There was a statistically significant change in BDNF levels post-chemotherapy in early-stage breast cancer patients, and plasma BDNF levels were associated with self-perceived concentration deficit in patients receiving chemotherapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29258453            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Meta-analysis\/Review: patients with ischemic stroke at high risk of post stroke depression have lower BDNF levels at the early stage of stroke.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29128330            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Coronary artery disease patients exhibited significantly lower plasma BDNF and higher vWF levels than those of control patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29409455            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Brain-derived neurotrophic factor (BDNF) was found to be the downstream target of miR-107 in breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27813254            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study showed that in first-episode psychosis subjects, with global DNA hypo-methylation and reduced BDNF gene-expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29056292            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            down-regulated in cord blood by prenatal smoking            \u003ca rel=\"nofollow\"\u003e             PMID:                        28130959            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BDNF\/TrkB axis plays a role in epithelial mesenchymal transition promoting the acquisition of (myo)fibroblast cell phenotype in idiopathic pulmonary fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28938915            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that Lnc RNA BDNF-AS inversely regulates the expression level of BDNF which modulates high-glucose induced apoptosis in human retinal pigment epithelial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28657668            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study show a linear relationship between the BDNF Val66Met genotypes and plasma BDNF levels in Caucasian depressed patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28848102            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915102191841,"sku":"BL-1757NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLSSAMkjEAACeKC8sE88607_11b1b137-980a-49b9-9911-7042dc5a5f25.jpg?v=1685853331"},{"product_id":"recombinant-human-nt-3-ntf3-protein-bl-1758np","title":"Recombinant Human NT-3 Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Neurotrophin-3 is produced by our E.coli expression system and the target gene encoding Tyr139-Thr257 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP20783\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNeurotrophin-3; NT-3; HDNF; Nerve Growth Factor 2; NGF-2; Neurotrophic Factor; NTF3\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNeurotrophin-3 (NT-3) is a member of the NGF family of neurotrophic factors and is structurally related to β-NGF, BDNF and NT-4. The NT3 cDNA encodes a 257 amino acid residue precursor protein with a signal peptide and a proprotein that are cleaved to yield the 119 amino acid residue mature NT3.The amino acid sequences of mature human, murine and rat NT-3 are identical. NT-3 selectively promotes the differentiation and survival of specific neuronal subpopulations in both the central as well as the peripheral nervous systems.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13.6 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e14 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 250mM NaCl, pH 7.2.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSeems to promote the survival of visceral and proprioceptive sensory neurons.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            8023           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            162660           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4908           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000397297           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29549646            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            brain-derived neurotrophic factor (BDNF) and neurotrophin 3 (NT3) levels in post-mortem brain tissue from patients with depression compared to healthy individuals - a proof of concept study            \u003ca rel=\"nofollow\"\u003e             PMID:                        29102768            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NT-3 has been shown to be both an osteogenic and angiogenic factor, and can also enhance expression of the key osteogenic factor, BMP-2, as well as the major angiogenic factor, VEGF, to promote bone formation, vascularization, and bone healing            \u003ca rel=\"nofollow\"\u003e             PMID:                        28370021            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression of NT-3 is associated with glioblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28402394            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Meta-analysis found the levels of both NT-3 and NT-4\/5 were significantly increased in bipolar disorder patients. Through subgroup analysis, this increase persisted only in patients in depressed state, but not in manic or euthymic state. In addition, we found the differences in NT-3 and NT-4\/5 were significantly associated with the duration of illness, but not by the mean age or female proportion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27214525            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NT3 upregulates cellular proliferation, extracellular matrix protein production, and collagen deposition in human aortic valve interstitial cells through the Trk-Akt-cyclin D1 cascade.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28356268            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The analysis of covariance (ANCOVA) indicated that the mean serum GDNF and NTF3 levels of ADHD patients were significantly higher than that of controls. However, serum BDNF and NGF levels did not show any significant differences between groups. These results suggest that elevated serum GDNF and NTF3 levels may be related to ADHD in children.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27561780            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There were no differences in neurotrophin levels between patients with schizophrenia and controls. We found lower BDNF and higher NT-3 serum levels in depressed patients with schizophrenia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26548545            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggest a gene dose-association between the A allele of rs6332 and the onset of AD in varepsilon4 non-carriers and the NTF-3 rs6489630 polymorphism being a relevant risk factor for AD in patients lacking the ApoE-varepsilon4 allele in this Chinese sample.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26814132            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Survival, differentiation, and neuroprotective mechanisms of human stem cells complexed with neurotrophin-3-releasing pharmacologically active microcarriers in an ex vivo model of Parkinson's disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25925835            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            No differences in plasma BDNF, NGF, NT3, NT4 and GDNF were found between autism spectrum disorders and control.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25275256            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NT-3 expression was found in axons of olfactory bulb.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24288162            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            genetic variation in the NTF3 gene is related to susceptibility to emotional side effects in response to methylphenidate treatment in Korean children with ADHD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23471121            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NT-3 appears to promote growth of metastatic breast cancer cells in the brain            \u003ca rel=\"nofollow\"\u003e             PMID:                        23001042            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NT-3 promoted motility, migration, invasion, soft-agar colony growth and cytoskeleton restructuring in TrkC-expressing U2OS cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        23027130            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There was no association between the presence of rs11063714 and curve progression in adolescent idiopathic scoliosis in a 2117-person Japanese cohort.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23038618            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results suggested that an NT-3 polymorphism, rs6332, may significantly influence executive function, reflecting interference performances among patients with mild-stage AD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23075484            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings suggest that NT-3, BDNF, LIF and their combinations predominantly support different ontogenetic events at different developmental stages in the innervation of the inner ear.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23149719            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we identify a TrkB ligand, neurotrophin 3 (NTF3), as capable of activating TrkB to induce anoikis resistance, and show that NTF3 is also a direct target of miR-200c            \u003ca rel=\"nofollow\"\u003e             PMID:                        23185507            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The specific aspects of proprioceptive sensory neuron subtype character is controlled by variation in the level of muscle NT-3 expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23522042            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NTF3 is transported from midbrain dopaminergic neurons and supports the survival of immature medium-sized spiny neurons.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23426664            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There is no significant difference in NGF, NT-3 and p75NTR expression in the myometrium or endometrium between the adenomyosis and the control group.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22454143            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            protein levels of translational, splicing, processing, chaperone, protein handling, and metabolism machineries were shown to depend on neurotrophin-3-induced TrkC activation in the medulloblastoma cell line DAOY            \u003ca rel=\"nofollow\"\u003e             PMID:                        18336001            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mice carrying one or two platelet-derived growth factor beta-NT3 transgenes on a background null for wildtype NT-3 are generated by crossing with an NT-3 null strain; although still ataxic, mice from this cross could survive for periods longer than a year.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21787840            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NTF3 gene polymorphisms are not associated with the occurrence of idiopathic scoliosis, but the promoter polymorphism (rs11063714) is associated with the curve severity, implicating an alleviating role of NTF3 in the curve progression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22158057            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Implantation of NT-3 gene-modified mesenchymal stem cells via a recombinant adenoviral vector into a demyelinated region of rat spinal cord results in significant improvement of locomotor function and electrophysiological restoration in rats.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21996274            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the study demonstrates for the first time that a neurotrophin factor can synergize with IGFBP-2 to promote hematopoietic cell expansion            \u003ca rel=\"nofollow\"\u003e             PMID:                        22459634            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            both apoptotic cell death and neuronal differentiation of tumor cells were the mechanisms of growth-inhibitory effect of NT-3-secreting human adipose tissue-derived mesenchymal stem cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        21720807            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Release of peripheral blood mononuclear cell-derived NT-3 correlates with its concentration in the brain-parenchymal fraction and corpus callosum cross-sectional area and may exert a direct or indirect neuroprotective effect in multiple sclerosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22036954            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings suggest that endogenous CNTF and exogenous BDNF and NT-3 play roles in the differentiation of embryonic spinal cord derived progenitor cells into astrocytes, neurons and oligodendrocytes, respectively            \u003ca rel=\"nofollow\"\u003e             PMID:                        21698095            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Collagen-binding neurotrophin-3 promotes axonal regeneration after spinal cord transection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20597688            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Co-culture of human neurotrophin-3 (NT-3) gene-modified Schwann cells (SCs) and human NT-3 receptor tyrosine protein kinase C (TrkC) gene-modified MSCs increase differentiation of neuron-like cells from mesenchymal stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19680743            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NT3 may be involved in early folliculogenesis, particularly in the activation of primordial follicles.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21392742            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results suggest that proneurotrophin-3 and proBDNF may play important roles in the response to noise-induced injuries or ototoxic damage via the Sortilin:p75(NTR) death-signalling complex.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21261755            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that serum NT-3 levels were similar in SSc and in the control group.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21085492            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            preliminary evidence of an association between NTF3 and the intelligence and selective attention deficit in the Korean population.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20576502            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study suggested that increased serum NT-3 levels in BD are likely to be associated with the pathophysiology of manic and depressive symptoms.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20060128            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Report the proangiogenic capacity of NT-3 and propose NT-3 as a novel potential agent for the treatment of ischemic disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20360537            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TrkC ligand neurotrophin-3 (NT-3) is upregulated in a large fraction of aggressive human neuroblastomas (NBs) and that it blocks TrkC-induced apoptosis of human NB cell lines, consistent with the idea that TrkC is a dependence receptor.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20160348            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF and NT-3 concentrations are increased in children with hydrocephalus.            \u003ca rel=\"nofollow\"\u003e             PMID:                        11580868            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Human eosinophils produce neurotrophin 3 on immunologic stimuli.            \u003ca rel=\"nofollow\"\u003e             PMID:                        11877300            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results suggest that the G(- 3004)-A3 haplotype has a modest effect of giving susceptibility to schizophrenia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        11920853            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NT3 is significantly decreased in the myenteric plexus of patients with active Crohn's disease and ulcerative colitis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        12598727            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fibroblasts genetically modified to express human neurotrophin-3 (NT-3) were placed in, and distal to, the lesion cavity in chronic spinal cord injured rats; grafted animals exhibited significant growth of corticospinal axons            \u003ca rel=\"nofollow\"\u003e             PMID:                        12710933            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Monocytes, produce, store and release nerve growth factor, brain-derived neurotrophic factor and NT-3            \u003ca rel=\"nofollow\"\u003e             PMID:                        15544837            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In transgenic mlc\/NT-3 mice following nerve injury, NT-3 plays an important role during the early stages of spindle denervation that ultimately effects reinnervation by group II and gamma fibers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        15589528            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Circulating neurotrophin-3 levels increased in early neonatal life, possibly due to exposure to various stimuli soon after birth            \u003ca rel=\"nofollow\"\u003e             PMID:                        15770067            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present data on neurotrophin-specific transcriptional down-regulation of NT3 in human Chronic obstructive pulmonary disease (COPD)indicate a pathophysiological role for neurotrophins in COPD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        15843147            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Human bronchial smooth muscle cells can express NGF, BDNF and NT-3. Expression may be differently regulated by inflammatory cytokines. Might have potential role in airway inflammation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16441896            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Light and electron microscopy immunohistochemistry showed that tonsillar samples were positive for NT3.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16786155            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915098882273,"sku":"BL-1758NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLSSAPu0XAACn6hsVMSg522_d4000aee-b239-418d-8ec7-c3b8eee51b3b.jpg?v=1685853192"},{"product_id":"recombinant-human-kgf-protein-bl-1760np","title":"Recombinant Human KGF Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Fibroblast Growth Factor 7\/Keratinocyte Growth Factor is produced by our E.coli expression system and the target gene encoding Cys32-Thr194 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP21781\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFibroblast growth factor 7; FGF-7; Heparin-binding growth factor 7; HBGF-7; Keratinocyte growth factor; FGF7; KGF\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFibroblast growth factor 7 (FGF7) is a secreted protein which is mainly located in epithelial cells and belongs to the heparin-binding growth factors family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. It is possible major paracrine effector of normal epithelial cell proliferation.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e18.9 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e17 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM Tris，1mM EDTA，5% Trehalose, 0.02% Tween 80, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by SEC-HPLC. (Regularly tested)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePlays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. Growth factor active on keratinocytes. Possible major paracrine effector of normal epithelial cell proliferation.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHeparin-binding growth factors family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            3685           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            148180           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:2252           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000267843           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29970688            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Findings suggest that excessive KGF and KGFR synthesis may contribute to the hyperproliferative state in cholesteatoma and could explain the pathological difference between cholesteatoma and CSOM.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29556625            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results suggest that fibroblast growth factor 7 may stimulate endometrial stromal cells proliferation and insulin-like growth factor-binding protein 1 and prolactin expressions through ERK and JNK signal pathways in an autocrine manner.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28270036            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The stability and activity of rhKGF mutants were analyzed using GROMACS molecular dynamics (MD) simulations and docking tools, respectively. The results showed that N159S (N105S in rhKGF sequence) and I172V (I118V in rhKGF) substitutions caused an increased stability and affinity of the rhKGF to Fibroblast growth factor receptor 2 (FGFR2).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28093295            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Tregs isolated from human lung tissue can be stimulated ex vivo to induce kgf expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28296468            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FGF7 stimulation of cell invasion and migration was partially suppressed by the FGFR2 knockdown. In addition, FGF7\/FGFR2 upregulated THBS1, and cell invasion and migration were decreased by knockdown of THBS1            \u003ca rel=\"nofollow\"\u003e             PMID:                        28339036            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Suppression of miR-219-5p may benefit the liver regeneration and prevent cirrhosis through increasing KGF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27855391            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study evaluated the expression of FGF7, AhR, and CYP1A1 in colorectal cancer cells and revealed a new mechanism by which KGF promotes cell proliferation through the AhR-cyclin D1 pathway in colon cancer cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26514676            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            KGF expression induced epithelial cell proliferation, reaching a peak level at day 4 and then decreased later, while in the long-term model, KGF expression in the EAC led to middle ear cholesteatoma formation            \u003ca rel=\"nofollow\"\u003e             PMID:                        25138153            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In the current study, conditioned media and chemically defined media with recombinant human keratinocyte growth factor (KGF) could induce hUC-MSC differentiation into sweat gland-like cells (SGCs).            \u003ca rel=\"nofollow\"\u003e             PMID:                        26574554            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Coexpression of KGF and MMP-9 in gastric cancer could be a useful prognostic factor, and MMP-9 might also serve as a novel target for both prognostic prediction and therapeutics.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26350198            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FGF7 over expression is associated with advanced clinical features in patients with upper tract and bladder urothelial carcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        25623741            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate the key roles played, on the melanosome transfer in normal skin, by KGF\/FGF7 released by dermal fibroblasts and by its receptor KGFR\/FGFR2b expressed and activated on the epidermal keratinocytes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25313018            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            First evidence of a role of FGF7 in the regulation of sequential steps of the autophagic process and strengthen the hypothesis of a direct interplay between autophagy and differentiation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24577098            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            An SNP in FGF7 is associated with an increased risk of chronic obstructive pulmonary disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22796760            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings indicate that topically delivered KGF-1 DNA plasmid can increase epithelial thickness and strength, demonstrating the potential of this approach to restore compromised skin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24434934            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Recombinant keratinocyte growth factor 1 in tobacco potentially promotes wound healing in diabetic rats.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24783215            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Sustained effect of KGF on cell survival and proliferation could be attributed to its ability to inhibit p53, retinoblastoma, caspases, and p27(kip) functions in apoptosis and cell cycle arrest.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24426773            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FGF7 stimulates osteogenic differentiation, but not proliferation, in embryonic stem cells, by activating ERK\/Runx2 signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24026476            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This paper provides an overview of the knowledge on molecular properties, biological functions and the ecent findings on clinical application of EGF7. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        24188496            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High FGF7 expression is associated with ameloblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24002438            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            IL-19 is important for cutaneous wound healing because it upregulates KGF expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23582717            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FGF7 supports hematopoietic stem and progenitor cells and leukemia-initiating cells indirectly via FGFR2IIIb expressed on stromal cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24051090            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The aim of this study was to determine whether the K-sam gene and keratinocyte growth factor (KGF) expression may be used to identify malignant tumors with a poor prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23545898            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            KGF could up-regulate IL-7 expression through the STAT1\/IRF-1, IRF-2 signaling pathway, which is a new insight in potential effects of KGF on the intestinal mucosal immune system.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23554911            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The LTA downstream segment alternate core promoter was active only after specific cellular stimulation and was the major promoter used when human T cells were stimulated with TGF-beta1 and fibroblast growth factor-7.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23547113            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Increased KGF expression promotes fibroblast activation in a double paracrine manner resulting in cutaneous fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23096718            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results implicate pericryptal myofibroblast-derived paracrine KGF and largely autocrine amphiregulin in the upregulation of claudin-2 in Caco-2 epithelial monolayers and consequent disruption of tight junction integrity            \u003ca rel=\"nofollow\"\u003e             PMID:                        22946653            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Keratinocyte growth factor up-regulates Interleukin-7 expression following intestinal ischemia\/reperfusion in vitro and in vivo.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22949940            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the activation of the stromal fibroblasts present in the pathological tissue, and the consequent increased secretion of KGF, play a crucial role in the deregulation of the epidermal proliferation and differentiation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22481617            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these data suggest that FGF7 is a novel regulator of CYP7A1 expression in hepatocytes and may prevent hepatocytes from accumulating toxic bile acids during liver injury and fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22713451            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Repression of Ink4a in aged (ETPs) Early T-cell progenitors results in their partial rejuvenation and this can be accomplished by in vivo fibroblast growth factor 7 administration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22555975            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In COPD, SNPs (rs12591300 and rs4480740) were significantly associated with COPD in an independent population (combined p values of 7.9E-7 and 2.8E-6). Increased lung tissue FGF7 expression was associated with worse measures of lung function.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21921092            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FGF7 enhanced keratinocyte proliferation and its expression was increased when NCTC 2544 cells were subjected to treatments with plantaricin A preparations or hyaluronic acid.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21782870            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Carcinoma-associated fibroblasts promotes the proliferation of a lingual carcinoma cell line by secreting keratinocyte growth factor.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21340484            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            KGF may have a role in ameliorating radiation-induced pulmonary injury in rats            \u003ca rel=\"nofollow\"\u003e             PMID:                        21436609            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results suggest that the growth factors HGF and KGF may play a role in enhancing IL-1-stimulated production of IL-8 by epithelial cells during mucosal inflammations.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21082280            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            KGF increases pigment production and deposition in melanocytes in vitro and in vivo            \u003ca rel=\"nofollow\"\u003e             PMID:                        19780816            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The upregulation of KGF\/KGFR might induce the formation of rete ridges and hyperpigmentation in solar lentigines.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20620021            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Modulation of calprotectin in human keratinocytes by keratinocyte growth factor and interleukin-1alpha.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20065999            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the expression of keratinocyte growth factor (KGF) and keratinocyte growth factor receptor (KGFR) in Hela cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        17593825            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            KGF and KGFR are both expressed in CaSki cells. Autocrine and recombinant human KGF affect cell proliferation and migration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17953372            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            keratinocyte growth factor works via an inducible lentivirus to protect bone marrow cells against bleomycin-induced pulmonary fibrosis            \u003ca rel=\"nofollow\"\u003e             PMID:                        19956603            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The goal of this study was to elucidate the control mechanisms by which exogenous proteins regulate keratinocyte growth factor (KGF) expression in fibroblasts adhered to differing substrates.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20036421            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The effect of KGF on limbal epithelial cell growth is mediated by upregulation of DeltaNp63alpha through the p38 pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19920075            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            KGF induced proliferation but did not cause significant differentiation of 3 hematopoietic cell lines and bone marrow cells transduced with human K-sam.            \u003ca rel=\"nofollow\"\u003e             PMID:                        11937263            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            play important roles in lung development, lung inflammation, and repair.            \u003ca rel=\"nofollow\"\u003e             PMID:                        11943656            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            keratinocyte growth factor (KGF), a key stimulator of epithelial cell proliferation during wound healing, preferentially binds to collagens I, III, and VI.            \u003ca rel=\"nofollow\"\u003e             PMID:                        11973338            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            KGF may hold promise for the treatment of very premature neonates with bronchopulmonary dysplasia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        12016100            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Following activation by KGF binding, KGF and the KGF receptor remain associated in active complexes through the endocytic pathway, which is described.            \u003ca rel=\"nofollow\"\u003e             PMID:                        12122441            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915097637089,"sku":"BL-1760NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYWAYrEfAADG8FUuZrA829_0b118559-7c4c-4847-8c40-d199de7f7f9f.jpg?v=1685853146"},{"product_id":"recombinant-mouse-shh-protein-bl-1763np","title":"Recombinant Mouse SHH Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Sonic Hedgehog is produced by our E.coli expression system and the target gene encoding Cys25-Gly198 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eQ62226\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSonic Hedgehog Protein; SHH; HHG-1; SHH\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMouse Sonic Hedgehog Homolog (SHH) belongs to a three-protein family called Hedgehog. The other two family members are Indian Hedgehog (IHH) and Desert Hedgehog (DHH). Hedgehog proteins are key signaling molecules in embryonic development. SHH is expressed in various embryonic tissues and plays critical roles in regulating the patterning of many systems, such as limbs and brain. SHH also plays an important role in adult, including the division of adult stem cells and the development of certain cancers and other diseases.Mouse Shh is synthesized as a 437 aa precursor that contains a 24 aa signal sequence and a 413 aa mature region. The mature region is autocatalytically processed into a nonglycosylated, 20 kDa, 174 aa N­terminal fragment (Shh­N), and a catalytic­processing,glycosylated, 34 kDa, 239 aa C­terminal fragment. The 20 kDa Shh­N fragment is the core of the active hedgehog molecule. Mouse Shh­N is 99%, 98%, and 100% aa identical to human, rat and gerbil Shh­N, respectively.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e19.8 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e20 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe C-terminal part of the sonic hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein into two parts (ShhN and ShhC) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated ShhN. Both activities occur in the reticulum endoplasmic. Once cleaved, ShhC is degraded in the endoplasmic reticulum.; The dually lipidated sonic hedgehog protein N-product (ShhNp) is a morphogen which is essential for a variety of patterning events during development. Induces ventral cell fate in the neural tube and somites. Involved in the patterning of the anterior-posterior axis of the developing limb bud. Essential for axon guidance. Binds to the patched (PTCH1) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes. In the absence of SHH, PTCH1 represses the constitutive signaling activity of SMO.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eEndoplasmic reticulum membrane. Golgi apparatus membrane.; [Sonic hedgehog protein N-product]: Cell membrane; Lipid-anchor.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHedgehog family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            mmu:20423           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            10090.ENSMUSP00000002708           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28547659            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            show that eliminating mouse MACS1 causes severe defects in laryngeal development, indicating that MACS1-directed Shh signalling is indispensable for respiratory organogenesis            \u003ca rel=\"nofollow\"\u003e             PMID:                        28155855            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results suggest distinct functions of tuberous sclerosis complex 1 protein (Tsc1) and tuberous sclerosis complex 2 protein (Tsc2) in cellular signaling as the two genes affect ciliary length control and sonic hedgehog protein signaling via different mechanisms.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29396625            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study indicated that Shh, Sfrp1, and Wnt5a collaborate to direct the pathfinding of descending 5-HT axons in the brainstem.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29196093            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data illustrate that persistent Hh signaling in the palatal epithelium contributes to the etiology and pathogenesis of submucous cleft palate through its interaction with a p63\/Irf6-dependent biological regulatory loop and through a p63-induced cell adhesion network.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29981310            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SOX2 functions downstream of HH signaling to regulate lingual epithelium homeostasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29945863            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SHH expression is associated with medulloblastoma formation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29378965            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Identify SMO-dependent Shh signalling as a specific process for the activation of adventitial fibroblasts and the subsequent proliferation of smooth muscle cells and neointima formation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29088375            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In the mutant Hammer toe (Hm) genome, a 150-kb noncoding DNA fragment from chromosome 14 is inserted into the region upstream of the Sonic hedgehog (Shh) promoter in chromosome 5. Two different regions are necessary for the syndactyly phenotype of Hm.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29255029            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that Sonic hedgehog (Shh), which encodes a secreted protein signal, is expressed in the sensory neurons, and that experimental ablation of neuronal Shh expression causes loss of taste receptor cells (TRCs).            \u003ca rel=\"nofollow\"\u003e             PMID:                        29279401            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Here by inducing expression of constitutively active Smoothened (SmoM2) or Gli2 (DeltaNGli2) in the adipocyte lineage of postnatal mice, the authors show that targeted activation of Hedgehog signaling suppresses high-fat-diet-induced obesity and improves whole-body glucose tolerance and insulin sensitivity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29205155            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data suggest a potential novel mechanism in which alterations in SHH variance during evolution may have driven changes in limb patterning and digit length.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28131983            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Epithelial-mesenchymal transition programs promote basal mammary stem cell and tumor-initiating cell stemness by inducing primary ciliogenesis and Hedgehog signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29158396            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the knockdown of Ihh suppressed osteoblast growth and differentiation via a mechanism which may be associated with the TGF-beta\/Smad and OPG\/RANKL signaling pathways.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28990069            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH signaling regulates the direction of cerebellar granule cells division.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28633908            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The authors report here that Sonic Hedgehog (Shh)-Smoothened signaling downregulates Shisa2, which inhibits the glycosylation and cell surface presentation of Frizzled3 in rodent commissural axon growth cones.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28885142            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ESP of fifth-stage larval Angiostrongylus cantonensis stimulates astrocyte activation and IL-1beta and IL-6 production through NF-kappaB and the Shh signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28950910            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results indicate for the first time a possible mechanism involved in the crosstalk between fibroblasts and osteoblasts, as it was possible to observe trophic factors released by fibroblasts interfering decisively in osteoblast metabolism in a Shh-independent manner.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28578539            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Importantly, Scube2 uncouples processing of Shh peptides from their lipid-mediated juxtamembrane positioning, and thereby explains the long-standing conundrum that N-terminally unlipidated Shh shows patterning activity in Scube2-expressing vertebrates            \u003ca rel=\"nofollow\"\u003e             PMID:                        28778988            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Shh signaling requires the coordinated activity of Sulf1 and Sulf2 in order to reach that threshold in the mouse ventral spinal cord            \u003ca rel=\"nofollow\"\u003e             PMID:                        28490013            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH-dependent activation of WNT signaling supports regeneration of the cortex following long-term glucocorticoid treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29211850            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            by acting upstream of Shh signaling pathway, Barhl2 plays a crucial role in patterning the progenitor domains and establishing the positional identities of progenitor cells in the diencephalon.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27349434            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Gli3 activity in mouse thymic epithelial cells (TECs) promotes positive selection and differentiation from CD4(+) CD8(+) to CD4(+) CD8(-) single-positive (SP4) cells in the fetal thymus and Gli3 represses Shh constitutive deletion of Gli3, and conditional deletion of Gli3 from TECs, reduced differentiation to SP4, whereas conditional deletion of Gli3 from thymocytes did not            \u003ca rel=\"nofollow\"\u003e             PMID:                        29361554            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study shows a new role for Maml1 as a component of Shh signaling, which plays a crucial role in both development and tumorigenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28726779            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Sonic Hedgehog Activates Phospholipase A2 to Enhance Smoothened Ciliary Translocation            \u003ca rel=\"nofollow\"\u003e             PMID:                        28591579            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            smaller mvShh conjugates resulted in faster wound resolution compared to the unconjugated Shh. This study is the first to show how the wound healing efficacy of multivalent protein-polymer conjugates is sensitive to the polymer MW, and our findings suggest that this parameter could be used to enhance the efficacy of growth factor conjugates.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28679037            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH can promote cell growth and cell osteoblastic\/cementoblastic differentiation via BMP pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        27289556            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These studies reveal a postnatal cell population with transient Shh signaling that contributes to oligodendrogenesis during corpus callosum myelination, and gives rise to cells that continue to proliferate in adulthood and contribute to corpus callosum remyelination            \u003ca rel=\"nofollow\"\u003e             PMID:                        29045809            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results support a model whereby mutations in Cdon and prenatal ethanol exposure increase Septo-optic dysplasia risk through spatiotemporal perturbations in Shh signaling activity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27935818            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results report the identification of a novel long-range enhancer for Shh-Shh-brain-enhancer-6 (SBE6)-that is located 100 kb upstream of Shh and that is required for the proper induction of Shh expression during this differentiation program.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27852806            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Hh orchestrates the balance between quiescent and activated NSCs, with important implications for understanding adult neurogenesis under normal homeostatic conditions or during injury.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27666792            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            neuroectodermal Shh expression, dorsal\/ventral patterning, and amount of proliferation in the ventral neuroectoderm was not changed in Wnt1-Cre;Kif3a(fl\/fl) mutants; however, tissue polarity and directional cell division were disrupted.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28941984            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The authors find that cholesterol, an important component of the cell membrane, directly binds to Smoothened and changes its shape so that it can activate Hedgehog signaling components inside cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27705744            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Embryonal tumors with multilayered rosettes (ETMRs) are characterized by a parallel activation of Shh and Wnt signaling. Co-activation of these pathways in mouse neural precursors is sufficient to induce ETMR-like tumors in vivo that resemble their human counterparts on the basis of histology and global gene-expression analyses, and that point to apical radial glia cells as the possible tumor cell of origin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28892064            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            reactivating SHH signaling in mutant lungs rescued the tip dilation phenotype and attenuated FGF signaling. Importantly, the reduced SHH signaling activity did not appear to be caused by decreased Shh expression or protein stability; instead, biologically active form of SHH proteins were reduced in both the Ext1 mutant epithelium and surrounding wild type mesenchymal cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28859094            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            provide compelling evidence that epidermal YAP and Hedgehog\/GLI2 signalling undergo positive regulatory interactions in the control of normal epidermal homeostasis and in basal cell carcinoma (BCC) development, which in the large majority of cases is caused by aberrant Hedgehog signalling activity            \u003ca rel=\"nofollow\"\u003e             PMID:                        28820907            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            conditional deletion of Shh in the anterior hypothalamus results in a fully penetrant phenotype characterised by a complete arrest of (Rathke's pouch) RP development, with lack of Lhx3\/Lhx4 expression in RP epithelium.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28807898            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Shh production and Gli signaling is activated in vivo in lung, enhancing the Th2 response during a murine model of allergic asthma            \u003ca rel=\"nofollow\"\u003e             PMID:                        28235772            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Shh is in part responsible for the dependence of taste cell renewal on gustatory innervation, neurotrophic support of taste buds likely involves a complex set of factors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28743797            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPC6 stimulates Hh signaling by binding to Hh and Ptc1 at the cilium and increasing the interaction of the receptor and ligand to promote the growth of developing long bones.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28696225            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate that the transcription factor Gli3 (Gli3)-mutant fetal liver (FL) had increased sonic hedgehog (Shh) signaling resulting in decreased B cell development.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28533268            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate odd-skipped related protein 1 (Osr1) as a mediator of Hedgehog (HH) signaling during foregut organogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28501478            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            direct targeting of Foxf2 by Shh signaling drives cranial neural crest cell mesenchyme proliferation during upper lip morphogenesis, and disruption of this sequence results in cleft lip.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28506991            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Dicer1 ablation impairs Shh-induced granule neuron precursor proliferation by disrupting the expression of distinct cell cycle regulator genes that are targets of miR-17 approximately 92 cluster members. This study establishes a molecular link between miRNAs and cell cycle progression in the proliferating Granule neuron precursors during normal cerebellar development and may facilitate miRNA application in treating med...            \u003ca rel=\"nofollow\"\u003e             PMID:                        27600805            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of Bmp4 in the ureteric mesenchyme depends on HH signaling and Foxf1, and that exogenous BMP4 rescued cell proliferation and epithelial differentiation in ureters with abrogated HH signaling or FOXF1 function.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28797033            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A model in which SHH signaling plays both positive and negative roles in patterning and organogenesis of the thymus and parathyroids.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27633995            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This suggests an important cross-talk between SHH and WIP1 pathways that accelerates tumorigenesis and supports WIP1 inhibition as a potential treatment strategy for MB.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27086929            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SHH expression is associated with Medulloblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28031228            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            sonic hedgehog signaling activity influences clonal spatial distribution of thalamic neurons.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28250409            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Both the number of lung CD31-CD45-Sca-1+ cells and the expression levels of the Shh signaling pathway were downregulated in the lung tissues of mice with pulmonary emphysema. These cells and Shh signaling pathway are reactivated during acute adenovirus infection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28352167            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915102388449,"sku":"BL-1763NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYWALedOAAC7NrlTd-U363_cda16a87-e716-4cca-b903-a59878552f9d.jpg?v=1685853339"},{"product_id":"recombinant-human-pro-ngf-protein-bl-1793np","title":"Recombinant Human pro-Beta NGF Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human pro-Nerve Growth Factor is produced by our E.coli expression system and the target gene encoding Glu19-Ala241 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP01138\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBeta-Nerve Growth Factor; Beta-NGF; NGF; NGFB;β-NGF; pro-Beta NGF\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe precursor form of the nerve growth factor (proNGF) like its mature form is characterized by the cystin knot motif consisting of three cystine bridges, whereas proneurotrophins and mature neurotrophins elicit opposite biological effects. ProNGF functions preferentially via the complex of pan-neurotrophin receptor p75 (p75NTR) and vps10p domain-containing receptor sortilin inducing neuronal apoptosis and contributing to age- and disease-related neurodegeneration.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e25 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e30 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl,500mM NaCl,5%Trehalose,5%Mannitol,0.01%tween80,1mM EDTA,pH8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (Probable). The immature NGF precursor (proNGF) functions as ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and\/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse. In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI. Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer. The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted. Endosome lumen.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            7808           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            162030           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4803           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000358525           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29527653            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Single nucleotide polymorphisms in NGF gene (rs6330) and NGFR gene (rs2072446 and rs734194) are associated with ischemic stroke. The NGF rs6330*T and NGFR rs2072446*T minor alleles might be nominated as a risk factor for developing ischemic stroke and NGFR rs734194*G minor allele as a protective against this disease at least in Armenian population            \u003ca rel=\"nofollow\"\u003e             PMID:                        29499660            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Neurotrophic factors and hippocampal activity in PTSD            \u003ca rel=\"nofollow\"\u003e             PMID:                        29799860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SNRPA may contribute to GC progression via NGF and could be a prognostic biomarker for GC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30039889            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that NGF signalling is strongly linked to pathological and regenerative processes in human teeth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28465581            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggest an interaction between NGF, GDNF and MMP-9 during the transition to malignancy in prostate cancer (PC). Also this interaction may involve in regulating PC cell differentiation, tumor invasion, progression, and the agressiveness of PC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28237042            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the anti-tumor activity of oleuropein against hepatocellular carcinoma could be attributed to influencing the pro-NGF\/NGF balance via affecting MMP-7 activity without affecting the gene expression of NGF            \u003ca rel=\"nofollow\"\u003e             PMID:                        29476769            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            co-expression patterns of NGF and heme oxygenase-1 might be used as prognostic indicators for gastric carcinoma patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        28679437            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This review will briefly address the peripheral and central sensitization mechanisms of airway neurons and will then focus on NGF signaling and its role in cough hypersensitivity.[review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        28494216            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            First-trimester plasma nerve growth factor is lower in patients who subsequently develop preeclampsia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27513943            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study show evidence of variation in plasmatic beta-NGF expression during the progression of dementia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27802234            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF is functionally linked to beta-catenin, promoting the migration of human ovarian cancer cells via the WNT\/beta-catenin pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27835587            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Varicella zoster virus DNA replication is regulated in part by an NGF pathway that is PI3-kinase-independent.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27683235            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Many studies indicate that the only presence of NGF is unable to generate cell carcinogenesis, both in normal neuronal and non-neuronal cells\/tissues. However, it cannot be excluded the possibility that the co-expression of NGF and pro-carcinogenic molecules might open to different consequence. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27439311            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the effect and underlying mechanisms of NGF\/BDNF on the production of NPW in PC12 cells and hypothalamus, is reported.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28249734            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data support a role for islet NGF in fine-tuning insulin secretion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27424144            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study indicated that dysmenorrhea pain severity is partly genetically determined by the chromosome 1p13.2, near the nerve growth factor locu.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27454463            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings suggest that IL-1beta and TNF-alpha regulate Nerve Growth Factor expression and production in synovial macrophages and fibroblasts in osteoarthritic joints.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28677145            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results advance our knowledge of the conformational properties of proNGF and NGF and help provide a rationale for the diverse biological effects of NGF and proNGF at the molecular level.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28798232            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study suggest that proNGF protein levels may augment the diagnostic accuracy of currently used CSF biomarker panels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26825093            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Neuroimmune-endocrine events may lead to overactivity of sympathetic nervous system that triggers cascade of pathologic conditions in ovary in polycystic ovary syndrome (PCOS). Data suggest women with PCOS exhibit reduction of CRH and NGF; reduction of CRH\/NGF may be under influence of sympathetic nervous system and may reflect deficit of neuronal stress-adaptation in PCOS patients. (CRH = corticotropin releasing hormone)            \u003ca rel=\"nofollow\"\u003e             PMID:                        27908212            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The rare nerve growth factor-beta (NGFB) mutation R221W causes a selective loss of thinly myelinated fibers and especially unmyelinated C-fibers. Carriers of this mutation show altered pain sensation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27146986            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF expression was positively correlated with disease severity and visceral hypersensitivity in irritable bowel syndrome patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27862119            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a stage-related modulation of beta-NGF and its receptors in the inflammatory process of OA            \u003ca rel=\"nofollow\"\u003e             PMID:                        28253191            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BDNF and NGF serum levels are reduced in the early and moderate glaucoma stages, suggesting the possibility that both factors could be further investigated as potential circulating biomarkers for the early detection of glaucoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28068360            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            overexpression of ARMS blocked NGF-mediated secretion, without affecting basal secretion, a decrease in ARMS resulted in potentiation. Similar effects were observed with synembryn-B, a protein that interacts directly with ARMS. Downstream of ARMS and synembryn-B are Galphaq and Trio proteins, which modulate the activity of Rac1 in response to NGF            \u003ca rel=\"nofollow\"\u003e             PMID:                        26966186            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that the standardized nerve growth factor (NGF) concentration was negatively correlated with continuous pain, neuropathic pain and total score, and the standardized S100 proteins S100A8\/A9 concentration was positively correlated with present pain intensity and continuous pain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27936243            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate that NGF inhibited CRT translocation induced by mitoxantrone. NGF effect on CRT translocation could have consequences in immunotherapy, potentially lessening the effectiveness of this type of treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28260038            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF stimulates generation of neurons, but not neuronal progenitors from embryonic stem cells and affects the proportion of specific types of neurons in cultures of differentiating embryonic stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28364186            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF attenuates these responses-both in vivo and in vitro. Therefore, NGF therapy may represent a novel approach for the management of diabetic keratopathy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27978558            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF signaling pathway provides a potential target for developing molecularly targeted therapies            \u003ca rel=\"nofollow\"\u003e             PMID:                        27792755            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these data suggest a positive feedback loop through which NGF-mediated upregulation of p75(NTR) can contribute to the chemo-resistance of Triple negative breast cancer cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27577679            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Based on these current developments, the present review provides not only a broad overview of the biological effects of NGF-TrkA-p75NTR on cancer cells and their microenvironment, but also explains why NGF and its receptors are going to evoke major interest as promising therapeutic anti-cancer targets in the coming decade.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27264679            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF\/CD133 might be an effective and potent therapeutic target for pancreatic cancer metastasis, particularly in perineural invasion            \u003ca rel=\"nofollow\"\u003e             PMID:                        27654574            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The analysis of covariance (ANCOVA) indicated that the mean serum GDNF and NTF3 levels of ADHD patients were significantly higher than that of controls. However, serum BDNF and NGF levels did not show any significant differences between groups.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27561780            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            All patients had serum neurotrophin (NT-3, BDNF, NGF) concentrations determined.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27367919            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum NGF does not differentiate between recurrent acute pancreatitis and chronic pancreatitis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27020638            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF FLIPs TrkA onto the death TRAIL in neuroblastoma cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        26962689            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Major depression patients had similar serum NGF to controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27008247            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data demonstrate the involvement and modulation of nerve growth factor and its receptors in chronic obstructive pulmonary disease and in its staging            \u003ca rel=\"nofollow\"\u003e             PMID:                        26408608            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study showed that IL-17, in addition to stimulating an inflammatory response, negatively regulates the action of NGF and NGF R in the polar forms of the leprosy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26616164            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Locally increased estrogen levels and inflammation may cause increased NGF production in the uterus of patients with adenomyosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25519715            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study is the first to thoroughly assess the enhancement of neural differentiation of bone marrow mesenchymal stem cells following transfection with bFGF and NGF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26572749            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest MMP7 (matrix metalloproteinase 7) in follicular fluid cleaves proNGF (pro-nerve growth factor) in ovarian follicle; both MMP7 and proNGF appear to be products of granulosa cells; processing of proNGF to NGF appears to regulate apoptosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26457789            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF promotes renal fibrosis via TGF-beta1-signaling activation, suggesting that in kidney diseases high NGF serum levels could contribute to worsen renal fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26066770            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study suggests that the circadian rhythm in the esophagus may be important for the mediation of and\/or the response to erosive damage in GERD patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26337663            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Intratumoral nerve growth factor expression is not associated with perineural invasion in patients with resected extrahepatic cholangiocarcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26547754            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF has a role in modulating trkANGFR\/p75NTR in alphaSMA-expressing conjunctival fibroblasts from human ocular cicatricial pemphigoid            \u003ca rel=\"nofollow\"\u003e             PMID:                        26569118            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NGF-induced tyrosine kinase independent TrkA signaling through CD44 is sufficient to maintain tumor aggressiveness in breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        25840418            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Urinary NGF, but not BDNF, levels decreased significantly after hyaluronic acid therapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24614892            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915103273185,"sku":"BL-1793NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLSSAcFRNAACp9vJKOuQ209_68554ca0-87a2-4742-904d-d05959270569.jpg?v=1685853373"},{"product_id":"recombinant-human-cntf-protein-bl-1799np","title":"Recombinant Human CNTF Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Ciliary Neurotrophic Factor is produced by our E.coli expression system and the target gene encoding Ala2-Met200 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP26441\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCiliary Neurotrophic Factor; CNTF\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCiliary Neurotrophic Factor (CNTF) is a potent survival factor for neurons and oligodendrocytes. CNTF has also been shown to prevent the degeneration of motor axons after axotomy. CNTF is highly conserved across species and exhibits cross-species activities. Human and rat CNTF share approximately 83% homology in their protein sequence. CNTF is structurally related to IL6, IL11, LIF and OSM. All of these four helix bundle cytokines share gp130 as a signal transducing subunit in their receptor complexes. CNTF, like FGF acidic, FGF basic, and PD-ECGF (platelet-derived endothelial cell growth factor), does not possess a signal sequence that would allow secretion of the factor by classical secretion pathways. The mechanism underlying the release of CNTF is unknown.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e22.93 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e25 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 100mM NaCl, pH 8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCytoplasm.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCNTF family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            2169           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            118945           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:1270           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000355370           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29564604            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Cytokines of the LIF\/CNTF family and metabolism            \u003ca rel=\"nofollow\"\u003e             PMID:                        26817395            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High hydrostatic pressure enables almost 100% refolding of recombinant human ciliary neurotrophic factor from inclusion bodies at high concentration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28323167            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CNTFR-specific mutants of CNTF have been developed that bind to the CNTFRalpha-LIFRbeta-gp130 receptor.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26187860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Human CNTF expression through lentiviral gene transfer in the rat striatum significantly decreased the levels of neuronal metabolites (N-acetyl-aspartate, N-acetyl-aspartyl-glutamate, and glutamate).            \u003ca rel=\"nofollow\"\u003e             PMID:                        25833344            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the biological effects of CNTF on retinoic acid (RA)-predifferentiated SH-SY5Y neuroblastoma cells and the underlying molecular mechanism of this effect were investigated for the first time            \u003ca rel=\"nofollow\"\u003e             PMID:                        25118897            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            R28E mutation in CNTF abrogatesIL-6 receptor-dependent but retains CNTF receptor-dependent signaling via glycoprotein 130\/ LIFR.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24802752            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this review, CNTF plays an important role in neurogenesis and differentiation of neural stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23948898            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The levels of expression and secretion of BDNF and CTNF of induced cells were assessed using immunocytochemical, Real-Time polymerase chain reaction, and enzyme linked immunosorbent assay (ELISA).            \u003ca rel=\"nofollow\"\u003e             PMID:                        23944834            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CNTF elevated in umbilical cord blood from pre-eclamptic pregnancies            \u003ca rel=\"nofollow\"\u003e             PMID:                        23654315            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CNTF-mediated protection of photoreceptors requires initial activation of the cytokine receptor gp130 in Muller glial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24191003            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Report favourable allelic patterns of ACTN3 and CNTF genes on aerobic performance in athletes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23676962            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that aspirin increased mRNA and protein expression of CNTF in primary mouse and human astrocytes in a dose- and time-dependent manner.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23653362            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we show that the release of CNTF by glial cells is a very powerful stimulus for optic fiber regeneration and retinal ganglion cell survival after optic nerve crush            \u003ca rel=\"nofollow\"\u003e             PMID:                        23194670            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ciliary neurotrophic factor levels were increased in painful PTT only.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22337942            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Peptide 6c, corresponding to human CNTF amino acid residues 147-150, induces neurogenesis, neuronal activity and proliferation of immature neurons in the dentate gyrus and improvement of spatial reference memory in mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20952820            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CNTF's effects on retinal pigment epithelial (RPE) physiology            \u003ca rel=\"nofollow\"\u003e             PMID:                        21912637            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that variants in CNTF were significantly associated with a lower age at onset of the eating disorders.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20219210            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The role played by CNTF in retinal cell differentiation and survival in retinal progenitors, is reported.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20428961            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ciliary neurotrophic factor, and related (CNTF), ligands targeting the established CNTF receptor alpha, binds to sortilin with high affinity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20584990            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In women the CNTF polymorphism (odds ratio (OR) = 2.15, 95%CI: 1.27-3.64, p = 0.004) are associated with weight gain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19833146            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studies indicate that leptin, CNTF, LIF and IL-6 present similar three-dimensional fold structure, interact with related class-I receptors and activate similar intracellular pathways.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19751193            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A null mutation in this protein was evaluated for a relationship to disease susceptibility and disease severity in patients with multiple sclerosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        11857064            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Association of a null mutation in the CNTF gene with early onset of multiple sclerosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        11890844            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Early onset of severe familial amyotrophic lateral sclerosis with a SOD-1 mutation: potential impact of CNTF as a candidate modifier gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        11951178            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CTNF binds to the IL-6 receptor and has a role in neuroprotection            \u003ca rel=\"nofollow\"\u003e             PMID:                        12643274            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            no evidence found to suggest that ciliary neurotrophic factor is involved in the pathogenesis of pelvic endometriosis            \u003ca rel=\"nofollow\"\u003e             PMID:                        12890930            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Constitutive expression of cytokines in brain induces changes in gene expression characteristic of chronic inflammation leading to either temporal weight reduction (CNTF) or severe cachexia (leukemia inhibitory factor).            \u003ca rel=\"nofollow\"\u003e             PMID:                        14715713            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results do not support an effect of the CNTF null allele on body composition, contrary to previous findings.            \u003ca rel=\"nofollow\"\u003e             PMID:                        14747836            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings support the hypothesis that CNTF and leptin engage distinct CNS sites and CNTF possesses inflammatory properties distinct from leptin            \u003ca rel=\"nofollow\"\u003e             PMID:                        15047605            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In spite of axokine gene expression in retinal pigment epithelium, no photoreceptor rescue in retinal degeneration mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        15180291            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            myogenic lineage-committed human myoblasts can dedifferentiate at a clonal level; CNTF is a novel regulator of skeletal myoblast dedifferentiation via p44\/p42 MAPK pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        15843428            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CNTF negatively regulates phototransduction, which reduces the photoresponsiveness of rods, resulting in lower electroretinogram amplitudes following light stimulus.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17192435            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Possible neuroprotective role of CNTF in the optic nerve head.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17563726            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We conclude that absence of CNTF does not increase susceptibility for neurodegenerative disorders and confirm that it does not affect onset and course of familial and sporadic ALS.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17651970            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Continuous expression of striatal CNTF at the dose mediated by the expression cassette used in this study was detrimental to transgenic mice with Huntington's disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18293418            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The relative treatment benefit of iloperidone compared with placebo in patients with schizophrenia is enhanced in patients homozygous G\/G for the rs1800169 polymorphism of CNTF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18303965            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In vivo and in vitro experiments implicate CNTF as an endogenous regulatory component of dopamine D2-receptor-dependent neurogenesis in the subventricular zone and the dentate gyrus of the hippocampus. (Review)            \u003ca rel=\"nofollow\"\u003e             PMID:                        18524890            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CNTF-mediated signaling is a molecular switch for neuronal versus glial differentiation of retinal stem cells\/progenitors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18669911            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ciliary neurotrophic factor, cardiotrophin-like cytokine, and neuropoietin share a conserved binding site on the ciliary neurotrophic factor receptor alpha chain            \u003ca rel=\"nofollow\"\u003e             PMID:                        18728012            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PTP-1B constitutes a key divergent element between leptin\/insulin and CNTF signaling pathways at the neuronal level.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19008309            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Certain SNP patterns in VDR and CNTF genes showed better improvement of parameters associated with the effects of low-resistance training using exercise machines as analyzed by comparison between SNP patterns and factor analysis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19082510            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study provided further evidence that the production of ciliary neurotrophic factor by Schwann cells is markedly reduced in Charcot-Marie-Tooth type 1A neuropathy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19525893            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fusion of HIV-1 TAT to CNTF may have modified the CNTF capacity to induce intracellular signaling in hypothalamic neurons.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19573019            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The CNTF 1357 G --\u0026gt; A polymorphism explains only a small portion of the variability in the muscle strength response to training in women.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19628720            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            An interaction between apoE3 and CNTF occurs with both delipidated apeE3 and apoE3 found within a lipoprotein particle in cerebrospinal fluid. This interaction potentiates the survival-promoting activity of CNTF for hippocampal neurons.            \u003ca rel=\"nofollow\"\u003e             PMID:                        9236223            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915100782817,"sku":"BL-1799NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLSiAHvV7AACmqEV5eeU758_05399fd1-f438-4cfb-a4fa-e3924afff2f5.jpg?v=1685853271"},{"product_id":"recombinant-mouse-lif-protein-bl-1823np","title":"Recombinant Mouse LIF Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Leukemia Inhibitory Factor is produced by our E.coli expression system and the target gene encoding Ser24-Phe203 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"P09056\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/P09056\/entry\"\u003eP09056\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLeukemia inhibitory factor;Differentiation-stimulating factor;lif;D factor\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMouse Leukemia inhibitory factor（lif）is a secreted protein which belongs to the LIF\/OSM family.LIF  has been implicated in a many physiological processes including development, hematopoiesis, bone metabolism, and inflammation. it has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e19.9 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e18 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 1 EU\/µg as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915099111649,"sku":"BL-1823NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLVaATtHeAABkuXGQSDA965_4055a4dd-22f8-4f1c-97c7-ea32e5fb848d.jpg?v=1685853202"},{"product_id":"recombinant-human-nrg1-nrg1b-protein-bl-1832np","title":"Recombinant Human NRG1Beta Protein (245AA)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Neuregulin-1 Beta is produced by our E.coli expression system and the target gene encoding Ser2-Lys246 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"AAA58639.1\" target=\"_blank\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/protein\/AAA58639.1\"\u003eAAA58639.1\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePro-neuregulin-1; Neuregulin-1 beta 1; NRG1-beta 1; HRG1-beta 1; EGF; NRG1; GGF; HGL; HRGA; NDF; SMDF\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePro-neuregulin-1,Neuregulin-1 beta 1（NRG1） is a  single-pass type I membrane protein and belongs to the neuregulin family .It contains 1 EGF-like domain and 1 Ig-like C2-type (immunoglobulin-like) domain. Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. The protein concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The multiple isoforms perform diverse functions such as inducing growth and differentiation of epithelial, glial, neuronal, and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Isoform 10 may play a role in motor and sensory neuron development.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e26.9 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e34 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 85% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915100881121,"sku":"BL-1832NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLViAJZmSAACR6jJqUPY586_76872335-9f55-48d3-92c8-ba42e3bfc37c.jpg?v=1685853275"},{"product_id":"recombinant-human-gdf11-protein-bl-1835np","title":"Recombinant Human\/Mouse\/Rat GDF-11 Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human\/Mouse\/Rat Growth Differentiation Factor 11 is produced by our Mammalian expression system and the target gene encoding Asn299-Ser407 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eO95390\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGrowth\/differentiation factor 11; GDF-11; Bone morphogenetic protein 11; BMP-11\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGrowth\/differentiation factor 11(GDF-11) is a secreted protein, which belongs to the transforming growth factor beta superfamily. GDF-11 controls anterior-posterior patterning by regulating the expression of Hox genes.  The secreted signal acts globally to specify positional identity along the anterior\/posterior axis during development. GDF11 has been shown to suppress neurogenesis through a pathway similar to that of myostatin, including stopping the progenitor cell-cycle during G-phase. The similarities between GDF11 and myostatin imply a likelihood that the same regulatory mechanisms are used to control tissue size during both muscular and neural development.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e12.5 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13-20 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSupplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 50% glycerol, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eStore at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening.Please minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped on dry ice\/polar packs.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted signal that acts globally to regulate anterior\/posterior axial patterning during development. May play critical roles in patterning both mesodermal and neural tissues. It is required for proper vertebral patterning and orofacial development. Signals through activin receptors type-2, ACVR2A and ACVR2B, and activin receptors type-1, ACVR1B, ACVR1C and TGFBR1 leading to the phosphorylation of SMAD2 and SMAD3.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            4216           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            603936           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:10220           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000257868           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30213293            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Physical inactivity was significantly related to the decreased GDF11 levels in COPD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29731621            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF11 expression was decreased in COPD patients' serum and cells when compared with that of healthy people.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29680737            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF11 may be a relevant myostatin-interacting peptide to successful aging in humans            \u003ca rel=\"nofollow\"\u003e             PMID:                        28701523            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The Growth Differentiation Factor 11 (GDF11) and Myostatin (MSTN) in tissue specific aging.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28472635            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Tumor-suppressor inactivation of GDF11 occurs by precursor sequestration in triple-negative breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        29161592            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These studies identify distinctive structural features of GDF11 that enhance its potency, relative to GDF8; however, the biological consequences of these differences remain to be determined.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28257634            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In elderly Chinese women, osteoporosis risk was significantly increased with increases in GDF11 serum levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27557752            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A Prodomain Fragment from the Proteolytic Activation of Growth Differentiation Factor 11 Remains Associated with the Mature Growth Factor and Keeps It Soluble            \u003ca rel=\"nofollow\"\u003e             PMID:                        28715204            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MSTN, but not GDF11, declines in healthy men throughout aging.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27304512            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF11 is highly concentrated in human platelets.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27509407            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The crystal structure of GDF11 was determined to a resolution of 1.50 A.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26919518            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF11 is essential for mammalian development and has been suggested to regulate aging of multiple tissues. It functions in the heart, skeletal muscle, and brain. Review.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27034275            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF11 inhibits rather than helps muscle regeneration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26001423            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Show that there is no age-related cardiac hypertrophy in disease-free 24-month-old C57BL\/6 mice and that restoring GDF11 in old mice has no effect on cardiac structure or function.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26383970            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            in vitro sprout formation was increased as well by GDF11 treatment            \u003ca rel=\"nofollow\"\u003e             PMID:                        26026854            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Suggest GDF11 functions as encephalic regionalizing factor in neural differentiated mouse embryonic stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25352416            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF11 is a critical rheostat for bone turnover and a key integrator of bone homeostasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25534870            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data demonstrate GDF11 to be a master regulator of neural stem cell transcription that can suppress cell proliferation and migration by regulating the expression of numerous genes involved in both these processes            \u003ca rel=\"nofollow\"\u003e             PMID:                        24244313            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of GDF11, a cytokine which blocks terminal erythroid maturation, was increased in erthyroblasts of thalassemic patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24658077            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Quantitative real-time reverse transcription-PCR in colorectal cancer specimens obtained from 130 patients showed that GDF11 mRNA expression in cancer tissue was significantly higher than in normal tissue            \u003ca rel=\"nofollow\"\u003e             PMID:                        17912435            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Members of the transforming growth factor beta (TGFbeta) superfamily, bone morphogenetic protein 2 (BMP2), and growth and differentiation factor 11 (GDF11), can signal cultured RGCs to form dendrites.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17997109            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We propose that Pcsk5, at least in part via GDF11, coordinately regulates caudal Hox paralogs, to control anteroposterior patterning, nephrogenesis, skeletal, and anorectal development.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18519639            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Differential antagonism of activin, myostatin and growth and differentiation factor 11 by wild-type and mutant follistatin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18535106            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Both WFIKKN1 and WFIKKN2 have high affinity for growth and differentiation factors 8 and 11.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18596030            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myostatin or 20 ng\/mL BMP-11 maintain the colony and cellular morphology of undifferentiated hESC, maintain POU5f1, NANOG, TRA-1-60, and SSEA4 expression, and display increased SMAD2\/3 phosphorylation            \u003ca rel=\"nofollow\"\u003e             PMID:                        19751112            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915101765857,"sku":"BL-1835NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLVuAbZRMAACcPwnSwmw477_82bae0a3-d0d6-43eb-9e55-d48d5fac8030.jpg?v=1685853313"},{"product_id":"recombinant-human-neurturin-protein-bl-1855np","title":"Recombinant Human Neurturin Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Neurturin is produced by our E.coli expression system and the target gene encoding Ala96-Val197 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eQ99748\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNeurturin; NRTN\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNeurturin is a member of the GDNF family of ligands, which include glial cell-derived neurotrophic factor (GDNF), Neurturin, Persephin, and Artemin. Neurturin is expressed in both neuronal and nonneuronal tissues. Similarly to other TGFβ family proteins, Neurturin is synthesized as a precursor protein that is cleaved at the dibasic cleavage site (RXXR) to release the carboxyterminal domain. The carboxy terminal domain of Neurturin contains the characteristic seven conserved cysteine residues necessary for the formation of the cysteine-knot and the single interchain disulfide bond. Biologically active human Neurturin is a disulfide-linked homodimer of the carboxy-terminal 102 amino acid residues. Unlike other members of TGF-β family, bioactivities of all GDNF family ligands are mediated through a unique multicomponent receptor complex composed of high affinity ligand binding component (GFRα-1-GFRα-4) and a common signaling component (cRET receptor tyrosine kinase). Each member of the GDNF family ligands has its preferred binding protein. Neurturin preferentially binds to GFRα-2 but can also bind GFRα-1 at higher concentrations. It may play a role in regulating the development and maintenance of the central and peripheral nervous systems and as well as non neuronal systems.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e11.8 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e15 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM Citrate, 6% Sucrose, 4% Mannitol, 0.05% Tween 80, pH 4.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSupports the survival of sympathetic neurons in culture. May regulate the development and maintenance of the CNS. Might control the size of non-neuronal cell population such as haemopoietic cells.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGF-beta family, GDNF subfamily\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            8007           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            602018           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4902           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000302648           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29414779            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            In the cochlea, NTN immunostaining was found in the supporting cells of organ of Corti, including Deiters' cells, Hensen cells as well as Claudius' cells. In the spiral ganglia, NTN was seen in both the cell bodies and the nerve fibers of neurons.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24139947            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Neurturin contributes toward an aggressive cancer cell phenotype, neuropathic pain and neuronal plasticity in pancreatic cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24067900            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Human neurturin protected crayfish neurons and glia from photodynamic injury.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22847529            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Cyclic AMP signalling through PKA but not Epac is essential for neurturin-induced biphasic ERK1\/2 activation and neurite outgrowths through GFRalpha2 isoforms.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21723942            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDNF and NRTN are new neuromodulators that regulate the development of the neuromuscular synapse            \u003ca rel=\"nofollow\"\u003e             PMID:                        11790765            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The gene expression of protein was studied in the developing human tooth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        12397373            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results obtained suggest the involvement of NTN, PSP, and ART in processes subserving both the organization of this cortical region during development and the functional activity and maintenance of the mature human hippocampal neurons.            \u003ca rel=\"nofollow\"\u003e             PMID:                        15829225            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Addition of neurturin to activated peripheral blood mononuclear leukocytes reduces the amount of detectable tumor necrosis factor protein without altering its transcription.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16081799            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDNF and NTN differentially regulate the expression of distinct miRNA precursors through the activation of mitogen-activated protein kinase            \u003ca rel=\"nofollow\"\u003e             PMID:                        16895582            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Depending on the brain's expressions of specific GDNF family GFRalpha2 receptor spliced isoforms, neurturin may promote or inhibit neurite outgrowth through the multicomponent receptor complex.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17522305            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDNF, NTN, GFRalpha-1, GFRalpha-2, and c-Ret proteins are differentially expressed in the different stages of hair follicle cycle. GFRalpha-mediated signaling involves c-Ret and may play a role in human HF biology.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18222320            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            No differences were found in the allelic frequencies of the variants or in the haplotype distribution between Hirschsprung's disease patients \u0026amp; controls, nor to any demographic\/clinical parameters within the group of patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18970938            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915104157921,"sku":"BL-1855NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLXKAOrMoAACjNu22QFo711_688339a4-4d24-405f-aa42-0dab2d120ea9.jpg?v=1685853405"},{"product_id":"recombinant-human-hmgb1-protein-mari-tag-bl-1897np","title":"Recombinant Human HMGB1 Protein (Truncated)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human High Mobility Group Protein B1 is produced by our E.coli expression system and the target gene encoding Pro92-Val176 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP09429\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHigh Mobility Group Protein B1; High Mobility Group Protein 1; HMG-1; HMGB1; HMG1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHigh mobility group protein B1 is a member of the HMGB family consisting of three members, HMGB1, HMGB2 and HMGB3.It  Contains 2 HMG box DNA-binding domains entitled box A and box B and It is a highly negative-charged C terminus. As a nuclear protein, HMGB1 stabilizes nucleosomes and allows bending of DNA that facilitates gene transcription which is essential for individual survival. Meanwhile, it is revealed that HMGB1 can also act as a cytokine extracellularlly and regulates monocyte, T cell, dendritic cell activities in inflammatory responses.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e10 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 50mM HEPES-Na, 500mM NaCl, 0.6mM DTT, pH 7.9.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMultifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability (Ref.71). Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and\/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2\/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogdenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins such as huntingtin (HTT) or TBP.; Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and\/or bringing distant regulatory sequences into close proximity. May have an enhancing role in nucleotide excision repair (NER). However, effects in NER using in vitro systems have been reported conflictingly. May be involved in mismatch repair (MMR) and base excision repair (BER) pathways. May be involved in double strand break repair such as non-homologous end joining (NHEJ). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). In vitro can displace histone H1 from highly bent DNA. Can restructure the canonical nucleosome leading to relaxation of structural constraints for transcription factor-binding. Enhances binding of sterol regulatory element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA sequences and increases their transcriptional activities. Facilitates binding of TP53 to DNA. Proposed to be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion implicating HSPB1; however, this function has been questioned. Can modulate the activity of the telomerase complex and may be involved in telomere maintenance.; In the cytoplasm proposed to dissociate the BECN1:BCL2 complex via competitive interaction with BECN1 leading to autophagy activation. Involved in oxidative stress-mediated autophagy. Can protect BECN1 and ATG5 from calpain-mediated cleavage and thus proposed to control their proautophagic and proapoptotic functions and to regulate the extent and severity of inflammation-associated cellular injury. In myeloid cells has a protective role against endotoxemia and bacterial infection by promoting autophagy. Involved in endosomal translocation and activation of TLR9 in response to CpG-DNA in macrophages.; In the extracellular compartment (following either active secretion or passive release) involved in regulation of the inflammatory response. Fully reduced HGMB1 (which subsequently gets oxidized after release) in association with CXCL12 mediates the recruitment of inflammatory cells during the initial phase of tissue injury; the CXCL12:HMGB1 complex triggers CXCR4 homodimerization. Induces the migration of monocyte-derived immature dendritic cells and seems to regulate adhesive and migratory functions of neutrophils implicating AGER\/RAGE and ITGAM. Can bind to various types of DNA and RNA including microbial unmethylated CpG-DNA to enhance the innate immune response to nucleic acids. Proposed to act in promiscuous DNA\/RNA sensing which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. Promotes extracellular DNA-induced AIM2 inflammasome activation implicating AGER\/RAGE. Disulfide HMGB1 binds to transmembrane receptors, such as AGER\/RAGE, TLR2, TLR4 and probably TREM1, thus activating their signal transduction pathways. Mediates the release of cytokines\/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10. Promotes secretion of interferon-gamma by macrophage-stimulated natural killer (NK) cells in concert with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the primary receptor promoting macrophage activation and signaling through TLR4 seems to implicate LY96\/MD-2. In bacterial LPS- or LTA-mediated inflammatory responses binds to the endotoxins and transfers them to CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes. Contributes to tumor proliferation by association with ACER\/RAGE. Can bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex. Binding to class A CpG activates cytokine production in plasmacytoid dendritic cells implicating TLR9, MYD88 and AGER\/RAGE and can activate autoreactive B cells. Via HMGB1-containing chromatin immune complexes may also promote B cell responses to endogenous TLR9 ligands through a B-cell receptor (BCR)-dependent and ACER\/RAGE-independent mechanism. Inhibits phagocytosis of apoptotic cells by macrophages; the function is dependent on poly-ADP-ribosylation and involves binding to phosphatidylserine on the cell surface of apoptotic cells. In adaptive immunity may be involved in enhancing immunity through activation of effector T cells and suppression of regulatory T (TReg) cells. In contrast, without implicating effector or regulatory T-cells, required for tumor infiltration and activation of T-cells expressing the lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant progression. Also reported to limit proliferation of T-cells. Released HMGB1:nucleosome complexes formed during apoptosis can signal through TLR2 to induce cytokine production. Involved in induction of immunological tolerance by apoptotic cells; its pro-inflammatory activities when released by apoptotic cells are neutralized by reactive oxygen species (ROS)-dependent oxidation specifically on Cys-106. During macrophage activation by activated lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes.; (Microbial infection) Critical for entry of human coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus NL63\/HCoV-NL63. Regulates the expression of the pro-viral genes ACE2 and CTSL through chromatin modulation.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNucleus. Chromosome. Cytoplasm. Secreted. Cell membrane; Peripheral membrane protein; Extracellular side. Endosome. Endoplasmic reticulum-Golgi intermediate compartment.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHMGB family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca href=\"https:\/\/www.genenames.org\/cgi-bin\/gene_symbol_report?hgnc_id=HGNC:4983\" rel=\"nofollow\"\u003e            4983           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca href=\"https:\/\/www.omim.org\/entry\/163905\" rel=\"nofollow\"\u003e            163905           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca href=\"https:\/\/www.genome.jp\/dbget-bin\/www_bget?hsa:3146\" rel=\"nofollow\"\u003e            hsa:3146           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca href=\"https:\/\/string-db.org\/network\/9606.ENSP00000343040\" rel=\"nofollow\"\u003e            9606.ENSP00000343040           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/UniGene\/clust.cgi?ORG=Hs\u0026amp;CID=434102\"\u003e            Hs.434102           \u003c\/a\u003e \u003c\/p\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTissue Specificity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eUbiquitous. Expressed in platelets.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eGene Functions References\u003c\/h3\u003e\u003col\u003e \u003cli\u003e            Based on these findings, ischemia\/reperfusion-induced MCPIP1 expression regulates the migration and apoptosis of human vascular endothelial cells via HMGB1 and CaSR, respectively.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29379093\" rel=\"nofollow\"\u003e             PMID:                        29379093            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studied association of plasma levels of high mobility group box 1 (HMGB1) in critically ill patients.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29862569\" rel=\"nofollow\"\u003e             PMID:                        29862569            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The high-mobility group box (HMGB) proteins, particularly HMGB1, are self-derived innate immune activators that have multiple functions in the regulation of immunity and inflammation. Recent discoveries have illustrated the close link between HMGB1 and heart allograft rejection.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29198620\" rel=\"nofollow\"\u003e             PMID:                        29198620            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-193a plays a suppressive role in osteogenic differentiation of human bone marrow-derived stroma cell via targeting HMGB1.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29787753\" rel=\"nofollow\"\u003e             PMID:                        29787753            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Platelet HMGB1 mediated neutrophil-extracellular traps release is a primary regulator of deep vein thrombosis in mice.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29391442\" rel=\"nofollow\"\u003e             PMID:                        29391442            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study findings suggested that TCTP promotes colorectal cancer metastasis through regulating the behaviors of HMGB1 and the downstream activation of the NF-kappaB signaling pathway.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30066846\" rel=\"nofollow\"\u003e             PMID:                        30066846            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            in the present study we explore the characteristic binding mode and energetics of Act D binding to 21 nt mimed CpG sequence in the positive regulatory region of hmgb1 gene to identify areas of pressing experimental need..            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28033959\" rel=\"nofollow\"\u003e             PMID:                        28033959            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study demonstrated that serum HMGB1 was upregulated and the expression levels of miR-381 were downregulated in patients with polymyositis (PM). Furthermore, high HMGB1 expression was associated with poor survival rate in patients with PM. A luciferase activity assay was used to confirm the binding of miR-381 and HMGB1 3' untranslated region.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29956737\" rel=\"nofollow\"\u003e             PMID:                        29956737            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High mobility group box 1 (HMGB1) and OV-6 antigen (OV-6) positive staining are promising prognostic parameters for hepatocellular carcinoma (HCC), suggesting that HMGB1 and OV-6 may cooperate with each other and predict poor prognosis of HCC.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29441453\" rel=\"nofollow\"\u003e             PMID:                        29441453            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results demonstrate that non-oxidizable HMGB1 induce a sustained cardiac fibroblasts migration despite the redox state of the environment and by altering CXCL12\/CXCR4 axis. This affects proper cardiac remodeling after an infarction.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28716707\" rel=\"nofollow\"\u003e             PMID:                        28716707            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High HMGB1 expression is associated with reduced chemosensitivity in the pleural effusion of non-small cell lung cancer.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28885675\" rel=\"nofollow\"\u003e             PMID:                        28885675            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This work indicates that NELL-1, HMGB1, and CCN2 might enhance bone defect healing via the recruitment of endogenous cells and induction of vascularization and act via different processes than BMP2.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28463604\" rel=\"nofollow\"\u003e             PMID:                        28463604            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            comparison of inhibitory potential of the already known inhibitors of Head and neck squamous cell carcinoma against HMGB1-binding pocket using simulations and docking.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/27900730\" rel=\"nofollow\"\u003e             PMID:                        27900730            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            identified 2 novel miR-193a-3p targets, the high mobility group box-1 (HMGB1) and the hypoxia upregulated-1 (HYOU1) gene products. HMGB1 silencing in cord blood ECFC-derived cells confirmed its role in regulating vascular function.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28276476\" rel=\"nofollow\"\u003e             PMID:                        28276476            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that HMGB1 is highly expressed in prostate cancer (PC) tissues. Highly expressed HMGB1 activates RAGE\/NF-kappaB signaling pathways, which facilitates the metastasis of prostate cancer.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29845254\" rel=\"nofollow\"\u003e             PMID:                        29845254            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 was identified as a down-stream target of miR-204. The miR-204\/HMGB1 axis mediated ZEB2-AS1's effect on pancreatic cancer.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29753015\" rel=\"nofollow\"\u003e             PMID:                        29753015            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study demonstrated that HMGB1 and TLR4 could contribute to the inflammatory lichen planus process in skin.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29728859\" rel=\"nofollow\"\u003e             PMID:                        29728859            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our research shows that HMGB1 participates in autophagy and DNA damage repair and that downregulation of HMGB1 enhances the sensitivity of multiple myeloma (MM)cells to Dex, suggesting that HMGB1 may serve as a target for MM treatment.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30157958\" rel=\"nofollow\"\u003e             PMID:                        30157958            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 plays a critical role in mitochondrial autophagy in cardiomyocytes. miR-410 targets its 3'UTR and regulates its transcription.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28914970\" rel=\"nofollow\"\u003e             PMID:                        28914970            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 is a good diagnostic biomarker for differentiating refractory M. pneumoniae pneumonia and non-refractory M. pneumoniae pneumonia.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30157804\" rel=\"nofollow\"\u003e             PMID:                        30157804            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 promoted lung cancer invasion and metastasis by upregulating the expression and activity of MMP-2 in an NF-kappaB-dependent manner.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29850505\" rel=\"nofollow\"\u003e             PMID:                        29850505            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            meta-analysis exploring the association of four HMGB1 polymorphisms with cancer.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29730397\" rel=\"nofollow\"\u003e             PMID:                        29730397            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            levels of serum HMGB1 were positively associated with 10-year CHD risk            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29704473\" rel=\"nofollow\"\u003e             PMID:                        29704473            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            high mobility group box 1-receptor for advanced glycation end-products (HMGB1-RAGE) signaling pathway may be involved in the pathogenesis of preterm premature rupture of membranes (pPROM)            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29673663\" rel=\"nofollow\"\u003e             PMID:                        29673663            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MiR-106 interacted with the 3'-UTR of HMGB1 and inhibited HMGB1 expression.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30055307\" rel=\"nofollow\"\u003e             PMID:                        30055307            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            It is a 30 kDa protein that is a lethal mediator in sepsis and is a recognized therapeutic target.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30135341\" rel=\"nofollow\"\u003e             PMID:                        30135341            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 knockdown and miR-505 overexpression promoted ADM-induced DNA damage in HCC cells.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29803174\" rel=\"nofollow\"\u003e             PMID:                        29803174            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings indicated that HMGB1 likely regulates autophagy in LO2 cells exposed to anoxia-reoxygenation injury            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29880383\" rel=\"nofollow\"\u003e             PMID:                        29880383            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            extracellular functions of HMGB1 in cellular and immune homeostasis at the airway mucosal surface            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28976774\" rel=\"nofollow\"\u003e             PMID:                        28976774            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our results indicate that genetic variations in the HMGB1 gene may serve as an important predictor of breast cancer progression and metastasis.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29725248\" rel=\"nofollow\"\u003e             PMID:                        29725248            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            soluble CD52 exerts a concerted immunosuppressive effect by first sequestering HMGB1 to nullify its proinflammatory Box B, followed by binding to the inhibitory Siglec-10 receptor, triggering recruitment of SHP1 to the intracellular immunoreceptor tyrosine-based inhibitory motif of Siglec-10 and its interaction with the TCR.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29997173\" rel=\"nofollow\"\u003e             PMID:                        29997173            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In lung cancer patients, circulating HMGB1-containing nucleosome is higher in those under chemotherapy, predicting poorly cancer cell differentiation state, enhanced cancer invasion and advanced TNM stages.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29679570\" rel=\"nofollow\"\u003e             PMID:                        29679570            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a number of microRNAs (miRNAs) are identified as a class of regulators for broad control of HMGB1-mediated biological actions in eukaryotic cells.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29651425\" rel=\"nofollow\"\u003e             PMID:                        29651425            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The study indicated polymorphisms in HMGB1 may be a novel biomarker for female lung adenocarcinoma risk.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29617336\" rel=\"nofollow\"\u003e             PMID:                        29617336            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Glycyrrhizin reduced the activity of JAK\/STAT signaling pathway, which is the upstream regulator of HMGB1.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29568761\" rel=\"nofollow\"\u003e             PMID:                        29568761            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 may be a useful prognostic biomarker in malignant pleural mesothelioma when detected by immunohistochemistry, but cannot be considered a diagnostic biomarker in histological samples of mesothelioma            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29356044\" rel=\"nofollow\"\u003e             PMID:                        29356044            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the present study indicates that PBX 3'UTR may induce inflammatory responses and sepsis via acting as a competing endogenous RNA for HMGB1.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29484406\" rel=\"nofollow\"\u003e             PMID:                        29484406            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            overexpression of HMGB1 potentially promoted epileptogenesis. CLinduced activation of glial cells may act via upregulation of HMGB1 and TLR4\/RAGE receptors, and the downstream transcription factor NFkappaB.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29393419\" rel=\"nofollow\"\u003e             PMID:                        29393419            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that HMGB1 is highly expressed in osteosarcoma tissues. Its expression is negatively regulated by miR-505 inhibiting proliferation, migration and invasion in osteosarcoma cells.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29251324\" rel=\"nofollow\"\u003e             PMID:                        29251324            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This review demonstrated the increased expression of HMGB-1 in thrombosis-related diseases, including coronary artery disease, stroke, peripheral arterial disease, disseminated intravascular coagulation, and venous thrombosis.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29940562\" rel=\"nofollow\"\u003e             PMID:                        29940562            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study shows elevated serum level of HMGB1 in patients with the antiphospholipid syndrome            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29410969\" rel=\"nofollow\"\u003e             PMID:                        29410969            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Chronic periodontitis nonsmokers had elevated levels of HMGB1 in gingival crevicular fluid. The levels of HMGB1 were correlated with severity of periodontitis. Chronic periodontitis smokers exhibited lower levels of HMGB1 than chronic periodontitis nonsmokers.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28209360\" rel=\"nofollow\"\u003e             PMID:                        28209360            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum HMGB1 levels in patients with inflamed appendix were significantly higher than in patients with normal appendix, and this could be a useful biomarker in improving the diagnostic accuracy of appendicitis.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/27922766\" rel=\"nofollow\"\u003e             PMID:                        27922766            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 silencing promoted the susceptibility of retinoblastoma cells to chemotherapeutic drugs through downregulating NF-kappaB.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29328447\" rel=\"nofollow\"\u003e             PMID:                        29328447            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 possesses beneficial actions, such as endothelial activation, enhancement of neurite outgrowth, and neuronal survival in ischemic stroke. [review]            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29054968\" rel=\"nofollow\"\u003e             PMID:                        29054968            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 mediates fibroblast activity via RAGE-MAPK and NF-kappaB signaling in keloid scar formation.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29283384\" rel=\"nofollow\"\u003e             PMID:                        29283384            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum HMGB1 may be a potential marker to monitor the surgical course in patients undergoing surgery for colorectal cancer.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/27834305\" rel=\"nofollow\"\u003e             PMID:                        27834305            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the promotive effects of HuR overexpression on the inflammatory response were attenuated when HUVECs were cotreated with HMGB1 short hairpin RNA. Therefore, the present results indicated that the ectopic expression of HuR may induce inflammatory responses and thus sepsis by activating the HMGB1 signaling pathway.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29115544\" rel=\"nofollow\"\u003e             PMID:                        29115544            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This is the first report to examine the risk factors associated with HMGB1 SNPs in the development of Rheumatoid arthritis disease in the Chinese Han population.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29200952\" rel=\"nofollow\"\u003e             PMID:                        29200952            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1\/IL-1beta complexes released after burn injuries can modulate immune responses            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29601597\" rel=\"nofollow\"\u003e             PMID:                        29601597            \u003c\/a\u003e \u003c\/li\u003e \u003c\/ol\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915104321761,"sku":"BL-1897NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYWAFv2ZAACqoeLekLo156_b38cfede-c714-47d1-9090-8dc66eb054e3.jpg?v=1685853411"},{"product_id":"recombinant-human-nrg1-nrg1b-protein-bl-1898np","title":"Recombinant Human NRG1Beta  Protein (71AA)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Neuregulin-1 Beta is produced by our E.coli expression system and the target gene encoding Thr176-Lys246 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"Q02297-6\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/Q02297\/entry#Q02297-6\"\u003eQ02297-6\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePro-neuregulin-1; Neuregulin-1 beta 1; NRG1-beta 1; HRG1-beta 1; EGF;NRG1; GGF; HGL; HRGA; NDF; SMDF\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eneuregulin-1 (heregulin-1，NRG1) is a member of  neuregulin family, which is comprised of four genes that encode a large number of secreted or membrane-bound isoforms. All family members share an EGF-like domain that interacts with the ErbB family of tyrosine kinase receptors. NRG1 isoforms can be classified into type I, type II and type III isoforms. NRG1 directs ligand for ERBB3 and ERBB4 tyrosine kinase receptors, concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. NRG proteins show distinct spatial and temporal expression patterns and play important roles during development of both the nervous system and the heart.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e8.2 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e7 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915104583905,"sku":"BL-1898NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYWADwNeAACrTR7PO1o926_1ff9cef3-0b40-4dcd-8264-c319237d1a04.jpg?v=1685853418"},{"product_id":"recombinant-human-persephin-protein-bl-1901np","title":"Recombinant Human Persephin Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Persephin is produced by our E.coli expression system and the target gene encoding Ala61-Gly156 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eO60542\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePersephin; PSP; PSPN\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePersephin is a secreted protein, belongs to the glial cell linederived neurotrophic factor (GDNF) family of the TGF-β superfamily. It shares 38-46% amino acid (aa) identity with family members GDNF, neurturin and artemin. It is expressed at very low levels in most tissues. Mature protein contains a signal sequence, a pro-domain and a 96 aa mature sequence with several cysteines that are conserved among family members. It circulates as an unglycosylated disulfide-linked homodimer. Like other GDNF family members, Persephin acts through engagement of GRFα4, a glycosylphosphatidylinositol (GPI)-linked GDNF receptor family Persephin is reported to promote both the survival and growth of central dopaminergic and motor neurons, and kidney development. These effects are correlated with the expression patterns of GFRα4, and RET.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e10.4 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e12 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 4mM HCl.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in 4mM HCl.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eExhibits neurotrophic activity on mesencephalic dopaminergic and motor neurons.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGF-beta family, GDNF subfamily\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            9579           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            602921           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:5623           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000245810           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        24375483            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Results identify persephin, a GDNF family member, as a novel ligand for GFRalpha1\/RET receptor complex.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20350599            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Persephin\/GFRalpha4 is unable to recruit RET protein into lipid rafts.            \u003ca rel=\"nofollow\"\u003e             PMID:                        15225646            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results obtained suggest the involvement of NTN, PSP, and ART in processes subserving both the organization of this cortical region during development and the functional activity and maintenance of the mature human hippocampal neurons.            \u003ca rel=\"nofollow\"\u003e             PMID:                        15829225            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            No differences were found in the allelic frequencies of the variants or in the haplotype distribution between Hirschsprung's disease patients \u0026amp; controls, nor to any demographic\/clinical parameters within the group of patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18970938            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915104682209,"sku":"BL-1901NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYaAH6YkAACa0HXXguQ797_d84ad902-b123-4ca7-9413-ee20755a9712.jpg?v=1685853422"},{"product_id":"recombinant-mouse-tgfb2-protein-bl-1912np","title":"Recombinant Mouse\/Rat TGF-beta 2 Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse\/Rat Transforming Growth Factor Beta 2 is produced by our Mammalian expression system and the target gene encoding Ala303-Ser414 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"P27090\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/P27090\/entry\"\u003eP27090\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGFB2; BSC-1 cell growth inhibitor; Cetermin; Glioblastoma-derived T-cell suppressor factor; G-TSF; MGC116892; Polyergin; TGF-beta2; TGF-beta-2; transforming growth factor beta-2\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTransforming growth factor beta 2 (TGF-β2) is a member of TGF-beta superfamily that shares a characteristic cysteine knot structure. Mice with TGF-β2 gene deletion show defects in development of cardiac, lung, craniofacial, limb, spinal column, eye, inner ear and urogenital systems. All TGF-β isoforms signal via the same heteromeric receptor complex, consisting of a ligand binding TGF-β receptor type II (TβR-II), and a TGF-β receptor type I (TβR-I). Signal transduction from the receptor to the nucleus is mediated via SMADs. TGF-β expression is found in cartilage, bone, teeth, muscle, heart, blood vessels, haematopoitic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e12.7 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e12 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 4mM HCl.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBiologically active. Please contact us to obtain bioactivity data.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in 4mM HCl.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915099963617,"sku":"BL-1912NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLZOAKwT1AAB-h8XnjI0971_5980b85c-6c4f-42b6-a028-7d776fb04c1f.jpg?v=1685853235"},{"product_id":"recombinant-human-gdf5-protein-bl-1968np","title":"Recombinant Human GDF-5 Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Growth\/Differentiation Factor 5 is produced by our E.coli expression system and the target gene encoding Ala382-Arg501 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP43026\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGrowth\/differentiation factor 5; GDF-5; Bone morphogenetic protein 14; BMP-14; Cartilage-derived morphogenetic protein 1; CDMP-1; Lipopolysaccharide-associated protein 4; LAP-4; LPS-associated protein 4; Radotermin; CDMP1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGrowth Differentiation Factor 5(GDF-5, BMP-14) is a member of the BMP family of TGFβ superfamily proteins. Human GDF-5, -6, and -7 are a defined subgroup of the BMP family. GDF-5 is synthesized as a homodimeric precursor protein consisting of a 354 amino acid (aa) Nterminal proregion and a 120 aa C-terminal mature peptide. Mature human GDF-5 shares 99% aa sequence identity with both mature mouse and rat GDF-5. GDF-5 signaling is mediated by formation of a heterodimeric complex consisting of a type 1 (BMPR-IB) and a type II (BMPR-IIor Activin RII) serine\/threonine kinase receptor which results in the phosphorylation and activation of cytosolic Smad proteins (Smad1, 5, and 8). GDF-5 is involved in multiple developmental processes including limb generation, cartilage development, joint formation, bone morphogenesis, cell survival, and neuritogenesis. Inhibition of GDF-5 expression or alteration of its signaling can facilitate the development of osteoarthritis.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13.7 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e15 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 4mM HCl.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in 4mM HCl.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGrowth factor involved in bone and cartilage formation. During cartilage development regulates differentiation of chondrogenic tissue through two pathways. Firstly, positively regulates differentiation of chondrogenic tissue through its binding of high affinity with BMPR1B and of less affinity with BMPR1A, leading to induction of SMAD1-SMAD5-SMAD8 complex phosphorylation and then SMAD protein signaling transduction. Secondly, negatively regulates chondrogenic differentiation through its interaction with NOG. Required to prevent excessive muscle loss upon denervation. This function requires SMAD4 and is mediated by phosphorylated SMAD1\/5\/8. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted. Cell membrane.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            4220           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            112600           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:8200           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000363489           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30044130            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            study shows that there exists a relationship between GDF5 (SNP rs143383) and Developmental dysplasia of the hip (DDH) in our population. Second, we found for the first time that the genotype TT and the T allele were overly expressed in the patients and the fathers. More studies on the confirmation of this genetic marker for DDH are called for.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29797005            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Two Pakistani families with sequence variants in GDF5 and TRPS1 causing brachydactyly type C and tricho-rhino-phalangeal syndrome type III are described.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29436063            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The dysfunctional gene GDF5 was successfully corrected in adipose tissue-derived mesenchymal stem cells using a pair of transcription activatorlike effector nucleases.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29393424            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            No association has been found between GDF5 +104 T\/C promoter polymorphism and osteoarthritis in the Eastern Turkey population.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28886316            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of the current study revealed that SNP rs143383 of GDF5 is a compelling risk factor for knee OA [Osteoarthritis] and that GDF5 has an etiological effect on the development of OA [Osteoarthritis].            \u003ca rel=\"nofollow\"\u003e             PMID:                        29056119            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A Study of IL-1beta, MMP-3, TGF-beta1, and GDF5 Polymorphisms and Their Association with Primary Frozen Shoulder in a Chinese Han Population            \u003ca rel=\"nofollow\"\u003e             PMID:                        28676856            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BMP-14 rs143383 polymorphism reduced the susceptibility to knee osteoarthritis (OA) and hand OA not only in total analysis but also in subgroup analysis; BMP-14 rs143383 polymorphism may be a protective factor against OA occurrence            \u003ca rel=\"nofollow\"\u003e             PMID:                        29049177            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The structure of Grem2-GDF5 complex has revealed a number of key findings for DAN-family mediated BMP2 inhibition.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27524626            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-615-3p negatively regulates the osteogenic differentiation of hLF cells through post-transcriptionally suppressing osteogenic regulators GDF5 and FOXO1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28460412            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            p38, c-jun, and NFkappaB pathways activated during intervertebral disc degeneration by IL-1beta but not GDF-5            \u003ca rel=\"nofollow\"\u003e             PMID:                        27391542            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF5 elicited significant (p \u0026lt; 0.05) changes in the expression of anabolic, catabolic and hypertrophic genes with several consistent effects in healthy donors and in OA patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        28481944            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF5 was up regulated in patients after chronic rhinosinusitis developing osteitis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27888647            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Titanium (Ti) surface modification with the combination of hBMP-2 and hGDF-5 for the two growth factor-coated Ti implants can improve the clinical properties of implants for orthopedic and dental applications.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28124978            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            he large array of modular enhancers for Gdf5 provide a new foundation for studying the spatial specificity of joint patterning in vertebrates, as well as new candidates for regulatory regions that may also influence osteoarthritis risk in human population            \u003ca rel=\"nofollow\"\u003e             PMID:                        27902701            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The purpose of this study is to investigate the immunohistochemical expression of cytokeratin 18 (CK18) and the reactivity to GDF5 (CDMP-1), called the morphogenetic protein-1, cartilage-derived, in lingual squamous cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27151703            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            homozygous sequence variants in the GDF5 gene underlie acromesomelic dysplasia type-grebe in consanguineous families            \u003ca rel=\"nofollow\"\u003e             PMID:                        27577507            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The prevention of IL-1Beta-induced nucleus pulposus extracellular matrix degeneration by miR-7 silencing was attenuated by GDF5 siRNA.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27583982            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mutations in three genes (GDF5, NPR2, BMPR1B) have been reported to cause different forms of acromesomelic dysplasia            \u003ca rel=\"nofollow\"\u003e             PMID:                        26926249            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we demonstrate that the transforming growth factor-beta1 and the growth differentiation factor 5 synergistically drive the nucleopulpogenic differentiation process. The commitment of the hASCs was robust and highly specific as attested by the expression of NP-related genes characteristic of young healthy human NP cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        26661057            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The data suggest that Ad-GDF-5 gene therapy is a potential treatment for IDD, which restores the functions of degenerative intervertebral disc through enhancing the ECM production of human NP cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26739524            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            An association of SNP in GDF5 with temporomandibular joint osteoarthritis in female Han Chinese.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25757091            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results demonstrate that SNP rs143383 of GDF5 is a compelling risk factor for both knee and hand osteoarthritis (OA) and provide further support for GDF5 in the etiology of OA [meta-analysis]            \u003ca rel=\"nofollow\"\u003e             PMID:                        25894512            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Two novel homozygous missense mutations in the GDF5 gene cause brachydactyly type C.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25820810            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our results showed that GDF-5 and BMPRII expressed both in normal and degenerated intervertebral disc tissues, and GDF-5 might have an inhibition effect on degenerated lumbar intervertebral discs            \u003ca rel=\"nofollow\"\u003e             PMID:                        25755766            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This meta-analysis finds that the C allele and CC genotype of the GDF5 gene are protective for knee osteoarthritis susceptibility.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25467786            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our results revealed that the GDF5 SNP was associated with susceptibility to the meniscus injury and postoperative function recovery in Chinese male soldiers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24227118            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            missense mutations p.T201P and p.L263P interfere with the protein structure and thereby reduce the amount of fully processed, biologically active GDF5, finally causing the clinical loss of function phenotype.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25092592            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The proregion is stabilized by an intramolecular disulfide bond. The isolated proregion folds independently of the mature domain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25174448            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Growth differentiation factor 5 and canonical Wnt signaling may contribute to molecular mechanisms of osteoarthritis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24561281            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results suggest that obesity leads to upregulation of GDF5 expression responsible for the promotion of brown adipogenesis through a mechanism relevant to activation of the NF-kappaB pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25223801            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results suggested that GDF5 polymorphism is associated with susceptibility to symptomatic lumbar disc herniation in Chinese Han population and type II collagen in the nucleus pulposus may be a factor in susceptibility to symptomatic lumbar disc herniation            \u003ca rel=\"nofollow\"\u003e             PMID:                        24105021            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Osteoarthritis chondrocytes do not respond in a predictable manner to culture with exogenous GDF5.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24466161            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High GDF5 expression is associated with osteoarthritis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24861163            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The expression of growth differentiation factor 5 (GDF5) and aggrecan in 15 cases of salivary gland pleomorphic adenomas, was investigated.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24398992            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            established an association between two SNPs (rs224332 and rs224333) of GDF5 and DDH development in a female Chinese population.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24114442            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In vitro findings suggest that the degenerating disc milieu, with high proinflammatory cytokine levels, may limit expression of GDF-5, resulting in limited regenerative capacity of the intact disc.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24582800            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These novel insights into the biology of GDF5 might also provide further clues on the pathophysiology of OA.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24098149            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The novel missense mutation p.Leu176Pro causes impaired secretion of GDF5 in Brachydactyly type C and mild Grebe type chondrodyslplasia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23812741            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF5 is the only osteoarthritis susceptibility gene so far identified with definite evidence.[Review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        24003854            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Overall, a statistically significant association was found between the +104T\/C polymorphism of GDF5 and risk of knee osteoarthritis            \u003ca rel=\"nofollow\"\u003e             PMID:                        23151597            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF5 harbors a C\/A transversion located -41 bp relative to the transcription start site that leads to increased gene expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22929025            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF5 polymorphisms are associated with susceptibility to low back pain during military training in Chinese soldiers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23725396            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In conclusion, the rs143383 variant was not found to associate with the risk of ACL rupture.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23090674            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we have identified four trans-acting factors that are binding to GDF5, three of which are modulating GDF5 expression via the OA susceptibility locus rs143383.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23825960            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Although the effect size of the association between OA and GDF5 is small, there is suggestive evidence for an association.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23423687            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF5 regulates TGF-beta-dependent angiogenesis in breast carcinoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23226264            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Growth differentiation factor 5 modulation of chondrogenesis of self-assembled constructs involves gap junction-mediated intercellular communication.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23121099            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            analysis of positive selection on the osteoarthritis-risk and decreased-height associated variants at the GDF5 gene in East Asians            \u003ca rel=\"nofollow\"\u003e             PMID:                        22905146            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our findings in 5 population cohorts from Northern Europe indicate that a variant in the GDF5 gene is a risk factor for lumbar disc degeneration in women.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21360499            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915103863009,"sku":"BL-1968NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLaSAUYkUAAC0eDTeA9o589_72de51d5-4611-4287-8128-ccfd826e896b.jpg?v=1685853393"},{"product_id":"recombinant-human-fibronectin-ed-b-domain-protein-his-tag-avi-bl-1970np","title":"Biotinylated Human Fibronectin Protein (ED-B domain, N-Avi-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBiotinylated Recombinant Human Fibronectin is produced by our E.coli expression system and the target gene encoding Glu1266-Thr1356 is expressed with a Avi, 6His tag at the N-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP02751\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFibronectin; FN1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFibronectin is a high-molecular weight glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. Similar to integrins, fibronectin binds extracellular matrix components such as collagen, fibrin, and heparan sulfate proteoglycans. Fibronectin plays a major role in cell adhesion, growth, migration, and differentiation, and it is important for processes such as wound healing and embryonic development. Altered fibronectin expression, degradation, and organization has been associated with a number of pathologies, including cancer and fibrosis. Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13.4 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e15 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.; Binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted, extracellular space, extracellular matrix.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            3778           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            135600           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:2335           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30237127            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Depletion of FN1 by siRNA knockdown markedly reduced the invasive capacity of prostate cancer cells in vitro.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29391407            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Human IL-7 binds more strongly to stretched than to relaxed Fibronectin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28845674            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGFB1-mediated PI3K\/Akt and p38 MAP kinase dependent alternative splicing of fibronectin extra domain A in human podocyte culture has been reported.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29729706            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings of this study provide evidence highlighting the prominent role played by FN1 in stimulating glioma growth, invasion, and survival through the activation of the PI3K\/AKT signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30048971            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The simultaneous delivery of multiple proinflammatory payloads to the cancer site conferred protective immunity against subsequent tumor challenges. A fully human homolog of IL2-F8-TNF(mut), which retained selectivity similar to its murine counterpart when tested on human material, may open new clinical applications for the immunotherapy of cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28716814            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Under the same condition, p53 protein expression, but not mRNA expression, was reversed by MG132. Taken together, our data demonstrate that the level of FN expression is associated with the status and expression of p53 in breast cancer cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        28765903            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our study thus demonstrates the dual roles of PTHrP on TGF-b1 signaling and FN up-regulation for the first time in glomerular mesangial cells . These data also provided new insights to guide development of therapy for diabetic kidney disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        28954822            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data suggest that miR-200b regulates EMT of chemo-resistant breast cancer cells by targeting FN1. miR-200b-based therapy may be an effective strategy in treating advanced breast cancer patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28972876            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Identification of novel integrin-binding domain mutations in FN1 in patients with glomerulopathy with fibronectin deposits.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27056061            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fibronectin fragments (FNFr) function as matrikines driving the chemotactic affinity of prostate cancer cells via the alpha5beta1 integrin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27715399            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fn with its inactive compact structure requires unfolding to assemble into active fibrils. Shear stress could induce conformational changes of plasma Fn.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29470988            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            B. burgdorferi does not primarily target insoluble matrix Fn deposited on endothelial surfaces but, instead, recruits and induces polymerization of soluble plasma Fn (pFn), an abundant protein in blood plasma that is normally soluble and nonadhesive.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28396443            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR1271 inhibited glioma cell growth by targeting FN1, and a low level of miR1271 in glioma tumor tissues was associated with lower survival rates in patients with glioma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28535003            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There is a significant association between a positive fetal fibronectin result and underlying inflammatory pathology of the placenta, even more so than the recognized relationship with short cervical length.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28535404            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The article focuses on summarizing the many binding partners for fibronectin such as extracellular matrix proteins, growth factors, and synthetic binding partners with a particular interest in binding partners whose adhesiveness is impacted by the molecular conformation of the fibronectin fibers. (Review)            \u003ca rel=\"nofollow\"\u003e             PMID:                        27496349            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FN1 fibrils regulate TGFB1-induced epithelial-mesenchymal transition.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28109697            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Breast cancer cells alter the dynamics of stromal fibronectin-collagen interactions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27503584            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study suggested that high a1-antitrypsin (AAT)expression might be a negative prognostic marker for lung adenocarcinoma. AAT promoted lung adenocarcinoma metastasis, whose functional target may be fibronectin . Our findings provide new insight into the mechanisms of lung adenocarcinoma metastasis            \u003ca rel=\"nofollow\"\u003e             PMID:                        28440399            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show the expression of ED-B fibronectin was much higher in mesenchymal than prostate cancer cells even after the epithelial to mesenchymal transition. Epithelial to mesenchymal transition is a key step for tumor progression contributing to the metastatic spread. Therefore, circulating cancer cells could seed into the metastatic niche taking advantage from the ED-B fibronectin that secrete their own.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27902486            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Thrombomodulin (TM) promotes angiogenesis by enhancing cell adhesion, migration, and FAK activation through interaction with fibronectin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27602495            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            thyroid nodule stiffness is correlated with fibrosis and expression of Gal-3 and FN-1            \u003ca rel=\"nofollow\"\u003e             PMID:                        27809694            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EGF and TNFalpha cooperatively promoted the motility of HCC cells mainly through NF-kappaB\/p65 mediated synergistic induction of FN in vitro. These findings highlight the crosstalk between EGF and TNFalpha in promoting HCC, and provide potential targets for HCC prevention and treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28844984            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            analysis of FN in breast cancer reveals its role and diagnostic potential            \u003ca rel=\"nofollow\"\u003e             PMID:                        27250024            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RT-PCR together with Sanger sequencing verified the presence of the FN1-ALK fusion transcripts            \u003ca rel=\"nofollow\"\u003e             PMID:                        27469327            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fibronectin is readily modified by ONOOH at low (physiologically-relevant) molar ratios of oxidant to protein.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27396946            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The 45 kDa gelatin-binding domain of fibronectin is responsible for the binding to TGM2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27394141            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Proteomics study showed a strong association of FN1, A2M, C4BPA and CFB in molecular subtypes of breast cancer. The findings also revealed the altered level expressions of these selected proteins could classify BC subtypes through plasma and tissue based expression analysis            \u003ca rel=\"nofollow\"\u003e             PMID:                        27498393            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FN1\/CCL2 levels are elevated in the bronchoalveolar lavage fluid from pulmonary sarcoidosis patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27259755            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Cancer-associated fibroblasts organize the fibronectin matrix and promote directional prostate cancer cell migration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29021221            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FN1 mutations that cause defective fibronectin secretion are found in SMD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29100092            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FN1 overexpression is an important determinant of thyroid cancer aggressiveness.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27173027            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Thyroid hormone T3 induces fibronectin and HIF-1alpha synthesis via PI3K\/AKT signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28974422            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mutations in FN are associated with glomerulopathy, but when we studied mutant proteins, the single-nucleotide mutations had only minor effects on conformation and matrix assembly. The mutations may destabilize their FNIII domains or generate dimers of dimers by disulfide cross-linking.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28745050            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fibronectin and Hepatocyte Growth Factor were shown to be produced by lung fibroblasts and, furthermore, to enhance malignant pleural mesothelioma cell migration and invasion            \u003ca rel=\"nofollow\"\u003e             PMID:                        28476806            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study identifies four likely Tourette disorder risk genes with multiple de novo damaging variants in unrelated probands: WWC1 (WW and C2 domain containing 1), CELSR3 (Cadherin EGF LAG seven-pass G-type receptor 3), NIPBL (Nipped-B-like), and FN1 (fibronectin 1).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28472652            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            fibrillar fibronectin on this polymer, but not a globular conformation obtained on control polymers, promotes synergistic presentation of integrin-binding sites and bound bone morphogenetic protein 2 (BMP-2), which enhances mesenchymal stem cell osteogenesis in vitro and drives full regeneration of a nonhealing bone defect in vivo at low GF concentrations.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27574702            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Fn plays a critical role in inflammasome-activated cells by amplifying caspase-1 activation and inducing inflammatory cell death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27870323            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            If the expression of Capon is decreased, myeloma cells are adhered to fibronectin or bone marrow stromal cells (bone marrow mesenchymal stem cells). In addition, the sensitivity of the cell line to chemotherapeutic agents was reduced after silencing Capon in the myeloma cell line which was adhered to bone marrow mesenchymal stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28671047            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Protease sensitivity resulting from mutations in the Fn-binding sequence could lead to degradation of type I collagen, early embryonic lethality            \u003ca rel=\"nofollow\"\u003e             PMID:                        27799304            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            C-terminal truncation of transglutaminase 2 (TG2) reduces binding to the small intestinal extracellular matrix (ECM) despite retained fibronectin (FN)-binding capacity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27685605            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            analysis of novel functions for two fibronectin isoforms and the mediating receptors in osteoblast differentiation            \u003ca rel=\"nofollow\"\u003e             PMID:                        28325836            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In vitro binding assays with purified components reveal that Tie-integrin recognition is direct, and further demonstrate that the receptor binding domain of the Tie2 ligand Ang-1, but not the receptor binding domain of Ang-2, can independently associate with a5b1 or aVb3. cooperative Tie\/integrin interactions selectively stimulate ERK\/MAPK signaling in the presence of both Ang-1 and fibronectin            \u003ca rel=\"nofollow\"\u003e             PMID:                        27695111            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results directly implicate the heparin-binding sequence of the first type III repeat of fibrillar fibronectin (FNIII1) in realignment of stress fibers in HUVECs and, importantly, show that the matricryptic heparin-binding RWRPK sequence located in FNIII1 is required for the response.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27521419            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGFbeta elevated the expression of CamK IIbeta and CamK IIdelta, while siRNA silencing of those two subtypes significantly reduced TGFbeta-mediated expression of collagen A1 and fibronectin 1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28130256            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings suggest that the up-regulated level of EDA+ FN is associated with liver damage in nonalcoholic fatty liver disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28397039            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In vitro binding studies support a previously unreported two-state \"catch-clamp\" mechanism of Fn binding by CshA, in which the disordered N-terminal domain of CshA acts to \"catch\" Fn, via formation of a rapidly assembled but also readily dissociable pre-complex, enabling its neighboring ligand binding domain to tightly clamp the two polypeptides together.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27920201            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data add new evidence that thermodynamic stability correlates primarily with unfolding rate rather than folding rate. The study also has implications for the question of whether opening of FNIII domains contributes to the stretching of fibronectin matrix fibrils.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27909052            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A positive fFN was associate with preterm birth \u0026lt;32 weeks (15.6% versus 4.2%, p = 0.043), \u0026lt;35 weeks (37.5% versus 11.1%, p = 0.002), \u0026lt;37 weeks (65.6% versus 20.8%, p \u0026lt; 0.001), and earlier gestational ages at delivery (35.2 +\/- 3.9 versus 37.4 +\/- 2.9, p = 0.001).            \u003ca rel=\"nofollow\"\u003e             PMID:                        26782923            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FN1 plays a role in the development of cisplatin resistance in non-small cell lung cancer (NSCLC), possibly by modulation of beta-catenin signaling through interaction with integrin-beta1 in NSCLC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27207836            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"20μg","offer_id":43915101274337,"sku":"BL-1970NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLaSAQ_J2AABrq2VplBM138_ca09fe93-bd30-4d87-af4c-5f6eef0ee68e.jpg?v=1685853291"},{"product_id":"recombinant-mouse-opg-protein-his-tag-bl-1993np","title":"Recombinant Mouse OPG Protein (C-10His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Tumor Necrosis Factor Receptor Superfamily Member 11B is produced by our Mammalian expression system and the target gene encoding Glu22-Leu401 is expressed with a 10His tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"O08712\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/O08712\/entry\"\u003eO08712\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTumor necrosis factor receptor superfamily member 11B; Osteoclastogenesis inhibitory factor; Osteoprotegerin; Tnfrsf11b; Ocif; Opg\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eOsteoprotegerin (OPG, Tnfrsf11b) is a secreted protein that regulates bone density. OPG is widely expressed and constitutively released as a homodimer by mesenchymal stem cells, fibroblasts and endothelial cells. Regulation of its expression by estrogen, parathyroid hormone and cytokines is complex and changes with age. OPG acts as decoy receptor for TNFSF11\/RANKL and thereby neutralizes its function in osteoclastogenesis. TRAIL decreases the release of OPG from cells that express it, while OPG inhibits TRAIL-induced apoptosis. Expression of RANK L on the cell surface, and thus its ability to stimulate osteoclastogenesis, is regulated by OPG by intracellular and extracellular mechanisms. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. It may also play a role in preventing arterial calcification.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e45.1 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e50-65 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915103371489,"sku":"BL-1993NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLa2APJWjAACxLFiTyoA189_427b8767-63dd-48b4-9380-065f87741c13.jpg?v=1685853377"},{"product_id":"recombinant-human-shh-protein-bl-2024np","title":"Recombinant Human SHH Protein (C24II)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Sonic Hedgehog  is produced by our E.coli expression system and the target gene encoding Cys24-Gly197 (C24II) is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eQ15465\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSonic Hedgehog Protein; SHH; HHG-1; SHH\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSonic Hedgehog Homolog (SHH) belongs to a three-protein family called Hedgehog. The other two family members are Indian Hedgehog (IHH) and Desert Hedgehog (DHH). Hedgehog proteins are key signaling molecules in embryonic development. SHH is expressed in various embryonic tissues and plays critical roles in regulating the patterning of many systems, such as limbs and brain. SHH also plays an important role in adult, including the division of adult stem cells and the development of certain cancers and other diseases. Human SHH is expressed as a 45kDa precursor, and undergoes a series of processing during secretion. After the removal of the signal peptide, a protease within the C-terminal domain catalyzes the cleavage of SHH into a 20 kDa N-terminal signaling domain (SHH-N) and a 25 kDa C-terminal domain (SHH-C). SHH-N has the “all signaling” capability. SHH-N binds to the 12 pass transmembrane protein Patched (Ptc) on cell surface, which releases the repression of the activity of Smoothened (Smo), a G-protein coupled receptor, by Ptc.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e19.8 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e20 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe C-terminal part of the sonic hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein into two parts (ShhN and ShhC) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated ShhN. Both activities occur in the reticulum endoplasmic. Once cleaved, ShhC is degraded in the endoplasmic reticulum.; The dually lipidated sonic hedgehog protein N-product (ShhNp) is a morphogen which is essential for a variety of patterning events during development. Induces ventral cell fate in the neural tube and somites. Involved in the patterning of the anterior-posterior axis of the developing limb bud. Essential for axon guidance. Binds to the patched (PTCH1) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes. In the absence of SHH, PTCH1 represses the constitutive signaling activity of SMO.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eEndoplasmic reticulum membrane. Golgi apparatus membrane.; [Sonic hedgehog protein N-product]: Cell membrane; Lipid-anchor.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHedgehog family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            10848           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            135750           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:6469           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000297261           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28496132            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Disturbed SHH link between KIF7 and C5orf42 contributes to neurodevelopmental features characteristic of C5orf42-related ciliopathies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29321670            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Histone deacetylase 6 (HDAC6) inhibition enhanced glioma stem cells (GSCs) radiosensitivity via inactivating sonic hedgehog protein (SHH)\/glioma-associated oncogene homolog 1 (Gli1) pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29222038            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Blockade of the Shh signaling pathway could reduce cell proliferation and migration only in MDA-MB-231 cells. Hh pathway inhibitor-1 (HPI-1) increased the percentages of late apoptotic cells in MDA-MB-231 cells and early apoptotic cells in T2 cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        29734730            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Structure-guided mutational analysis shows that interaction between ShhN and Ptch1 is steroid-dependent.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29954986            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Protease nexin-1 prevents growth of human B cell lymphoma via inhibition of sonic hedgehog signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29483508            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH-related signaling pathway affects antineoplastic drug resistance in cultured glioma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29313231            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH is expressed in cilia in the airway epithelial cells.SHH may mediate noncanonical hedgehog signaling through motile cilia to dampen respiratory defenses.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29358407            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SHH expression is associated with radioresistance in esophageal adenocarcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29715275            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Identify SMO-dependent Shh signalling as a specific process for the activation of adventitial fibroblasts and the subsequent proliferation of smooth muscle cells and neointima formation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29088375            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In conclusion, our data suggest that overexpression of the Hedgehog components SHH, GLI2 and FOXA2 might be used as markers of an aggressive hemangioma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28370639            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings showed the upexpression of sonic hedgehog and vascular endothelial growth factor with co-localization in varicocele veins which imply that the reducing hypoxia or using sonic hedgehog antagonists may be helpful for this vascular disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26867642            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Shh and Gli1 expression were associated with lymph node metastasis, TNM stage and tumor recurrence, suggesting Shh and Gli1 protein could become the valuable biomarker in evaluating the lymph node metastasis in oral squamous cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28886265            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Epithelial-mesenchymal transition programs promote basal mammary stem cell and tumor-initiating cell stemness by inducing primary ciliogenesis and Hedgehog signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29158396            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Case Report: medullablastoma with activated SHH expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29517209            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NAFLD progression is usually accompanied by activation of the Sonic hedgehog (SHH) pathway leading to fibrous buildup (scar tissue) and inflammation of the liver tissue. For the first time patients with holoprosencephaly, a disease caused by SHH signaling mutations, are shown to have increased liver steatosis independent of obesity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28645738            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Gpr161 is a critical factor in the basal suppression machinery of Shh signaling, neural tube morphogenesis and closure. (Review)            \u003ca rel=\"nofollow\"\u003e             PMID:                        27731925            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Oncogenic activation of SHH is associated with Rubinstein-Taybi Syndrome and Medulloblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29551561            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results showed that Shh and Gli1 were upregulated in prostate cancer tissues and were targeted by a phytogenic neoplastic compound carnosol.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28886322            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Hh signaling activation might reflect aggressive tumoral behavior, since high epithelial GLI2 expression positively correlates with a higher pathological Gleason score. Moreover, higher epithelial GLI3 expression is an independent marker of a more favorable prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28877722            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPT2 reduced alpha-ketoglutarate level in cells leading to the inhibition of proline hydroxylase 2 (PHD2) activity involved in the regulation of HIF1alpha stability. Accumulation of HIF1alpha, resulting from GPT2-alpha-ketoglutarate-PHD2 axis, constitutively activates sonic hedgehog (Shh) signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28839461            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show SHH proteolysis is under the mechanism of Scube2 which is enriched at the surface of Shh-producing cells by heparan sulfate proteoglycans.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27199253            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            influences sweat gland differentiation of stem cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27120089            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            during Hedgehog signaling, ligand binding inhibits Patched by trapping it in an inactive conformation, a mechanism that explains the dramatically reduced activity of oncogenic Patched1 mutants.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27647915            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In an in vitro model of LPS inflammation of the blood-brain barrier, sonic hedgehog signaling was activated by Wip1 overexpression and inhibited by silencing. Wip1 may protect the BBB against LPS damage via SHH signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29128669            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the effect gene of the Shh pathway, gli1, was found to have a reduced level of expression along with a decreased expression of gli2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26446020            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH can promote cell growth and cell osteoblastic\/cementoblastic differentiation via BMP pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        27289556            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings suggest that oral squamous cell carcinoma (OSCC)derived sonic hedgehog protein (SHH) stimulates angiogenesis at the tumor invasive front.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29187450            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of SHH and GLI1 may be useful prognostic markers of Merkel cell carcinoma because increased expression was associated with better prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28551328            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SHH expression is associated with esophageal squamous cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29054489            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studies suggest significance of other signaling aside from hedgehog in the pathogenesis of basal cell carcinoma (BCC) of the skin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28574612            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Gorlin syndrome-derived induced pluripotent stem cells (iPSCs) expressed lower basal levels than control iPSCs of the genes encoding the Hh ligands Indian Hedgehog (IHH) and Sonic Hedgehog (SHH).            \u003ca rel=\"nofollow\"\u003e             PMID:                        29088246            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH activation is associated with Rhabdomyosarcoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28881358            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studies suggest that embryonic signaling pathways, the likes of Notch, Wnt, and Hedgehog and tumor marker Oct-4 offer targets for cascade-specific molecular inhibition as they are fundamental to (cancer and normal) stem cell maintenance and growth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27730468            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Methylation at K436 and K595 respectively by Set7 increases the stability and DNA binding ability of Gli3, resulting in an enhancement of Shh signaling activation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27146893            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Altogether, these data suggested that curcumin inhibited the activities of BCSCs through suppressing Shh pathway, which might be an effective chemopreventive agent for bladder cancer intervention.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28870814            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SHH expression is associated with Small Cell Lung Cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28870922            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Accumulating evidence suggest that cytochrome P450 (CYP26), the primary retinoid-inactivating enzyme, plays a critical role in the integration of two neoplastic molecular programs: the retinoid metabolism and Hedgehog pathways. (Review)            \u003ca rel=\"nofollow\"\u003e             PMID:                        28754309            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CHSY1 overexpression in HCC contributes to the malignant behavior of hepatocellular carcinoma cells via activation of the hedgehog signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28652022            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We found a novel 7q36.3 duplication involving 2 genes (SHH and RBM33) in a patient with complete corpus callosum agenesis (Figure), moderate learning difficulties, and macrocephaly            \u003ca rel=\"nofollow\"\u003e             PMID:                        28284480            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study showed that SHH expression was significantly high among breast cancer patients with advanced tumor grade, stage, nodal involvement and metastasis and this expression strongly correlated with proliferation marker.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28739739            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This suggests an important cross-talk between SHH and WIP1 pathways that accelerates tumorigenesis and supports WIP1 inhibition as a potential treatment strategy for MB.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27086929            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            YB-1 is induced by Shh in CGNPs            \u003ca rel=\"nofollow\"\u003e             PMID:                        26725322            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH siRNA synergistically enhanced cytotoxicity induced by itraconazole in MCF-7 cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27810405            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Hedgehog pathway activation in T-cell acute lymphoblastic leukemia predicts response to SMO and GLI1 inhibitors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27694322            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that negative feedback mediated by GLI3 (GLI-Kruppel family member) acts to finely tune SHH (sonic hedgehog) signaling. During medulloblastoma (MB) formation, nerve tissue cells appear to express nestin which hyperactivates SHH signaling by abolishing negative feedback by GLI3. Restoration of intrinsic negative feedback by repressing nestin expression represents a promising approach to treat MB. [REVIEW]            \u003ca rel=\"nofollow\"\u003e             PMID:                        28389227            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The study reveals several novel individual and repetitive mutations of SHH gene in Gallbladder Cancer and Cholelithiasis samples that may be used as diagnostic markers for gallbladder carcinogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28058596            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that agedunin induces its anti-metastatic effect through inhibition of sonic hedgehog protein [SHH] signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26988754            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings suggest that Usp7 is important for MB cell proliferation and metastasis by activating Shh pathway, and is a putative therapeutic target for MBs            \u003ca rel=\"nofollow\"\u003e             PMID:                        28137592            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            importance of MAOA for initiating the pre-metastatic niche in stromal cells and promoting PCa metastasis to bone and visceral organs, mediated by activation of paracrine Shh-IL6-RANKL signaling underlying tumor-stromal interactions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28292438            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915103895777,"sku":"BL-2024NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLSaAZzGIAACh79rcJzw823_1d4b0248-4e45-4ea8-91b5-ff5d1d6d7bab.jpg?v=1685853394"},{"product_id":"recombinant-human-shh-protein-bl-2025np","title":"Recombinant Human SHH Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Sonic Hedgehog is produced by our E.coli expression system and the target gene encoding Cys24-Gly197 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eQ15465\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSonic Hedgehog Protein; SHH; HHG-1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSonic Hedgehog Homolog (SHH) belongs to a three-protein family called hedgehog. The other two family members are Indian Hedgehog (IHH) and Desert Hedgehog (DHH). Hedgehog proteins are key signaling molecules in embryonic development. SHH is expressed in various embryonic tissues and plays critical roles in regulating the patterning of many systems, such as limbs and brain. SHH also plays an important role in adult, including the division of adult stem cells and the development of certain cancers and other diseases. Human SHH is expressed as a 45kDa precursor, and undergoes a series of processing during secretion. After the removal of the signal peptide, a protease within the C-terminal domain catalyzes the cleavage of SHH into a 20 kDa N-terminal signaling domain (SHH-N) and a 25 kDa C-terminal domain (SHH-C). SHH-N has the “all signaling” capability. SHH-N binds to the 12 pass transmembrane protein Patched (Ptc) on cell surface, which releases the repression of the activity of Smoothened (Smo), a G-protein coupled receptor, by Ptc.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e19.69 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e19 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 100mM NaCl, 1mM DTT, pH 7.5.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe C-terminal part of the sonic hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein into two parts (ShhN and ShhC) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated ShhN. Both activities occur in the reticulum endoplasmic. Once cleaved, ShhC is degraded in the endoplasmic reticulum.; The dually lipidated sonic hedgehog protein N-product (ShhNp) is a morphogen which is essential for a variety of patterning events during development. Induces ventral cell fate in the neural tube and somites. Involved in the patterning of the anterior-posterior axis of the developing limb bud. Essential for axon guidance. Binds to the patched (PTCH1) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes. In the absence of SHH, PTCH1 represses the constitutive signaling activity of SMO.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eEndoplasmic reticulum membrane. Golgi apparatus membrane.; [Sonic hedgehog protein N-product]: Cell membrane; Lipid-anchor.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHedgehog family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            10848           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            135750           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:6469           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000297261           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28496132            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Disturbed SHH link between KIF7 and C5orf42 contributes to neurodevelopmental features characteristic of C5orf42-related ciliopathies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29321670            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Histone deacetylase 6 (HDAC6) inhibition enhanced glioma stem cells (GSCs) radiosensitivity via inactivating sonic hedgehog protein (SHH)\/glioma-associated oncogene homolog 1 (Gli1) pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29222038            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Blockade of the Shh signaling pathway could reduce cell proliferation and migration only in MDA-MB-231 cells. Hh pathway inhibitor-1 (HPI-1) increased the percentages of late apoptotic cells in MDA-MB-231 cells and early apoptotic cells in T2 cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        29734730            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Structure-guided mutational analysis shows that interaction between ShhN and Ptch1 is steroid-dependent.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29954986            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Protease nexin-1 prevents growth of human B cell lymphoma via inhibition of sonic hedgehog signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29483508            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH-related signaling pathway affects antineoplastic drug resistance in cultured glioma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29313231            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH is expressed in cilia in the airway epithelial cells.SHH may mediate noncanonical hedgehog signaling through motile cilia to dampen respiratory defenses.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29358407            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SHH expression is associated with radioresistance in esophageal adenocarcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29715275            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Identify SMO-dependent Shh signalling as a specific process for the activation of adventitial fibroblasts and the subsequent proliferation of smooth muscle cells and neointima formation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29088375            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In conclusion, our data suggest that overexpression of the Hedgehog components SHH, GLI2 and FOXA2 might be used as markers of an aggressive hemangioma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28370639            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings showed the upexpression of sonic hedgehog and vascular endothelial growth factor with co-localization in varicocele veins which imply that the reducing hypoxia or using sonic hedgehog antagonists may be helpful for this vascular disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26867642            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Shh and Gli1 expression were associated with lymph node metastasis, TNM stage and tumor recurrence, suggesting Shh and Gli1 protein could become the valuable biomarker in evaluating the lymph node metastasis in oral squamous cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28886265            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Epithelial-mesenchymal transition programs promote basal mammary stem cell and tumor-initiating cell stemness by inducing primary ciliogenesis and Hedgehog signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29158396            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Case Report: medullablastoma with activated SHH expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29517209            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            NAFLD progression is usually accompanied by activation of the Sonic hedgehog (SHH) pathway leading to fibrous buildup (scar tissue) and inflammation of the liver tissue. For the first time patients with holoprosencephaly, a disease caused by SHH signaling mutations, are shown to have increased liver steatosis independent of obesity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28645738            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Gpr161 is a critical factor in the basal suppression machinery of Shh signaling, neural tube morphogenesis and closure. (Review)            \u003ca rel=\"nofollow\"\u003e             PMID:                        27731925            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Oncogenic activation of SHH is associated with Rubinstein-Taybi Syndrome and Medulloblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29551561            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results showed that Shh and Gli1 were upregulated in prostate cancer tissues and were targeted by a phytogenic neoplastic compound carnosol.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28886322            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Hh signaling activation might reflect aggressive tumoral behavior, since high epithelial GLI2 expression positively correlates with a higher pathological Gleason score. Moreover, higher epithelial GLI3 expression is an independent marker of a more favorable prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28877722            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPT2 reduced alpha-ketoglutarate level in cells leading to the inhibition of proline hydroxylase 2 (PHD2) activity involved in the regulation of HIF1alpha stability. Accumulation of HIF1alpha, resulting from GPT2-alpha-ketoglutarate-PHD2 axis, constitutively activates sonic hedgehog (Shh) signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28839461            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show SHH proteolysis is under the mechanism of Scube2 which is enriched at the surface of Shh-producing cells by heparan sulfate proteoglycans.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27199253            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            influences sweat gland differentiation of stem cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27120089            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            during Hedgehog signaling, ligand binding inhibits Patched by trapping it in an inactive conformation, a mechanism that explains the dramatically reduced activity of oncogenic Patched1 mutants.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27647915            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In an in vitro model of LPS inflammation of the blood-brain barrier, sonic hedgehog signaling was activated by Wip1 overexpression and inhibited by silencing. Wip1 may protect the BBB against LPS damage via SHH signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29128669            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the effect gene of the Shh pathway, gli1, was found to have a reduced level of expression along with a decreased expression of gli2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26446020            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH can promote cell growth and cell osteoblastic\/cementoblastic differentiation via BMP pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        27289556            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings suggest that oral squamous cell carcinoma (OSCC)derived sonic hedgehog protein (SHH) stimulates angiogenesis at the tumor invasive front.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29187450            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of SHH and GLI1 may be useful prognostic markers of Merkel cell carcinoma because increased expression was associated with better prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28551328            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SHH expression is associated with esophageal squamous cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29054489            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studies suggest significance of other signaling aside from hedgehog in the pathogenesis of basal cell carcinoma (BCC) of the skin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28574612            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Gorlin syndrome-derived induced pluripotent stem cells (iPSCs) expressed lower basal levels than control iPSCs of the genes encoding the Hh ligands Indian Hedgehog (IHH) and Sonic Hedgehog (SHH).            \u003ca rel=\"nofollow\"\u003e             PMID:                        29088246            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH activation is associated with Rhabdomyosarcoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28881358            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studies suggest that embryonic signaling pathways, the likes of Notch, Wnt, and Hedgehog and tumor marker Oct-4 offer targets for cascade-specific molecular inhibition as they are fundamental to (cancer and normal) stem cell maintenance and growth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27730468            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Methylation at K436 and K595 respectively by Set7 increases the stability and DNA binding ability of Gli3, resulting in an enhancement of Shh signaling activation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27146893            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Altogether, these data suggested that curcumin inhibited the activities of BCSCs through suppressing Shh pathway, which might be an effective chemopreventive agent for bladder cancer intervention.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28870814            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SHH expression is associated with Small Cell Lung Cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28870922            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Accumulating evidence suggest that cytochrome P450 (CYP26), the primary retinoid-inactivating enzyme, plays a critical role in the integration of two neoplastic molecular programs: the retinoid metabolism and Hedgehog pathways. (Review)            \u003ca rel=\"nofollow\"\u003e             PMID:                        28754309            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CHSY1 overexpression in HCC contributes to the malignant behavior of hepatocellular carcinoma cells via activation of the hedgehog signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28652022            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We found a novel 7q36.3 duplication involving 2 genes (SHH and RBM33) in a patient with complete corpus callosum agenesis (Figure), moderate learning difficulties, and macrocephaly            \u003ca rel=\"nofollow\"\u003e             PMID:                        28284480            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study showed that SHH expression was significantly high among breast cancer patients with advanced tumor grade, stage, nodal involvement and metastasis and this expression strongly correlated with proliferation marker.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28739739            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This suggests an important cross-talk between SHH and WIP1 pathways that accelerates tumorigenesis and supports WIP1 inhibition as a potential treatment strategy for MB.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27086929            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            YB-1 is induced by Shh in CGNPs            \u003ca rel=\"nofollow\"\u003e             PMID:                        26725322            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH siRNA synergistically enhanced cytotoxicity induced by itraconazole in MCF-7 cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27810405            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Hedgehog pathway activation in T-cell acute lymphoblastic leukemia predicts response to SMO and GLI1 inhibitors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27694322            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that negative feedback mediated by GLI3 (GLI-Kruppel family member) acts to finely tune SHH (sonic hedgehog) signaling. During medulloblastoma (MB) formation, nerve tissue cells appear to express nestin which hyperactivates SHH signaling by abolishing negative feedback by GLI3. Restoration of intrinsic negative feedback by repressing nestin expression represents a promising approach to treat MB. [REVIEW]            \u003ca rel=\"nofollow\"\u003e             PMID:                        28389227            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The study reveals several novel individual and repetitive mutations of SHH gene in Gallbladder Cancer and Cholelithiasis samples that may be used as diagnostic markers for gallbladder carcinogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28058596            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that agedunin induces its anti-metastatic effect through inhibition of sonic hedgehog protein [SHH] signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26988754            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings suggest that Usp7 is important for MB cell proliferation and metastasis by activating Shh pathway, and is a putative therapeutic target for MBs            \u003ca rel=\"nofollow\"\u003e             PMID:                        28137592            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            importance of MAOA for initiating the pre-metastatic niche in stromal cells and promoting PCa metastasis to bone and visceral organs, mediated by activation of paracrine Shh-IL6-RANKL signaling underlying tumor-stromal interactions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28292438            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915100029153,"sku":"BL-2025NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLSmAM6-HAACkUCcLxgI972_a51eaae1-ee0a-47e6-ba85-dc61c67546f8.jpg?v=1685853238"},{"product_id":"recombinant-human-gdnf-protein-bl-2026np","title":"Recombinant Human GDNF Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Glial Cell Line-Derived Neurotrophic Factor is produced by our E.coli expression system and the target gene encoding Ser78-Ile211 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP39905\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGlial Cell Line-Derived Neurotrophic Factor; hGDNF; Astrocyte-Derived Trophic Factor; ATF; GDNF\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGlial Cell Line-Derived Neurotrophic Factor (GDNF) is a disulfide-linked homodimeric glycoprotein that belongs to the TGF-β superfamily. It has been shown to promote the survival of various neuronal subpopulations in both the central as well as the peripheral nervous systems at different stages of their development. Human GDNF cDNA encodes a 211 amino acid residue prepropeptide that is processed to yield a dimeric protein. Mature human GDNF was predicted to contain two 134 amino acid residue subunits. Cells known to express GDNF include Sertoli cells, type 1 astrocytes, Schwann cells, neurons, pinealocytes and skeletal muscle cells. Mutations in this gene may be associated with Hirschsprung disease.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e15.1 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e17 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 1 EU\/µg as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNeurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGF-beta family, GDNF subfamily\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            4232           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            171300           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:2668           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000409007           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30176167            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            the inverse relationship between GFRalpha1 and C-Ret, as knocking down C-Ret led to increases in GFRalpha1 expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29018141            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study showed that the GDNF levels in preterm newborns were higher in cord blood and lower in CSF as compared to term newborns.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29031644            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We thus confirmed the role of GDNF as an adaptive survival factor, and its alteration appears to have a key role in nephrocalcinosis. We also discovered that, in GDNF-silenced cells, death occurs in a programmed but caspase-independent manner.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29208768            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results suggested that while alterations at 5:37812784 T \u0026gt; A and 5:37812782 T \u0026gt; A sites related with higher GDNF serum levels and less functionality, and alterations at rs62360370 G \u0026gt; A 3'UTR SNP of GDNF associated with higher severity and lower functionality. However, alterations at both rs2075680 C \u0026gt; A and rs79669773 T \u0026gt; C SNPs affect neither GDNF serum levels nor severity and functionality in bipolar disorder.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28891527            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            To our knowledge, this is the first study which correlates GDNF levels with metabolic parameters. Our results show no differences in GDNF serum level between schizophrenia, a first depressive episode, and healthy controls. GDNF serum level did not correlate with metabolic parameters except for total cholesterol in depression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28689143            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggest an interaction between NGF, GDNF and MMP-9 during the transition to malignancy in prostate cancer (PC). Also this interaction may involve in regulating PC cell differentiation, tumor invasion, progression, and the agressiveness of PC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28237042            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study also demonstrates that the interaction between GDNF and proN-cadherin activates specific intracellular signaling pathways; furthermore, GDNF promoted the secretion of matrix metalloproteinase-9 (MMP-9), which degrades the ECM via proN-cadherin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28212546            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Protective effect of GDNF-engineered amniotic fluid-derived stem cells on the renal ischaemia reperfusion injury in vitro.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29114949            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDNF has a role in lower than expected motor development, but while IL-1beta and CXCL8\/IL-8 values were higher in the group with typical motor development among preterm neonates            \u003ca rel=\"nofollow\"\u003e             PMID:                        28553016            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings provide preliminary evidence that silencer II hypermethylation in the gdnf promoter II may underlie high gene transcription in high-grade glioma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26232065            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            there is a decrease in epidermal GDNF and GFRalpha-1 protein expression in normal human skin with ageing            \u003ca rel=\"nofollow\"\u003e             PMID:                        27346872            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In SOD1(G93A) spinal cords, we verified a strict correlation in the expression of the TNFalpha, TNFR1 and GDNF triad at different stages of disease progression. Yet, ablation of TNFR1 completely abolished GDNF rises in both SOD1(G93A) astrocytes and spinal cords, a condition that accelerated motor neuron degeneration and disease progression            \u003ca rel=\"nofollow\"\u003e             PMID:                        27288458            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In functional dyspepsia patients, duodenal expression of GDNF protein was significantly increased compared with controls. GDNF was localized in enteric glial cells, eosinophils, and epithelial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27718082            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Suppression of miR-383 may increase the therapeutic potential of human bone-marrow-derived MSCs in treating spinal cord injury via augmentation of GDNF protein levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28365701            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our results suggest that GDNF rs3096140 might be involved in the genetic background of smoking, independent of anxiety characteristics.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27994179            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            No correlations between the levels of serum neurotrophins and the severity of ADHD were observed. These results suggest that elevated serum GDNF and NTF3 levels may be related to ADHD in children.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27561780            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BDNF and GDNF interact with the 5-HT-system of the brain through feedback mechanisms engaged in autoregulation            \u003ca rel=\"nofollow\"\u003e             PMID:                        28320272            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study shows no correlation between GDNF rs884344 and rs3812047 polymorphisms and subjects with tinnitus.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27180191            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results demonstrate the pivotal role of GDNF as well as the PI3K\/Akt pathway, but not the MAPK pathway, in the prevention of diabetesinduced neuronal apoptosis in the hippocampus.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26549420            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Increased plasma levels of GDNF were found in untreated attention deficit hyperactivity disorder patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25753832            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDNF levels were lower in the ECT responders compared with pre-ECT levels            \u003ca rel=\"nofollow\"\u003e             PMID:                        25354171            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The GDNF polymorphism rs3096140 is associated with Tourette syndrome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26096985            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDNF levels were significantly higher in mania and lower in schizophrenia compared to healthy controls. BDNF levels were negatively correlated to illness severity scores in affective episodes            \u003ca rel=\"nofollow\"\u003e             PMID:                        25543333            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that glial cell-derived neurotrophic factor (GDNF) was down-regulated in the medullary sponge kidney (MSK) cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25692823            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Osteogenic features of MSCs from ossification of yellow ligament patients are promoted by un-methylated GDNF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25913759            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The glial cell line-derived neurotrophic factor(GDNF)-induced growth and differentiation of cultured enteric neurons is paralleled by increased expression of SNAP-25 and formation of synaptic vesicles reflecting enhanced synaptogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25655772            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            improvement in behavioral performance (open-field and grip-strength tests), as well as increased life-span was observed in rodents treated with NCAM-VEGF or NCAM-GDNF co-transfected cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        25619885            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate the glial cell derived neurotrophic factor (GDNF) signaling pathway as a potential target for improving responses to conventional genotoxic therapeutics.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25575823            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In major depressive disorder patients, serum GDNF levels were lower compared to controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24899094            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the PTX-sensitive alpha-subunit of G proteins, Go1 and Gi3, plays an important role in a monoamine-independent production of GDNF evoked by amitriptyline            \u003ca rel=\"nofollow\"\u003e             PMID:                        25869129            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results suggest that D2R activation induces a Gbetagamma- and extracellular signal-regulated kinase 1\/2-dependent increase in the level of Zif268, which functions to directly up-regulate the expression of GDNF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23373701            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            An increased risk of HD[Heroine Dependence] and depression was associated with rs2910709 T\/T genotype and rs884344 C allele, respectively, suggesting GDNF is a novel susceptibility gene for depression and HD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24022000            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            histone H3K9 hyperacetylation in promoter II of the gdnf gene might be one of the reasons for its abnormal high transcription in glioma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24619502            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study found association between single nucleotide polymorphisms in the regulatory sites of Glial Derived Neurotrophic Factor (GDNF) and bipolar disorder.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24997227            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Transgenic expression of human glial cell line-derived neurotrophic factor from integration-deficient lentiviral vectors is neuroprotective in a rodent model of Parkinson's disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24635742            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            No differences in plasma BDNF, NGF, NT3, NT4 and GDNF were found between autism spectrum disorders and control.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25275256            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDNF expression was upregulated upon radiation therapy in submandibular glands.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25036711            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This hypothesis offers a dramatically different explanation for the etiology of sporadic Parkinson's disease as a manifestation of acquired resistance to GDNF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25448159            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            serum levels of GDNF may be an unsuitable biomarker for schizophrenia, although it may be associated with working memory in healthy controls and the pathophysiology of attention deficits in schizophrenia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24861509            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDNF is a novel candidate gene of anxiety.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24324616            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDNF increases the metastasis and migration of colon cancer cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        24165321            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Transgenic GDNF+\/- mice, not wild-type, show increased kidney glomerular damage with a low nephron number.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24247178            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings collectively demonstrate that GFRalpha1 released by nerves enhances perineural invasion through GDNF-RET signaling and that GFRalpha1 expression by cancer cells enhances but is not required for it.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24778213            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Changes in transcriptional factor binding capacity are due to changes in promoter region methylation and might be the underlying mechanism for aberrantly high gdnf expression in glioma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23606280            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Glial cell-derived neurotrophic factor has a regulatory effect on cell migration in oral squamous cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24070603            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The novelty of the study lies in its large number of exclusively adolescent depression patients showing significant reduction of BDNF, NGF and GDNF serum levels as compared to controls. A gender bias with much reduction in female has also been recorded.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23769609            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            inducible lentivirus-mediated hGDNF gene delivery system may provide useful tools for basic research on gene therapy for chronic neurological disorders such as Parkinson's disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        23717608            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate GDNF-RET signaling as a rational therapeutic target to combat or delay the onset of aromatase inhibitor resistance in breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23650283            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Human GDNF protected crayfish neurons and glia from photodynamic injury.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22847529            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915098357985,"sku":"BL-2026NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLTqAf67ZAACzRLwg0Io705_e7bd0637-a289-407e-a8d1-ed68f8b7f680.jpg?v=1685853175"},{"product_id":"recombinant-mouse-shh-protein-bl-2030np","title":"Recombinant Mouse SHH Protein (C25II)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Sonic Hedgehog is produced by our E.coli expression system and the target gene encoding Cys25-Gly198(Cys25Ile-Ile) is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eQ62226\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSonic Hedgehog Protein; SHH; HHG-1; SHH\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMouse Sonic Hedgehog Homolog (SHH) belongs to a three-protein family called Hedgehog. The other two family members are Indian Hedgehog (IHH) and Desert Hedgehog (DHH). Hedgehog proteins are key signaling molecules in embryonic development. SHH is expressed in various embryonic tissues and plays critical roles in regulating the patterning of many systems, such as limbs and brain. SHH also plays an important role in adult, including the division of adult stem cells and the development of certain cancers and other diseases.Mouse Shh is synthesized as a 437 aa precursor that contains a 24 aa signal sequence and a 413 aa mature region. The mature region is autocatalytically processed into a nonglycosylated, 20 kDa, 174 aa N­terminal fragment (Shh­N), and a catalytic­processing,glycosylated, 34 kDa, 239 aa C­terminal fragment. The 20 kDa Shh­N fragment is the core of the active hedgehog molecule. Mouse Shh­N is 99%, 98%, and 100% aa identical to human, rat and gerbil Shh­N, respectively.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e19.8 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e18-20  KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 1mM DTT, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe C-terminal part of the sonic hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein into two parts (ShhN and ShhC) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated ShhN. Both activities occur in the reticulum endoplasmic. Once cleaved, ShhC is degraded in the endoplasmic reticulum.; The dually lipidated sonic hedgehog protein N-product (ShhNp) is a morphogen which is essential for a variety of patterning events during development. Induces ventral cell fate in the neural tube and somites. Involved in the patterning of the anterior-posterior axis of the developing limb bud. Essential for axon guidance. Binds to the patched (PTCH1) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes. In the absence of SHH, PTCH1 represses the constitutive signaling activity of SMO.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eEndoplasmic reticulum membrane. Golgi apparatus membrane.; [Sonic hedgehog protein N-product]: Cell membrane; Lipid-anchor.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHedgehog family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            mmu:20423           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            10090.ENSMUSP00000002708           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28547659            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            show that eliminating mouse MACS1 causes severe defects in laryngeal development, indicating that MACS1-directed Shh signalling is indispensable for respiratory organogenesis            \u003ca rel=\"nofollow\"\u003e             PMID:                        28155855            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results suggest distinct functions of tuberous sclerosis complex 1 protein (Tsc1) and tuberous sclerosis complex 2 protein (Tsc2) in cellular signaling as the two genes affect ciliary length control and sonic hedgehog protein signaling via different mechanisms.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29396625            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study indicated that Shh, Sfrp1, and Wnt5a collaborate to direct the pathfinding of descending 5-HT axons in the brainstem.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29196093            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data illustrate that persistent Hh signaling in the palatal epithelium contributes to the etiology and pathogenesis of submucous cleft palate through its interaction with a p63\/Irf6-dependent biological regulatory loop and through a p63-induced cell adhesion network.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29981310            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SOX2 functions downstream of HH signaling to regulate lingual epithelium homeostasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29945863            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SHH expression is associated with medulloblastoma formation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29378965            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Identify SMO-dependent Shh signalling as a specific process for the activation of adventitial fibroblasts and the subsequent proliferation of smooth muscle cells and neointima formation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29088375            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In the mutant Hammer toe (Hm) genome, a 150-kb noncoding DNA fragment from chromosome 14 is inserted into the region upstream of the Sonic hedgehog (Shh) promoter in chromosome 5. Two different regions are necessary for the syndactyly phenotype of Hm.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29255029            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that Sonic hedgehog (Shh), which encodes a secreted protein signal, is expressed in the sensory neurons, and that experimental ablation of neuronal Shh expression causes loss of taste receptor cells (TRCs).            \u003ca rel=\"nofollow\"\u003e             PMID:                        29279401            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Here by inducing expression of constitutively active Smoothened (SmoM2) or Gli2 (DeltaNGli2) in the adipocyte lineage of postnatal mice, the authors show that targeted activation of Hedgehog signaling suppresses high-fat-diet-induced obesity and improves whole-body glucose tolerance and insulin sensitivity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29205155            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data suggest a potential novel mechanism in which alterations in SHH variance during evolution may have driven changes in limb patterning and digit length.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28131983            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Epithelial-mesenchymal transition programs promote basal mammary stem cell and tumor-initiating cell stemness by inducing primary ciliogenesis and Hedgehog signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29158396            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the knockdown of Ihh suppressed osteoblast growth and differentiation via a mechanism which may be associated with the TGF-beta\/Smad and OPG\/RANKL signaling pathways.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28990069            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH signaling regulates the direction of cerebellar granule cells division.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28633908            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The authors report here that Sonic Hedgehog (Shh)-Smoothened signaling downregulates Shisa2, which inhibits the glycosylation and cell surface presentation of Frizzled3 in rodent commissural axon growth cones.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28885142            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ESP of fifth-stage larval Angiostrongylus cantonensis stimulates astrocyte activation and IL-1beta and IL-6 production through NF-kappaB and the Shh signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28950910            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results indicate for the first time a possible mechanism involved in the crosstalk between fibroblasts and osteoblasts, as it was possible to observe trophic factors released by fibroblasts interfering decisively in osteoblast metabolism in a Shh-independent manner.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28578539            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Importantly, Scube2 uncouples processing of Shh peptides from their lipid-mediated juxtamembrane positioning, and thereby explains the long-standing conundrum that N-terminally unlipidated Shh shows patterning activity in Scube2-expressing vertebrates            \u003ca rel=\"nofollow\"\u003e             PMID:                        28778988            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Shh signaling requires the coordinated activity of Sulf1 and Sulf2 in order to reach that threshold in the mouse ventral spinal cord            \u003ca rel=\"nofollow\"\u003e             PMID:                        28490013            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH-dependent activation of WNT signaling supports regeneration of the cortex following long-term glucocorticoid treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29211850            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            by acting upstream of Shh signaling pathway, Barhl2 plays a crucial role in patterning the progenitor domains and establishing the positional identities of progenitor cells in the diencephalon.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27349434            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Gli3 activity in mouse thymic epithelial cells (TECs) promotes positive selection and differentiation from CD4(+) CD8(+) to CD4(+) CD8(-) single-positive (SP4) cells in the fetal thymus and Gli3 represses Shh constitutive deletion of Gli3, and conditional deletion of Gli3 from TECs, reduced differentiation to SP4, whereas conditional deletion of Gli3 from thymocytes did not            \u003ca rel=\"nofollow\"\u003e             PMID:                        29361554            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study shows a new role for Maml1 as a component of Shh signaling, which plays a crucial role in both development and tumorigenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28726779            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Sonic Hedgehog Activates Phospholipase A2 to Enhance Smoothened Ciliary Translocation            \u003ca rel=\"nofollow\"\u003e             PMID:                        28591579            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            smaller mvShh conjugates resulted in faster wound resolution compared to the unconjugated Shh. This study is the first to show how the wound healing efficacy of multivalent protein-polymer conjugates is sensitive to the polymer MW, and our findings suggest that this parameter could be used to enhance the efficacy of growth factor conjugates.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28679037            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SHH can promote cell growth and cell osteoblastic\/cementoblastic differentiation via BMP pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        27289556            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These studies reveal a postnatal cell population with transient Shh signaling that contributes to oligodendrogenesis during corpus callosum myelination, and gives rise to cells that continue to proliferate in adulthood and contribute to corpus callosum remyelination            \u003ca rel=\"nofollow\"\u003e             PMID:                        29045809            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results support a model whereby mutations in Cdon and prenatal ethanol exposure increase Septo-optic dysplasia risk through spatiotemporal perturbations in Shh signaling activity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27935818            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results report the identification of a novel long-range enhancer for Shh-Shh-brain-enhancer-6 (SBE6)-that is located 100 kb upstream of Shh and that is required for the proper induction of Shh expression during this differentiation program.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27852806            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Hh orchestrates the balance between quiescent and activated NSCs, with important implications for understanding adult neurogenesis under normal homeostatic conditions or during injury.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27666792            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            neuroectodermal Shh expression, dorsal\/ventral patterning, and amount of proliferation in the ventral neuroectoderm was not changed in Wnt1-Cre;Kif3a(fl\/fl) mutants; however, tissue polarity and directional cell division were disrupted.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28941984            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The authors find that cholesterol, an important component of the cell membrane, directly binds to Smoothened and changes its shape so that it can activate Hedgehog signaling components inside cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27705744            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Embryonal tumors with multilayered rosettes (ETMRs) are characterized by a parallel activation of Shh and Wnt signaling. Co-activation of these pathways in mouse neural precursors is sufficient to induce ETMR-like tumors in vivo that resemble their human counterparts on the basis of histology and global gene-expression analyses, and that point to apical radial glia cells as the possible tumor cell of origin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28892064            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            reactivating SHH signaling in mutant lungs rescued the tip dilation phenotype and attenuated FGF signaling. Importantly, the reduced SHH signaling activity did not appear to be caused by decreased Shh expression or protein stability; instead, biologically active form of SHH proteins were reduced in both the Ext1 mutant epithelium and surrounding wild type mesenchymal cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28859094            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            provide compelling evidence that epidermal YAP and Hedgehog\/GLI2 signalling undergo positive regulatory interactions in the control of normal epidermal homeostasis and in basal cell carcinoma (BCC) development, which in the large majority of cases is caused by aberrant Hedgehog signalling activity            \u003ca rel=\"nofollow\"\u003e             PMID:                        28820907            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            conditional deletion of Shh in the anterior hypothalamus results in a fully penetrant phenotype characterised by a complete arrest of (Rathke's pouch) RP development, with lack of Lhx3\/Lhx4 expression in RP epithelium.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28807898            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Shh production and Gli signaling is activated in vivo in lung, enhancing the Th2 response during a murine model of allergic asthma            \u003ca rel=\"nofollow\"\u003e             PMID:                        28235772            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Shh is in part responsible for the dependence of taste cell renewal on gustatory innervation, neurotrophic support of taste buds likely involves a complex set of factors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28743797            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPC6 stimulates Hh signaling by binding to Hh and Ptc1 at the cilium and increasing the interaction of the receptor and ligand to promote the growth of developing long bones.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28696225            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate that the transcription factor Gli3 (Gli3)-mutant fetal liver (FL) had increased sonic hedgehog (Shh) signaling resulting in decreased B cell development.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28533268            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate odd-skipped related protein 1 (Osr1) as a mediator of Hedgehog (HH) signaling during foregut organogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28501478            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            direct targeting of Foxf2 by Shh signaling drives cranial neural crest cell mesenchyme proliferation during upper lip morphogenesis, and disruption of this sequence results in cleft lip.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28506991            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Dicer1 ablation impairs Shh-induced granule neuron precursor proliferation by disrupting the expression of distinct cell cycle regulator genes that are targets of miR-17 approximately 92 cluster members. This study establishes a molecular link between miRNAs and cell cycle progression in the proliferating Granule neuron precursors during normal cerebellar development and may facilitate miRNA application in treating med...            \u003ca rel=\"nofollow\"\u003e             PMID:                        27600805            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of Bmp4 in the ureteric mesenchyme depends on HH signaling and Foxf1, and that exogenous BMP4 rescued cell proliferation and epithelial differentiation in ureters with abrogated HH signaling or FOXF1 function.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28797033            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A model in which SHH signaling plays both positive and negative roles in patterning and organogenesis of the thymus and parathyroids.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27633995            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This suggests an important cross-talk between SHH and WIP1 pathways that accelerates tumorigenesis and supports WIP1 inhibition as a potential treatment strategy for MB.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27086929            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SHH expression is associated with Medulloblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28031228            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            sonic hedgehog signaling activity influences clonal spatial distribution of thalamic neurons.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28250409            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Both the number of lung CD31-CD45-Sca-1+ cells and the expression levels of the Shh signaling pathway were downregulated in the lung tissues of mice with pulmonary emphysema. These cells and Shh signaling pathway are reactivated during acute adenovirus infection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28352167            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915098456289,"sku":"BL-2030NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYWACQahAACwnvkkYs8971_a48488fa-e9db-4647-b472-dadb9f76f888.jpg?v=1685853180"},{"product_id":"recombinant-human-osm-protein-his-tag-bl-2236np","title":"Recombinant Human OSM Protein (N-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Oncostatin M is produced by our E.coli expression system and the target gene encoding Ala26-Arg221 is expressed with a 6His tag at the N-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP13725\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eOncostatin-M; OSM\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eOncostatin M (OSM) is a glycoprotein belonging to the interleukin-6 family of cytokines that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. OSM encodes a growth regulator, which Inhibits the proliferation of a number of tumor cell lines. It stimulates proliferation of AIDS-KS cells. OSM regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells. OSM is considered as a pleiotropic cytokine that initiates its biological activities through specific cell surface receptors. The low affinity LIF receptor that shares the similarity of containing protein gp130 has now been identified to be a component of a high- affinity OSM receptor that will transduce OSM signals. OSM has also been shown to play a role in both pro and anti-inflammatory actions. OSM may also be involved in many biometabolism processes including liver development, haematopoeisis, inflammation, bone formation and destruction and possibly CNS development.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e24.44 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e28 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mMTris-HCl, 1mM EDTA, 200mM NaCl, pH 7.5.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.001 ng\/µg (0.01 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGrowth regulator. Inhibits the proliferation of a number of tumor cell lines. Stimulates proliferation of AIDS-KS cells. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells. Uses both type I OSM receptor (heterodimers composed of LIFR and IL6ST) and type II OSM receptor (heterodimers composed of OSMR and IL6ST). Involved in the maturation of fetal hepatocytes, thereby promoting liver development and regeneration.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLIF\/OSM family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            8506           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            165095           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:5008           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000215781           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29269396            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            OSM [oncostatin M]might be involved in the invasiveness of extravillous trophoblasts under hypoxia conditions via increasing MMP-2 and MMP-9 enzymatic activities through STAT3 signaling. Increased MMP-9 activity by OSM seems to be more important in primary trophoblasts.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30091322            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            IL6 family cytokine oncostatin-M (OSM) induced a switch to the EMT phenotype and protected cells from targeted drug-induced apoptosis in OSM receptors (OSMRs)\/JAK1\/STAT3-dependent manner            \u003ca rel=\"nofollow\"\u003e             PMID:                        28729401            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Oncostatin M induces RIG-I and MDA5 expression and enhances the double-stranded RNA response in fibroblasts.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28560754            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The IL-6-type cytokine oncostatin M (OSM) indeed induces cellular properties associated with tumorigenesis and disease progression in non-transformed human prostate epithelial cells, including morphological changes, epithelial-to-mesenchymal transition (EMT), enhanced migration and pro-invasive growth patterns.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29526757            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            downregulation of miR-20a-5p is caused by promoter hypermethylation. MiR-20a-5p could also suppress the production of IL-17 by targeting OSM and CCL1 production in CD4(+) T cells in patients with active VKH.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28972028            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our findings suggested that OSM suppresses SLUG expression and tumor metastasis of lung adenocarcinoma cells through inducing the inhibitory effect of the STAT1-dependent pathway and suppressing the activating effect of STAT3-dependent signaling            \u003ca rel=\"nofollow\"\u003e             PMID:                        27486982            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genistein (a specific Tyr phosphorylation inhibitor) leads to the interaction of CHOP (C\/EBP Homologous Protein) with C\/EBP-beta, thus negatively regulating it. Knockdown of C\/EBP-beta also leads to inhibition of PMA-mediated OSM induction.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27676154            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data provide evidence that OSM regulates an epithelial-mesenchymal transition and cancer stem cell plasticity program that promotes tumorigenic properties in pancreatic cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28053127            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OSM-induced plasticity was Signal Transducer and Activator of Transcription 3 (STAT3)-dependent, and also required a novel intersection with transforming growth factor-beta (TGF-beta)\/SMAD signaling. Removal of OSM or inhibition of STAT3 or SMAD3 resulted in a marked reversion to a non-invasive, epithelial phenotype.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28288136            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Neutrophils are a major source of OSM-producing cells in patients with chronic rhinosinusitis and severe asthma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27993536            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OSM and OSMR are highly expressed in inflammatory bowel disease intestinal mucosa compared to control mucosa. OSM promotes inflammatory behavior in human intestinal stroma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28368383            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study showed that in atrial fibrillation (AF) with thrombus, the atrial tissue infiltration of M1 macrophages increased significantly; the OSM expression was also found to increase simultaneously; downstream tissue factor (TF) increased and tissue factor pathway inhibitors (TFPI)decreased, leading to an imbalance between TF and TFPI eventually. OSM might be related to thrombosis in patients with AF mediated by TF and TFPI            \u003ca rel=\"nofollow\"\u003e             PMID:                        28471981            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a novel STAT3\/SMAD3-signaling axis is required for OSM-mediated senescence.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27892764            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This result demonstrates that HPV16 oncoproteins upregulate oncostatin M and play an important role to promote oral squamous cell carcinoma development            \u003ca rel=\"nofollow\"\u003e             PMID:                        27349249            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The identification of the OSM inflammatory pathway as an important mediator of epithelial mesenchymal transition in triple-negative breast cancer (TNBC) may provide a novel potential opportunity to improve therapeutic strategies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28106823            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Oncostatin M and interleukin-31: Cytokines, receptors, signal transduction and physiology.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26198770            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Oncostatin M can regulate airway smooth muscle responses alone or in synergy with IL-17A.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25849622            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we demonstrated that recombinant human OSM (rhOSM) promoted tumor angiogenesis in EC cell lines by activating STAT3 (signal transducer and activator of transcription 3) and enhanced both cell migration and cell inva            \u003ca rel=\"nofollow\"\u003e             PMID:                        25954856            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OSM expression in osteoblasts increases in response to Osteopontin-induced inflammation in vitro.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26304992            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that OSM promotes osteoblastic differentiation of vascular smooth muscle cells through JAK3\/STAT3 pathway and may contribute to the development of atherosclerotic calcification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25735629            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            administration of Fstl1 induced airway remodeling and increased OSM, whereas administration of an anti-OSM Ab blocked the effect of Fstl1 on inducing airway remodeling, eosinophilic airway inflammation            \u003ca rel=\"nofollow\"\u003e             PMID:                        26355153            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OSM promotes mucosal epithelial barrier dysfunction, and its expression is increased in patients with eosinophilic mucosal disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25840724            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Oncostatin M regulates neuronal function and confers neuroprotectin in an animal model of ischemic stroke.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26311783            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In patients with diabetes, bone marrow plasma OSM levels were higher and correlated with the bone marrow to peripheral blood stem cell ratio.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25804939            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OSM promotes STAT3-dependent intestinal epithelial cell proliferation and wound healing in vitro.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24710357            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Autocrine activation of STAT3 in MCF-7 cells ectopically expressing OSM-induced cellular scattering.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25252914            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            oncostatin M is a cytokine possessing vigorous antiviral and immunostimulatory properties which is released by APC upon interaction with CD40L present on activated CD4+ T cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24418171            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that pro-inflammatory cytokines such as IL6 or OSM could activate pathways associated with prostate cancer progression and synergize with cell-autonomous oncogenic events to promote aggressive malignancy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23867565            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OSM may promote a clinically relevant EMT\/CSC-like phenotype in human breast cancer via a PI3K-dependent mechanism            \u003ca rel=\"nofollow\"\u003e             PMID:                        23584474            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            white adipose tissue macrophages are a source of OSM and OSM levels are significantly induced in obesity\/type 2 diabetes. OSM produced from immune cells in WAT may act in a paracrine manner on adipocytes to promote inflammation in adipose tissue.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24297795            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data suggest that increased serum OSM levels are associated with the coronary stenosis score and that circulating levels of this chemokine may reflect the extent of coronary atherosclerosis            \u003ca rel=\"nofollow\"\u003e             PMID:                        24600984            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGFBI and periostin, extracellular matrix proteins implicated in tumorigenesis and metastasis, were identified as oncostatin M-induced secreted proteins in mesenchymal stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23735324            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Oncostatin M is a FIP1L1\/PDGFRA-dependent mediator of cytokine production in chronic eosinophilic leukemia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23621172            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data show that OSM and IL-1beta are not only a biological characteristic signature of hypertensive leg ulcer, but these cytokines reflect a specific inflammatory state, directly involved in the pathogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23313749            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OSM induced proliferation of Ewing sarcoma cell lines.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22982441            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that OSM enhances invasion activities of extravillous trophoblasts during placentation through increased enzyme activity of MMP-2 (primarily) and MMP-9 (to some extent).            \u003ca rel=\"nofollow\"\u003e             PMID:                        22931588            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A unique loop structure in oncostatin M determines binding affinity toward oncostatin M receptor and leukemia inhibitory factor receptor.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22829597            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Oncostatin M signaling may cause suppression of estrogen receptor-alpha and disease progression i breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22267707            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Oncostatin M (OSM), a cytokine of the IL-6 family, was identified as a major coupling factor produced by activated circulating CD14+ or bone marrow CD11b+ monocytes\/macrophages.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22267310            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Oncostatin M (OSM) is a major mediator of cardiomyocyte dedifferentiation and remodeling during acute myocardial infarction (MI) and in chronic dilated cardiomyopathy (DCM).            \u003ca rel=\"nofollow\"\u003e             PMID:                        22056139            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            JAK2 V617F-mediated up-regulation of OSM may contribute to fibrosis, neoangiogenesis, and the cytokine storm observed in myeloproliferative neoplasms.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22051730            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            c-MYC is an important molecular switch that alters the cellular response to OSM-mediated signaling from tumor suppressive to tumor promoting.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21975934            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A possible interaction between IL-6, OSM, u-PA and VEGF in prostate cancer was investigated.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21965736            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This report uses an in vitro model with human umbilical vein endothelial cells and isolated human neutrophils to examine the effects of two locally derived cytokines, granulocyte-macrophage colony-stimulating factor and G-CSF, on oncostatin M expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21775705            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OSM is expressed in atherosclerotic lesions and may contribute to the progression of atherosclerosis by promoting SMC proliferation, migration and extracellular matrix protein synthesis through the STAT pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        21376322            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Taken together, our data show that KIT D816V promotes expression of OSM through activation of STAT5.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21457934            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The purpose of this study was to investigate the possible suppressive or stimulatory role of OSM in the ovarian cancer model of SKOV3 cells, as well as the involvement of the ERK1\/2, p38 and STAT3 signaling pathways.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21399864            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            promotes STAT3 activation, VEGF production, and invasion in osteosarcoma cell lines            \u003ca rel=\"nofollow\"\u003e             PMID:                        21481226            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a cytokine-triggered regulatory network for PCSK9 expression that is linked to JAKs and the ERK signaling pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        21196532            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915098489057,"sku":"BL-2236NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLSiAXpVUAACq3oz8lsk365_fcb55d9c-7246-4805-9812-d443f93dbd45.jpg?v=1685853181"},{"product_id":"recombinant-human-serpin-a7-protein-his-tag-bl-2241np","title":"Recombinant Human Serpin A7 Protein (C-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Serine Protease Inhibitor-clade A7 is produced by our Mammalian expression system and the target gene encoding Ala21-Ala415 is expressed with a 6His tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"P05543\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/P05543\/entry\"\u003eP05543\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThyroxine-Binding Globulin; Serpin A7; T4-Binding Globulin; SERPINA7; TBG\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSerpin A7 is a secreted protein which belongs to the Serpin family. As a 54 kDa protein, Serpin A7 is synthesized primarily in the liver and secreted in plasma. Genomically, Serpin A7 is a serpin, although it has no inhibitory function like many other members of this class of proteins. Serpin A7 binds thyroid hormone in circulation. It is one of three proteins (along with transthyretin and albumin) responsible for carrying the thyroid hormones thyroxine (T4) and 3,5,3’-triiodothyronine (T3) in the bloodstream. Of these three proteins, Serpin A7 has the highest affinity for T4 and T3, but is present in the lowest concentration. Despite its low concentration, Serpin A7 carries the majority of T4 in serum. Due to the very low serum concentration of T4 and T3 in the blood, Serpin A7 is rarely more than 25% saturated with its ligand. Unlike transthyretin and albumin, Serpin A7 has a single binding site for T4\/T3. Serpin A7 tests are sometimes used in finding the reason for elevated or diminished levels of thyroid hormone, and defects in Serpin A7 are a cause of Serpin A7 deficiency.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e49.9 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e55-65 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915106320609,"sku":"BL-2241NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLU6ACy_lAAClmsBr_EQ220_0d3035a3-14ab-4ac9-bd3c-11de5c4799a9.jpg?v=1685853487"},{"product_id":"recombinant-human-mouse-rat-gdf8-protein-bl-2256np","title":"Recombinant Human\/Mouse\/Rat GDF-8 Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human\/Mouse\/Rat Growth Differentiation Factor 8 is produced by our Mammalian expression system and the target gene encoding Lys262-Ser375 is expressed.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eO14793\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGrowth\/differentiation factor 8; GDF-8; Myostatin; Mstn; Gdf8\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGrowth\/differentiation factor 8(Mstn, GDF-8) is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. It is expressed specifically in developing and adult skeletal muscle. It exists as a homodimer, and interacts with WFIKKN2, leading to inhibit its activity. This protein can act specifically as a negative regulator of skeletal muscle growth. It regulates cell growth and differentiation in both embryonic and adult tissues.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e13.1 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e12-15 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eActs specifically as a negative regulator of skeletal muscle growth.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGF-beta family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            4223           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            601788           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:2660           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000260950           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30241032            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            the maturation and secretion of myostatin precursor MstnPP and its metabolites in a human muscle cell line, was investigated.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29546591            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Acute high-intensity interval exercise decreased irisin levels and increased myostatin levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29558345            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Autosomal Dominant Polycystic Kidney Disease patients with moderately preserved renal function have higher levels of FasL, myostatin and urine TGF-beta1 than controls            \u003ca rel=\"nofollow\"\u003e             PMID:                        29794429            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Tolloid cleavage activates latent GDF8 by destabilizing specific prodomain-growth factor interfaces and primes the growth factor for release from the prodomain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29343545            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myostatin pathway is down-regulated in the neuromuscular diseases.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29192144            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the prodomain:GDF8 complex can exist in a fully latent state and an activated or \"triggered\" state where the prodomain remains in complex with the mature domain            \u003ca rel=\"nofollow\"\u003e             PMID:                        29348202            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Higher serum myostatin levels correlated with muscle mass loss, hyperammonemia, and impaired protein synthesis, as reflected by lower serum albumin levels and lower branched-chain amino acid to tyrosine ratio levels. High serum myostatin levels were also associated with a reduced OS rate in LC patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28627027            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study showed the expression of myostatin in healthy endometrium and a higher expression in endometriosis and endometrial cancer, suggesting myostatin involvement in human endometrial physiology and related pathologies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28345488            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studied levels of myostatin in both serum and synovial fluid in patients with knee osteoarthritis and found both correlated with severity of knee osteoarthritis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27878995            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myostatin (and Smad2) were significantly up-regulated in the failing heart of female patients, but not male patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28465115            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The Growth Differentiation Factor 11 (GDF11) and Myostatin (MSTN) in tissue specific aging.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28472635            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MSTN 153Arg(R) polymorphism is associated with long distance running success.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28007336            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GDF8 promotes ovarian cancer cell migration via ALK4\/5-SMAD2\/3-E-cadherin signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27481097            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results demonstrat that GDF8 stimulates the expression and secretion of CTGF in human granulosa cells and provide evidence that both proteins may play critical roles in the regulation of extracellular matrix formation in these cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27392496            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These studies identify distinctive structural features of GDF11 that enhance its potency, relative to GDF8; however, the biological consequences of these differences remain to be determined.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28257634            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum myostatin levels were significantly decreased in heart failure patients and associated with lower extremity muscle wasting.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27390974            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our data showed a virtual absence of the variant (K) allele in MSTN rs1805086 in Japanese population, and no differences in allele\/genotype frequencies in ACTN3 rs1815739 among centenarians and healthy controls of this country.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27861536            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MSTN, but not GDF11, declines in healthy men throughout aging.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27304512            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Multivariate regression analysis revealed that myostatin levels correlated significantly with tricuspid annular plane systolic excursion values and right ventricle myocardial performance index among the study patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        27323660            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study measured circulating myostatin levels in seven inherited muscle diseases using an immunoaffinity LC-MS\/MS approach, found significantly lower serum myostatin concentrations in numerous muscle disease patient populations and the associations with clinical measurements suggests the potential utility of myostatin as a biomarker of genetic muscle disease progression            \u003ca rel=\"nofollow\"\u003e             PMID:                        28074267            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data indicated that serum myostatin concentration did not correlate with muscle and bone mass in postmenopausal women            \u003ca rel=\"nofollow\"\u003e             PMID:                        27144806            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myostatin mRNA expression in skeletal muscle was significantly reduced compared with pre-exercise values at all time points with no difference between exercise intensity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27467217            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Low expression of serum MSTN is associated with Cachexia Prevention in Patients with Medullary Thyroid Cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27165248            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myostatin was differentially expressed in the muscle and adipose tissue in relation to physical activity and dysglycaemia            \u003ca rel=\"nofollow\"\u003e             PMID:                        26572800            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our results suggest that serum levels of myostatin and irisin are related in patients with type 2 diabetes            \u003ca rel=\"nofollow\"\u003e             PMID:                        26438394            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Matrix metalloproteinase 14 was highly expressed in uterine leiomyoma and correlated with myostatin and activin A mRNA expression. Moreover, MMP14 and myostatin mRNA expression correlated significantly and directly with the intensity of dysmenorrhea.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26138721            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A synthetic peptide corresponding to this decorin region dose-dependently inhibited the response to myostatin in cardiomyocytes            \u003ca rel=\"nofollow\"\u003e             PMID:                        27559042            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings suggest that GDF8 and CTGF may play critical roles in the regulation of proliferative events in human granulosa cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26577677            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myostatin concentrations in plasma and protein expression in placental tissue are significantly higher in women with preeclampsia. Cytokine production by first-trimester placental tissues was altered following myostatin treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25736326            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myostatin is a well-described negative regulator of postnatal skeletal and cardiac muscle mass and modulates metabolic processes. It functions in the heart, skeletal muscle, and brain. Review.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27034275            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Plasma myostatin levels are increased in chronic obstructive pulmonary disease patients who have cor pulmonale.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26998756            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In human granulosa cells, GDF8 may play an important role in the modulation of cellular responsiveness to gonadotropins and in the regulation of ovarian steroid production, most likely as a luteinization inhibitor.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26607022            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Plasma myostatin might be suitable in predicting weight regain after marked weight loss, but no association with weight loss was observed in patients undergoing a non-surgical weight loss program.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26393401            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Plasma MSTN level was elevated in an early stage of CKD, which could be involved in the progression of sarcopenia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26502079            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            it is becoming clearer that besides its conventional role in muscle, myostatin plays a critical role in metabolism. Hence, molecular mechanisms by which myostatin regulates several key metabolic processes need to be further explored.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26305594            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The aim of this study was to investigate MSTN polymorphisms in an elderly sarcopenic population in Turkey and determine how they relate to sarcopenia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26046327            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There is a significant decrease in levels of circulating myostatin in postsurgical acute phase reaction.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25749570            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myostatin myocardial expression increases in the presence of structural cardiomyopathy either of hypertensive or other origin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25915890            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In contrast to elite endurance and power track and field athletes, the MSTN 153RR genotype was not found in short distance-swimmers, and among the long distance-swimmers it was not associated with top level swimming performance.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25936293            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Lower serum myostatin independently associated with MetS, central obesity, low HDL-C, and high triglycerides after adjustment. Higher serum myostatin is associated with favorable metabolic profiles.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25254550            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate that GDF8 down-regulates PTX3 expression via SMAD-dependent signaling in human granulosa cells suggesting a potential role for GDF8 in the regulation of follicular function.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25641196            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Adenomyotic tissues express high levels of myostatin, follistatin, and activin type II receptors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26086422            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This is the first demonstration of a spatial asymmetry in the expression pattern of Mstn\/IGF-I in healthy hearts, which is likely to play a role in the different growth regulation of left vs. right ventricle            \u003ca rel=\"nofollow\"\u003e             PMID:                        25591711            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myostatin expression in placental tissue is altered under stress conditions (e.g. obesity and abnormal glucose metabolism) found in pregnancies complicated with gestational diabetes mellitus.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25443639            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we show that the K153R mutation significantly increases the rate of proteolysis of promyostatin by furin, but has no effect on the activity of the latent complex or the cleavage of the latent complex by bone morphogenetic protein 1 (BMP-1).            \u003ca rel=\"nofollow\"\u003e             PMID:                        25543063            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MyoD acts to promote SC proliferation and transition of cells into differentiation, while myogenin is known to drive terminal differentiation            \u003ca rel=\"nofollow\"\u003e             PMID:                        25108351            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            role of myostatin in cardiovascular disease and cachexia            \u003ca rel=\"nofollow\"\u003e             PMID:                        24680839            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Myostatin localization was positively identified in extravillous trophoblast. Myostatin positively affected proliferation and migration of extravillous trophoblast.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25093622            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study demonstrated that the variant alleles of MSTN A55T and K153R polymorphisms could significantly enhance muscle hypertrophy in response to strength training among Han Chinese men.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24479661            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915100979425,"sku":"BL-2256NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLY6AW1a_AADEpvBizaY096_11a4907c-4925-4473-9dea-35f3b1d639a6.jpg?v=1685853279"},{"product_id":"recombinant-human-vitronectin-protein-his-tag-bl-2319np","title":"Recombinant Human Vitronectin Protein (N-Truncated, C-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Vitronectin is produced by our Mammalian expression system and the target gene encoding Val62-Leu478 is expressed with a 6His tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAAH05046.1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eComplement S-protein; epibolin; Serum Spreading Factor; Serum-spreading factor; Somatomedin B; S-protein; V75; Vitronectin; VN; VNT; VTN\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eVitronectin, also known as VTN, is a large glycoprotein found in blood and the extracellular matrix (ECM). Vitronectin is a plasma glycoprotein implicated as a regulator of diverse physiological process, including blood coagulation, fibrinolysis, pericellular proteolysis, complement dependent immune responses, and cell attachment and spreading. Blocking of Hic(a member of the pneumococcal surface protein C (PspC) family) by specific antiserum or genetic deletion significantly reduced pneumococcal binding to soluble and immobilised vitronectin and to Factor H, respectively. In addition, Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e48.3 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e60-70 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM Tris HCl, 150mM  NaCl, 0.02% Tween 80, pH8.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 90% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eVitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.; Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted, extracellular space.; Parasitophorous vacuole.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            12724           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            193190           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:7448           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000226218           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29780059            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            The 10 kDa C-terminal fragment of the ECM protein vitronectin (VTN) was then selected as a promising circulating biomarker in discriminating Nonalcoholic steatohepatitis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29463024            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The authors observed that exposure of Burkholderia pseudomallei and the closely related yet avirulent Burkholderia thailandensis to human plasma increased epithelial cell invasion by \u0026gt;20 fold. Receptor blocking studies with RGD-domain containing peptide and alphaV beta3 blocking antibody identified complement-activated vitronectin as the factor facilitating this invasion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28186697            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Additionally, the authors utilized vitroenctin-derived peptides to map the minimal Rickettsia conorii Adr1\/human vitronectin interaction to the C-terminal region of vitronectin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28299286            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We show that small N-terminal fragments of VN consistent with processing of the RGD motif are present in liquid biopsies of cancer patients as well as in the urine of healthy individuals.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27189837            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum vitronectin levels are elevated in human glioma, as well as are independently associated with pathologic grade based on WHO classification and 5-year poor prognosis. Moreover, this biomarker significantly discriminates gliomas from controls, other non-glioma brain tumors and other non-tumor neurological diseases, distinguishes high-grade gliomas from low-grade gliomas, and predicts 5-year progression and mortality.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27871448            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Elevated serum VN levels represented high diagnostic value and had close relation to clinicopathological factors and early recurrence, suggesting that serum VN might be a useful diagnostic and prognostic marker for HCC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27802203            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We confirmed increased levels of C1R and VTN in sera from patients with Joint hypermobility syndrome by western blot analyses            \u003ca rel=\"nofollow\"\u003e             PMID:                        26709396            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study examines the complexes of PAI-1 with tissue-type and urokinase-type plasminogen activator and vitronectin revealed by changes in the conformation and dynamics of the reactive center loop.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26548921            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ail-expressing Yersinia pestis strains bind vitronectin - a host protein with functions in cell attachment, fibrinolysis and inhibition of the complement system.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26377177            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression of VN in tumor cells independently indicated poor clinical prognosis in patients with osteosarcoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26617861            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The mean level of PAI-1 was 23.02 +\/- 15 (8.2-71.19) ng\/mL and vitronectin was 83.10% +\/- 23.77% (12%-126%) in the tumor group.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24770328            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Bacterial protein-E and host vitronectin play a role in the attachment to bronchial epithelial cells and is also involved in the subsequent intracellular invasion of nontypeable Haemophilus influenzae.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26572616            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            P. aeruginosa isolates obtained from CF patients significantly bound vitronectin. Porin D was defined as a novel P. aeruginosa vitronectin-receptor            \u003ca rel=\"nofollow\"\u003e             PMID:                        26047937            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Lpd of P. aeruginosa is a surface exposed moonlighting protein that binds two human terminal pathway inhibitors, vitronectin and clusterin            \u003ca rel=\"nofollow\"\u003e             PMID:                        26368530            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The VN level may be relevant as a clinical biomarker for adverse cardiovascular outcomes not only in patients with ischemic heart disease undergoing coronary interventions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24823429            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Vitronectin expression in the airways of subjects with asthma and chronic obstructive pulmonary disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        25768308            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Gpm1 in Candida albicans attaches to human endothelial cells and to keratinocytes via the adhesive protein vitronectin            \u003ca rel=\"nofollow\"\u003e             PMID:                        24625558            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Vitronectin is identified as a common constituent of amyloid deposits in 175 formalin-fixed and paraffin-embedded tissue samples from a large variety of different amyloid diseases.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26101327            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Hic interacts with vitronectin and simultaneously with Factor H, and both human proteins may contribute to colonisation and invasive disease caused by serotype 3 pneumococci.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25181963            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            VTN plays a significant role in the malignant growth of tumor.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25179307            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Melanoma cell adhesion to vitronectin is dependent on beta-1,6-branched N-glycans.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24687613            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A total of 17 site-specific N-glycopeptides were completely identified in all of the three N-glycosylation sites of vitronectin in human plasma, including 12 N-glycopeptides first reported.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25374123            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The presence of VN on the material surfaces enhanced cell-mediated FN reorganization and secretion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23899674            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            serum levels of both fibronectin and vitronectin may be the diagnostic markers in melanoma patients, but not markers of prognosis            \u003ca rel=\"nofollow\"\u003e             PMID:                        24999757            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors demonstrate that an evolutionarily conserved rickettsial antigen, Adr1\/RC1281, interacts with human vitronectin and is sufficient to mediate resistance to serum killing when expressed at the outer-membrane.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24286496            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The interaction between uPAR and vitronectin triggers ligand-independent adhesion signalling by integrins.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25168639            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A strong linkage disequilibrium was found in vitronectin promoter in Chinese with vascular disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23041018            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Vn competes with hTSP-1 for binding to Atl repeats and vice versa. In conclusion, this study identifies the Atl repeats as bacterial adhesive structures interacting with the human glycoproteins hTSP-1 and Vn.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24371140            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            increased expression levels of VN protein and mRNA in placental maternal-fetal interface of EOSP may be involved in adhesion and repair of placental infarct lesions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23124223            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Interaction of vitronectin with integrin alphavbeta3 results in the continued activation of the kinase mTOR.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23722547            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In conclusion, the head domains of UspA2\/2H have extensive sequence polymorphism without losing vitronectin-binding capacity promoting a general evasion of the host immune system.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23474333            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study highlights that ascites-derived fibronectin and vitronectin exhibit different properties depending on the ascites            \u003ca rel=\"nofollow\"\u003e             PMID:                        23811340            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            An isogenic nontypeable Haemophilus influenzae 3655Deltahpf mutant devoid of protein F displayed a reduced binding of vitronectin, and was consequently more sensitive to killing by human serum compared with the wild type.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23387957            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The choline-binding protein PspC of Streptococcus pneumoniae interacts with the C-terminal heparin-binding domain of vitronectin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23603906            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Importance of vitronectin and its interaction with the urokinase receptor in tumor growth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23327926            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There was no difference in serum vitronectin levels between Behcet's disease patients and control subjects, and there was no statistically significant difference between vitronectin levels in Behcet patients with and without ocular involvement.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22810367            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this study, the authors demonstrate meningococcal interactions with vitronectin via a novel adhesin, Msf (meningococcal surface fibril, previously NhhA or Hsf).            \u003ca rel=\"nofollow\"\u003e             PMID:                        22050461            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            higgh plasms levels is associated with the risk of metabolic syndrome and type 2 diabetes mellitus            \u003ca rel=\"nofollow\"\u003e             PMID:                        21800006            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A series of truncated vitronectin molecules revealed that the C-terminal domain comprising vitronectin(353-363) harboured the major binding region for Haemophilus influenzae protein E.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21542857            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High serum vitronectin is associated with breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21253761            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PAI-2 is capable of inhibiting uPA in the presence of PAI-1, particularly on adherent cells in the presence of vitronectin            \u003ca rel=\"nofollow\"\u003e             PMID:                        21316840            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Thrombospondin 1, fibronectin, and vitronectin are differentially dependent upon RAS, ERK1\/2, and p38 for induction of vascular smooth muscle cell chemotaxis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21193465            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results provide the first evidence for vitronectin gene expression in urothelial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21048021            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Plasminogen activator inhibitor-1 and vitronectin expression level and stoichiometry regulate vascular smooth muscle cell migration through physiological collagen matrices            \u003ca rel=\"nofollow\"\u003e             PMID:                        20492459            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            expression of vitronectin at the periphery of mesothelial cells and within ovarian cancer cell clusters suggests a potential role for this molecule during intraperitoneal implantation of ovarian cancer cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        20121701            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study directly reveals the binding mode between the N-terminal domain of UspA2 Moraxella catarrhalis and the C-terminal part of vitronectin and thus sheds light upon the mechanism of Moraxella catarrhalis-dependent serum resistance.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20199596            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data reveal that multimeric VTNC attenuate Cyr61 binding to immobilized VTNC, while monomeric VTNC was ineffective.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20195466            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A fragment of vitronectin containing the RGD integrin binding site showed similar binding affinity as that of full vitronectin protein to purified integrin alphavbeta3 but had diminished cell adhesion and spreading function in vivo.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20600001            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Neisseria meningitidis Opc expressed in acapsulate as well as capsulate bacteria can increase human brain endothelial cell line adhesion and entry by first binding to serum vitronectin            \u003ca rel=\"nofollow\"\u003e             PMID:                        20502634            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915102912737,"sku":"BL-2319NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLbeAR4e9AACXYXx8py8046_cf4df9c1-2b49-4419-b950-17264fd34f30.jpg?v=1685853359"},{"product_id":"recombinant-human-afamin-protein-his-tag-bl-2322np","title":"Recombinant Human Afamin Protein (C-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Afamin is produced by our Mammalian expression system and the target gene encoding Leu22-Asn599 is expressed with a 6His tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"P43652\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/P43652\/entry\"\u003eP43652\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAfamin; AFM; ALB2; ALB2alpha-Alb; ALBA; ALBAalpha-albumin; ALF; Alpha-Alb; Alpha-albumin\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAfamin also known as Alpha -Albumin is a secreted monomeric glycoprotein of the Alb\/Albumin family of molecules. AFM is known to bind and transport vitamin E family molecules, playing an important role for transporting at the blood-brain-barrier. Afamin has been shown to act as extracellular chaperone for poorly soluble, acylated Wnt proteins, forming a stable, soluble complex with functioning Wnt proteins. AFM also serves as an osteoclast-derived chemoattractant for preosteoblasts, providing a rational for the observation that bone formation often follows bone resorption. The importance of Afamin in transport of molecules has led to a suggested diagnostic role in various diseases, including pre-eclampsia, ovarian cancer, and both gestational and type-2 diabetes.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e67.6 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e80-100 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915104223457,"sku":"BL-2322NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLbiAbqDhAACEUhX3vPg754_b496a651-9be6-4d66-9705-c8dffd86ccb5.jpg?v=1685853407"},{"product_id":"recombinant-human-plgf-2-protein-his-tag-bl-2323np","title":"Recombinant Human PLGF-2 Protein (C-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Placenta Growth Factor is produced by our Mammalian expression system and the target gene encoding Leu19-Arg170 is expressed with a 6His tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"P49763-3\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/P49763\/entry#P49763-3\"\u003eP49763-3\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePlGF2; PlGF-2; PGF; PLGF; PlGF2; PlGF; PGFL\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003ePlacental growth factor is a protein that in humans is encoded by the PGF gene. It is a secreted protein and belongs to the PDGF\/VEGF growth factor family. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF‑1), 152 (PlGF‑2), and 203 (PlGF‑3) amino acids (aa) respectively. PlGF is mainly found as a variably glycosylated, secreted, 55 ‑ 60 kDa disulfide linked homodimer.The protein is a member of the VEGF (vascular endothelial growth factor) sub-family-a key molecule in angiogenesis and vasculogenesis, in particular during embryogenesis. The main source of PGF during pregnancy is the placental trophoblast. PGF is also expressed in many other tissues, including the villous trophoblast. PlGF (especially PlGF‑1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF‑2, like VEGF164\/165, shows heparin‑dependent binding of neuropilin (Npn)‑1 and Npn‑2, and can inhibit nerve growth cone collapse. Circulating PlGF often correlates with tumor stage and aggressiveness, and therapeutic PlGF‑2 antibodies are being investigated for their ability to inhibit tumor growth and angiogenesis.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e18.2 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e25-30 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915099767009,"sku":"BL-2323NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLbiABh9VAACQH19ZRiY435_b7291d23-5bb9-47c7-9011-a7a5a699abf4.jpg?v=1685853228"},{"product_id":"recombinant-human-tgfbr2-protein-fc-tag-bl-0043np","title":"Recombinant Human TGFBR2 Protein (C-Fc)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Transforming Growth Factor-beta Receptor Type II is produced by our Mammalian expression system and the target gene encoding Thr23-Asp159 is expressed with a human IgG1 Fc tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP37173\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGF-beta receptor type-2; TGF-beta type II receptor;TGFBR2; Transforming growth factor-beta receptor type II\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGFBR2 is a single-pass type I membrane protein and contains one protein kinase domain. TGFBR2 exsits as a heterodimeric complex with another receptor protein and binds TGF-beta. Signals triggered through the TGF-beta receptor complex prompt various responses by the cell. One such response is to inhibit cell growth and division. Based on this action, the TGF-beta receptor type 2 is sometimes called a tumor suppressor. Defects in TGFBR2 have been associated with Marfan syndrome, Loeys-Deitz aortic aneurysm syndrome, Osler-Weber-Rendu syndrome and the development of various types of tumors.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e42.6 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e59 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBiologically active. Please contact us to obtain bioactivity data.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTransmembrane serine\/threonine kinase forming with the TGF-beta type I serine\/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCell membrane; Single-pass type I membrane protein. Membrane raft.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eProtein kinase superfamily, TKL Ser\/Thr protein kinase family, TGFB receptor subfamily\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            11773           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            133239           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:7048           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000351905           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28443643            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            TGFBR2 Polymorphisms Are Associated with Colorectal Cancer in Patients with Lynch Syndrome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30275229            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study has confirmed or corrected the clinical diagnosis, and enlarged the mutation spectrum of FBN1 and TGFBR2 and confirmed that parental mosaicism may be the cause of the varied phenotypic expression of these connective tissue disorders.The results should be helpful for prenatal diagnosis and genetic counseling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30101859            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the restoration of TGFBR2 in miR-204 overexpression Gastric cancer (GC) cells, which recovered resistance to 5-FU treatments compared with miR-204 overexpression GC cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29940566            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MiR-9-5p promotes the proliferation, metastasis and invasion of non-small cell lung cancer cells by down-regulating TGFBR2 expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29239816            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Microarray-based analyses revealed that the expression of miR-20b was significantly increased, whereas TGFBR2 and MYC were significantly downregulated and upregulated, respectively, in all ES cells compared to their expression in human mesenchymal stem cells (hMSCs).            \u003ca rel=\"nofollow\"\u003e             PMID:                        29039480            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study provides evidence that TGFBR2 rs6785358 polymorphism might be associated with the risk of hypospadias.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28894026            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Down-regulation of TGF-beta RII was found in the invasive non-functioning pituitary adenomas compared to noninvasive ones.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29031543            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings reveal a novel role for miR-204\/ANGPT1\/TGFbetaR2 axis in tumor angiogenesis. We propose that therapeutic manipulation of miR-204 levels may represent a promising approach in breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27703260            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High TGFBR2 expression is associated with small cell lung cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28055980            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            expression induced by IL-6 in keratinocytes            \u003ca rel=\"nofollow\"\u003e             PMID:                        27892604            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            hsa-miR-1193 may be involved in sporadic colorectal cancer tumourigenesis at least in part by suppression of TGFBR2, and the A allele of rs11466537 disturbed the regulation of hsa-miR-1193 on TGFBR2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28494187            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that TGFbR2 expression decreases in human gastric cancer (GC) tissue specimens and indicate that the expression of TGFbR2 is mainly dependent on post-transcriptional regulators in GC through miR-155 binding to the 3'-UTR of its mRNA.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29247570            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrated that Increased Transforming Growth Factor beta2 in the Neocortex of Alzheimer's Disease and Dementia with Lewy Bodies is Correlated with Disease Severity and Soluble Abeta42 Load.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27911312            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate the most significant gene level association seen with transforming growth factor beta receptor 2 (TGFBR2) and clear cell epithelial ovarian cancer (EOC).            \u003ca rel=\"nofollow\"\u003e             PMID:                        27533245            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Abnormal expression of TGF-beta type II receptor isoforms contributes to prognosis in acute myeloid leukemia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28052022            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            altered Tgfbeta signaling in cultured mouse and human enteroids supports further the in vivo data and reveals a critical role for Tgfbeta signaling in generating precursor secretory cells. Overall, our data reveal a key role for Tgfbeta signaling in regulating ISCs clonal dynamics and differentiation, with implications for cancer, tissue regeneration, and inflammation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27791005            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MiR-130 is up-regulated in gastric cancer (GC) tissues and directly targets TGF-beta type II receptor (TGFbetaR2).            \u003ca rel=\"nofollow\"\u003e             PMID:                        27304191            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-17-5p negatively regulated TGFBR2 expression by directly binding to the 3'UTR of TGFBR2 mRNA, thereby promoting gastric cancer cell growth and migration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27120811            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High TGFBR2 expression is associated with mesenchymal to epithelial transition of breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28987542            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Inhibition of TGFBR2 had the similar effect as miR-9 overexpression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27756824            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we describe and characterize the functional impact of a novel VUS in the TGFBR2 kinase domain (c.1255G\u0026gt;T; p.Val419Leu), in a patient with the clinical diagnosis of Marfan syndrome spectrum. Our results establish that the V419L variant leads to aberrant TGF-beta signaling and confirm the diagnosis of Loeys-Dietz syndrome in this patient.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28679693            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Apo and inhibitor-bound TGFBR2 kinase structures are presented at high resolution (\u0026lt;2 A).            \u003ca rel=\"nofollow\"\u003e             PMID:                        27139629            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGF-beta type I, II, and III receptors were all identified in pregnant serum; all were substantially elevated in early-onset but not late-onset PE. Endoglin was increased in both subtypes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28633389            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this is the first clinical report to demonstrate a potential causal association between TGFB2 gene mutations and aortic root dilatation in combination with the myxomatous degeneration of both atrioventricular valves.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28633253            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Molecular modeling and molecular dynamic simulation of the effects of variants in the TGFBR2 kinase domain as a paradigm for interpretation of variants obtained by next generation sequencing.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28182693            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A novel mutation in the TGFBR2 gene was identified in a patient with Loeys-Dietz syndrome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28344185            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ZNF32 was found to directly bind to the TGF-betaR2 (transforming growth factor-beta receptor 2) promoter to promote its expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27763636            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High TGFBR2 expression is associated with glioma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28184932            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these findings delineate the important function of the TGFbeta signaling pathway in the early development of kidney and TbetaRII was shown to be able to promote the expression of Six2 through Smad3 mediating transcriptional regulation and in turn activate the proliferation of MM cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28420207            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            YAP-1 promotes Tregs differentiation in hepatocellular carcinoma by enhancing TGFBR2 transcription.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28472799            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Gasdermin C is upregulated by inactivation of Tgfbr2 in the presence of mutated Apc, promoting colorectal cancer cell proliferation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27835699            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Depending on the TGFBR2 expression status of their donor cells, shed exosomes show distinct proteomic signatures and promote altered cytokine secretion profiles in recipient cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28376875            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-520f inhibited tumor cell invasion by directly targeting ADAM9 and the TGFbeta receptor TGFBR2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28209612            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study demonstrated that the TGFBR2 mutation was not present in the sample of cervico-cerebral artery dissection patients (CCAD); however, a positive association was identified between the MTHFR-C677T polymorphism and genetically confirmed Mexican mestizo spontaneous CCAD patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        27017342            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A genetic investigation found a TGFbetaR2 gene mutation, leading to the diagnosis of Loeys-Dietz syndrome type2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27017362            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results showed that transfection of CD34(+) cells with SiRNA targeting TGF-bRII and their co-culture with human bone marrow mesenchymal stromal cells (MSCs) could considerably increase the number of progenitors            \u003ca rel=\"nofollow\"\u003e             PMID:                        27344285            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Cell invasion (matrigel) was reduced only in the Hs578T cells (p \u0026lt; 0.01). Silencing decreased the expression of the prometastatic molecules S100A4 and TGFbetaR2 in both cell lines and CD44 in Hs578T cells. We conclude that ECM1 is a key player in the metastatic process and regulates the actin cytoskeletal architecture of aggressive breast cancer cells at least in part via alterations in S100A4 and Rho A.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27770373            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our study uncovers a novel mechanism that miR-19a-3p\/19b-3p inhibits autophagy-mediated fibrogenesis by targeting TGF-beta R II.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27098600            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGFBR2 signaling can affect Notch1 glycosylation via regulation of glycosyltransferase LFNG expression and provide a first mechanistic example for altered glycosylation in microsatellite instability colorectal tumor cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27156840            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CD44 and TGFBR2 are the functional targets of miR-373, which are responsible for the tumor suppressive functions of miR-373            \u003ca rel=\"nofollow\"\u003e             PMID:                        26858153            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Polymorphism of TGFBR2 is associated with coronary artery disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27234600            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results found TGFBR2 to be significantly related to the regulated phosphoproteome in glioblastoma as a result of integrative upstream kinase\/ regulator analyses and experimentally validated as a novel regulator of glioblastoma stem cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26670566            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Reduced expression of TGF-beta type II receptor and extracellular matrix components in response to reduced fibroblast size\/mechanical force was fully reversed by restoring size\/mechanical force            \u003ca rel=\"nofollow\"\u003e             PMID:                        26780887            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results suggested that high CDKN1A\/p21 and low TGFBR2 expression was closely correlated with adverse pathological parameters and poor prognosis in breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26823785            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings suggest that the upregulation of miR-590-5p promotes cellular malignant behavior via the target gene TGFbetaRII in vulvar squamous cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26498065            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TGFBR2 is regulated by an epigenetic auto-feedback regulation in non-small cell lung cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26356817            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we reported a sporadic Japanese case of LDS with a novel TGFBR2 p.Y424H mutation, which appeared to cause pregnancy-related fatal aortic\/arterial dissections.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26301661            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            AT2R downregulates the expression of TGF-betaRII in human proximal tubule cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        26867007            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High levels of TbetaRII expression were associated with lymph node metastasis, increasing tumor clinical stage, and poorer 5-year disease-free survival in patients with breast cancer. TbetaRII may be a potential prognostic marker for breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26551005            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915099177185,"sku":"BL-0043NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLWyAFW1JAACsRky9aj0436_28cdafbc-d623-410f-aaec-a5439df7b650.jpg?v=1685853205"},{"product_id":"recombinant-mouse-ifngr-protein-fc-tag-bl-0112np","title":"Recombinant Mouse IFNGR1 Protein (C-Fc)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Interferon Gamma Receptor 1 is produced by our Mammalian expression system and the target gene encoding Ala26-Asp253 is expressed with a human IgG1 Fc tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"P15261\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/P15261\/entry\"\u003eP15261\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCD119; Interferon gamma receptor 1; IFNGR1; IFN-gamma receptor 1; IFN-gamma-R1; CD119 antigen; IFN gamma receptor 1; IFNGR; immune interferon receptor 1; interferon gamma receptor 1; interferon-gamma receptor alpha chain\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe tetrameric receptor complex for IFNγ consists of two subunits, IFNGR1 (IFNγ Rα) and IFNGR2 (IFNγ Rβ), through which the dimeric IFN-γ exerts its biological functions, including antiviral, antiproliferation and immune-modulatory activity in mammals. Both IFNGR1 and IFNGR2 are single transmembrane proteins belonging to the class II cytokine family. FNGR1, widely expressed in most host cells, is essential for IFNγ binding, receptor trafficking, and signal transduction. IFNGR1 possesses an intracellular Janus tyrosine kinase (JAK) 1 binding site, a signal transducer and activator of transcription 1 (STAT1) binding site. The resulting STAT1 homodimers translocate from the cytoplasm to the nucleus and bind to the interferon-gamma activated sequence (GAS) promoter to induce expression of downstream interferon stimulated genes (ISGs).\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e53 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e72-94 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915105796321,"sku":"BL-0112NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLZOAEjKxAACUp4q96Mo674_ecb33d5e-6992-467c-b8d5-d74e8ddf5069.jpg?v=1685853467"},{"product_id":"recombinant-mouse-flt3lg-protein-fc-tag-bl-0126np","title":"Recombinant Mouse FLT3LG Protein (C-Fc)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Fms-like Tyrosine Kinase 3 Ligand is produced by our Mammalian expression system and the target gene encoding Gly27-Arg188 is expressed with a human IgG1 Fc tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"P49772\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/P49772\/entry\"\u003eP49772\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFms-related tyrosine kinase 3 ligand (Flt3L); SL cytokine; Flt3 ligand\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFms-related tyrosine kinase 3 ligand(Flt3L) is a single-pass type I membrane protein and consists of 232 amino acids. Flt3L is a hematopoietic four helical bundle cytokine, structurally homologous to stem cell factor and colony stimulating factor. Flt3L synergizes well with a number of other colony stimulating factors and interleukins. Flt3L stimulates the proliferation and differentiation of various blood cell progentiors by activating FLT3.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e45.5 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e58-70 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915105239265,"sku":"BL-0126NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLZaAPBwiAACffxnhf9Q786_74f88a45-065c-469b-bc25-55e32cadc39f.jpg?v=1685853445"},{"product_id":"recombinant-mouse-tgfbr2-protein-fc-tag-bl-0131np","title":"Recombinant Mouse TGFBR2 Protein (C-Fc)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Mouse Transforming Growth Factor-beta Receptor Type II is produced by our Mammalian expression system and the target gene encoding Ile24-Asp159 is expressed with a human IgG1 Fc tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"Q62312-2\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/Q62312\/entry#Q62312-2\"\u003eQ62312-2\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTGF-beta receptor type-2; TGFR-2; TGF-beta type II receptor; Transforming growth factor-beta receptor type II; TGF-beta receptor type II; TbetaR-II; Tgfbr2\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTransforming growth factor-β (TGF-β) is an essential regulator in the processes of development, cell proliferation, and extracellular matrix deposition. TGF-β regulates cellular processes by binding to three high-affinity cell surface receptors: TGF-β receptor type I (TGF-β-RI), TGF-β receptor type II (TGF-β-RII), and TGF-ββ receptor type III (TGF-β-RIII). TGF-β RII is consists of a C-terminal protein kinase domain and an N-terminal ectodomain and belongs to transforming growth factor-beta (TGF-β) receptor subfamily. TGF-β RII has a protein kinase domain which can form a heterodimeric complex with another receptor protein and bind TGF-beta. This receptor\/ligand complex phosphorylates protein will enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e42.3 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e55-65 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBiologically active. Please contact us to obtain bioactivity data.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915105435873,"sku":"BL-0131NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLZeANnS9AACi9IhDeWU340_bff1facb-fc74-40c8-b318-542b6d7aa03b.jpg?v=1685853452"},{"product_id":"recombinant-human-mouse-rat-irisin-protein-fc-tag-bl-0136np","title":"Recombinant Human\/Mouse\/Rat Irisin Protein (C-Fc)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human\/Mouse\/Rat Fibronectin Type III Domain-containing Protein 5  is produced by our Mammalian expression system and the target gene encoding Asp32-Glu143 is expressed with a human IgG1 Fc tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eQ8NAU1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFibronectin type III domain-containing protein 5; Fibronectin type III repeat-containing protein 2; Irisin; FNDC5\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFibronectin type III domain-containing protein 5, the precursor of irisin, is a protein that is encoded by the FNDC5 gene.Human Irisin is synthesized as a 212 amino acid (aa) precursor encoding a type 1 transmembrane protein with a 121 aa extracellular domain (ECD), a 21 aa transmembrane domain, and a 39 aa cytoplasmic domain. The ECD of Irisin contains a fibronectin type III domain and multiple glycosylation sites. The ECD is proteolytically cleaved to release the 112 aa soluble Irisin hormone into circulation.Mature human, mouse share 100% sequence identity.Irisin induces expression of peroxisome proliferatoractivated receptor γ coactivator 1α (PGC1α) and uncoupling protein1(UCP1), mitochondrialassociated metabolic proteins. Irisin induces the transition of white adipose tissue into more metabolically active beige adipose tissue.Irisin also regulates neuronal cell differentiation and neurite outgrowth in the brain and is involved in the differentiation of osteoblasts.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e39.7 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e50-60 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eContrary to mouse, may not be involved in the beneficial effects of muscular exercise, nor in the induction of browning of human white adipose tissue.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCell membrane; Single-pass type I membrane protein. Peroxisome membrane; Single-pass type I membrane protein.; [Irisin]: Secreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            20240           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            611906           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:252995           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000362570           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29673927            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            There is a decrease in serum irisin level in type 2 diabetic patients with even more significant reduction in patients with diabetic nephropathy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28875825            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FNDC5 mRNA expression in skeletal muscle and circulating irisin concentration relatively to exercise mode, intensity, frequency and duration and the characteristics of the sample used            \u003ca rel=\"nofollow\"\u003e             PMID:                        29127759            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum concentrations of irisin are elevated in post-myocardial infarction patients with increased risk for adverse cardiovascular events.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29657036            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Acute high-intensity interval exercise decreased irisin levels and increased myostatin levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29558345            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            serum levels were significantly lower in pre-eclampsia than normotensive pregnancies            \u003ca rel=\"nofollow\"\u003e             PMID:                        29430974            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Glucocorticoid receptor positively regulates transcription of FNDC5 in the liver.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28240298            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study finds that soccer matches performed different workout times have strong stimulatory effects on irisin levels in all subjects but nesfatin-1 response varied among the subjects and it did not change significantly in afternoon match.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30084805            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that Irisin concentration in umbilical cord blood was found to be associated with preterm birth (PTB). On the other hand, no differences in maternal blood irisin levels between mothers with preterm and term deliveries were established.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29997715            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Irisin concentrations do not predict risk of developing diabetes prospectively            \u003ca rel=\"nofollow\"\u003e             PMID:                        29108900            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            serum irisin levels were significantly lower in patients with psoriasis, and associated with serum lipid levels and disease activity; these results can be interpreted that irisin is involved in the disease pathogenesis of patients with psoriasis in relation to metabolic dysregulation            \u003ca rel=\"nofollow\"\u003e             PMID:                        27652568            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study show the serum irisin levels had significant positive correlation with seizure severity Chalfont score and the duration of epilepsy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29860632            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            clinical evidence of the association between serum irisin and vascular calcification in HD patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        29490308            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The pooled data indicated that the levels of irisin were at least 45.78 ng\/ml higher in patients with polycystic ovary syndrome than that in the healthy controls. The current meta-analysis suggested that irisin might contribute to the development of PCOS independent of insulin resistance.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29069945            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            With adjustment for body mass index, circulating irisin in polycystic ovary syndrome patients seems comparable to healthy controls. [meta-analysis]            \u003ca rel=\"nofollow\"\u003e             PMID:                        29217128            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            serum irisin levels were lower in Peritoneal Dialysis patients with Protein Energy Wasting than those of the patients without PEW            \u003ca rel=\"nofollow\"\u003e             PMID:                        29248911            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that decreased irisin levels are associated with metabolic syndrome in prepubertal children; irisin may be a biomarker for metabolic syndrome in prepubertal children. This study was conducted in Seoul, Republic of Korea.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28904307            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings revealed that irisin may play a critical role in the IL-6-induced epithelialmesenchymal transition of osteosarcoma cells via the STAT3\/Snail signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29048621            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FNDC5 gene interactions with candidate genes FOXOA3 and APOE            \u003ca rel=\"nofollow\"\u003e             PMID:                        29143599            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Irisin is negatively associated with serum testosterone in apopulation sample of men with Metabolic syndrome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28759938            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Irisin replenishment in mCaROCK1 mice partially reversed insulin resistance.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27411515            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Suggest that irisin exerts beneficial effect on mood in COPD patients, possibly by inducing the expression of BDNF in brain areas associated with reward-related processes involved in by depression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28744117            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Modulation of Irisin and Physical Activity on Executive Functions in Obesity and Morbid obesity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27476477            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Obese children had significantly higher irisin and lower oxytocin levels than the healthy controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28077341            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We determined FNDC5 polymorphisms frequencies in the Israeli population and demonstrated that maternal and neonatal FNDC5 rs726344 polymorphism is significantly associated with increased risk for preterm birth. Women bearing FNDC5 rs726344 GG genotype had 2.18 fold higher chance to deliver on time compared to AG and AA genotypes.Neonatal carrying FNDC5 rs726344 GG genotype had 2.24 fold higher chance to be born on time.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29408625            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Lower levels of irisin are independently associated with elevated skin AF values, indicating that circulating irisin levels could be associated with AGEs accumulation, which is one of the reasons causing vascular complications in diabetic patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28408433            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Association of Irisin Plasma Levels with Anthropometric Parameters in Children with Underweight, Normal Weight, Overweight, and Obesity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28553647            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            irisin was significantly higher in obese than in control children, and was inversely correlated with Acrp30 and high molecular weight (HMW) oligomers; inverse correlation between Irisin and Acrp30 and, more significantly, between Irisin and HMW oligomers suggests that the two cytokines are closely connected            \u003ca rel=\"nofollow\"\u003e             PMID:                        28385328            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Irisin is an oxidative stress marker and a metabolic protective hormone.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28277125            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mild cold exposure increased vasoconstriction with a drop in in-the-ear temperature and these were related. Greater irisin was related to a greater fasting fat oxidation in the absence of shivering            \u003ca rel=\"nofollow\"\u003e             PMID:                        27006247            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Activation of the nuclear receptor constitutive androstane receptor (CAR) induced FNDC5 mRNA expression in the liver.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27007446            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HCC-liver tissue over-expressed FNDC5\/Irisin in association with gene expression of mediators involved in lipogenesis, inflammation and cancer, suggesting a possible protective role of the hormone from the liver damage.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28012856            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The secretion of FNDC5 from myotubes and beta-cells in response to exogenous fatty acids, the effects of recombinant FNDC5 on insulin biosynthesis and glucose-stimulated insulin secretion, and beta-cell apoptosis are reported.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28724742            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Irisin regulates the number and function of endothelial progenitor cells via the PI3K\/Akt\/eNOS pathway in mouse model of diabetes mellitus.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27002278            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            there is a correlation between sport performance, insulin sensitivity, and irisin levels            \u003ca rel=\"nofollow\"\u003e             PMID:                        28386566            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results firstly revealed that irisin mitigated oxygen-glucose deprivation-induced neuronal injury in part via inhibiting ROS-NLRP3 inflammatory signaling pathway, suggesting a likely mechanism for irisin-induced therapeutic effect in ischemic stroke.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28961497            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data indicate that increased irisin levels may have protective roles in liver cancer cells through partial activation of the PI3K\/AKT pathway, which may facilitate liver cancer progression and decrease the sensitivity to chemotherapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28867187            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Decreased serum irisin levels are related to emphysema in patients with COPD and involved in epithelial apoptosis, resulting in emphysema.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28424548            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Irisin levels are lower in MI and CAD implying that their production may depend on myocardial blood supply.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28732565            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings suggest that irisin plays an important role in metabolic disorders and may be affected by physiopathological status.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28732566            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The FNDC5 rs3480 variant is associated with protection from clinically significant fibrosis in patients with NAFLD, while irisin expression is correlated with the severity of NAFLD and may be involved in extracellular matrix deposition. These data suggest that irisin is involved in regulation of hepatic fibrogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28472477            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The median irisin levels were determined higher in T1DM group compared to the control one.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28222023            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The modulation of body composition and muscle strength induced by 16-week of resistance training in older women with and without obesity is not associated with changes in circulating Irisin levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28244561            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            serum irisin levels were correlated with anthropometric and metabolic markers of obesity and type 2 diabetes mellitus .            \u003ca rel=\"nofollow\"\u003e             PMID:                        27220658            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Plasma irisin modestly increases during moderate and high-intensity afternoon exercise in obese females.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28125733            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            correlation between irisin and adiposity related factors suggests that that in the case of this clinical model, irisin is regulated by adiposity and not by GH            \u003ca rel=\"nofollow\"\u003e             PMID:                        27472279            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Collectively, our study identified serum irisin as a predictive biomarker for 1-year all-cause mortality in acute heart failure patients though large multicenter studies are highly needed.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28595171            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            T2DM and diabetic nephropathy are associated with decreased levels of irisin. FNDC5 rs16835198 TT genotype associates with decreased risk of T2DM in Egyptians with no effect on renal complications. Also, G allele has insulin desensitizing action with no association with circulating irisin levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28479383            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            irisin might serve as a possible signal for linking body fat\/muscle mass with the hypothalamic center governing reproductive function            \u003ca rel=\"nofollow\"\u003e             PMID:                        27692156            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate that cytokines might predict irisin concentration in mothers and their offspring.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27828992            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915101176033,"sku":"BL-0136NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLZmAUtpEAACtZX_Pssw244_62a7013d-2700-4796-928c-762402f289d1.jpg?v=1685853286"},{"product_id":"recombinant-human-opg-protein-fc-tag-bl-0229np","title":"Recombinant Human OPG Protein (C-Fc)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Osteoprotegerin is produced by our Mammalian expression system and the target gene encoding Glu22-Leu201 is expressed with a human IgG1 Fc tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eO00300\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTumor necrosis factor receptor superfamily member 11B; Osteoclastogenesis inhibitory factor; Osteoprotegerin; TNFRSF11B; OCIF; OPG\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTNFRSF11B is a secreted protein, containing 2 death domains and 4 TNFR-Cys repeats. TNFRSF11B is a decoy receptor for the receptor activator of nuclear factor kappa B ligand (RANKL). By binding RANKL, TNFRSF11B inhibits nuclear kappa B (NF-κB) which is a central and rapid acting transcription factor for immune-related genes, and a key regulator of inflammation, innate immunity, and cell survival and differentiation. TNFRSF11B levels are influenced by voltage-dependent calcium channelsCav1.2. TNFRSF11B can reduce the production of osteoclasts by inhibiting the differentiation of osteoclast precursors into osteoclasts and also regulates the resorption of osteoclasts in vitroand in vivo. TNFRSF11B binding to RANKL on osteoblast\/stromal cells, blocks the RANKL-RANK ligand interaction between osteoblast\/stromal cells and osteoclast precursors. This has the effect of inhibiting the differentiation of the osteoclast precursor into a mature osteoclast.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e47.2 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e50-80 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eActs as decoy receptor for TNFSF11\/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10\/TRAIL and protect against apoptosis. TNFSF10\/TRAIL binding blocks the inhibition of osteoclastogenesis.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            11909           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            239000           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4982           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000297350           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28867452            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            OPG is one promising susceptibility gene of bone mineral density or osteoporotic fractures.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28496203            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The concentration of circulating osteoprotegerin can be a biomarker for both medial artery calcification and atherosclerosis in patients with chronic kidney disease (CKD); OPG might be an early indicator of all-cause mortality in CKD patients with advanced medial arterial calcification            \u003ca rel=\"nofollow\"\u003e             PMID:                        29974642            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We conclude that non-small cell lung cancer patients have a higher content of OPG in bronchoalveolar lavage fluid than healthy people.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29052177            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            positive correlation of OPG with age and an inverse correlation with IGF-I favor the compensatory response of OPG against bone loss in the aging skeleton            \u003ca rel=\"nofollow\"\u003e             PMID:                        29895074            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results indicated that mice treated with low levels of human recombinant OPG may have a more stable aneurysmal phenotype due to compensatory production of collagen and increased vessel wall thickness of the aorta, potentially protecting the aneurysm from rupture.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29749489            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TNF-alpha, DKK1, and OPG have roles in pathogenesis of knee osteoarthritis            \u003ca rel=\"nofollow\"\u003e             PMID:                        28676900            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPG mRNA expression was higher in tumour tissue from patients with metastatic prostate cancer compared to local disease. The RANKL\/OPG ratio was low in normal prostate tissue and high in tumours with bone metastases. Expression was high in BPH tissue but did not exceed as much as in the tumour tissue.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29204705            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results of this study concluded that the RANK, RANK-L and OPG system participates in bone remodeling after RME            \u003ca rel=\"nofollow\"\u003e             PMID:                        29297549            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In cardiovascular risks, OPG serum level might increase as a preventive compensatory mechanism to neutralize the RANKL level increment. The determination of the OPG-RANKL system is a diagnostic indicator for the intensity of vascular calcification and atherosclerosis in SSc patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29336616            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Demonstrate that rs3134069 in TNFRSF11B increases risk of ischemic stroke by decreasing TNFRSF11B expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29501268            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            sRANKL and OPG may play a role in the pathogenesis of diabetes as well as metabolic disturbance            \u003ca rel=\"nofollow\"\u003e             PMID:                        28146138            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The study revealed an enhanced sensitivity of aortic valve interstitial cells to osteogenic inductors in aortic stenosis patients, which indicates probable implication of OPN, OPG, and BMP2 genes in pathogenesis of aortic valve calcification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29308559            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Patients with metabolic syndrome have increased osteoprotegerin serum levels than healthy individuals; osteoprotegerin plays an important role in the development of arteriosclerosis, and the effect of osteoprotegerin on intima media thickness strongly depends on the extent of arteriosclerotic changes in metabolic syndrome            \u003ca rel=\"nofollow\"\u003e             PMID:                        29077157            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In African-Americans, higher OPG levels were associated with characteristics common in patients with heart failure with preserved ejection fraction (HFpEF) and were significantly associated with known precursors to HFpEF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28787318            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            rs2073618 not associated with bone mineral density            \u003ca rel=\"nofollow\"\u003e             PMID:                        28488893            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TRACP-5b level is significantly associated with the OPG level and with the severity and extent of coronary atherosclerosis in coronary artery disease patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        28428481            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Vascular smooth cells are a significant source of osteoprotegerin within the vasculature but that RANKL, once present, downregulates this production and appears capable of preventing the \"protective\" upregulation of OPG seen with VSMCs exposed to physiological levels of cyclic strain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29635231            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            higher serum OPG levels represent an independent risk factor for cardiovascular and fracture risk.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28677166            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            For the OPG gene, an association was observed between the group with chronic arthralgia and joint TMD and the control group (P=0.04). There was also a tendency towards an association of the haplotype CGCCAA with an increased risk of developing chronic joint pain, even in the absence of TMD (P=0.06).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28464982            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Vitamin D, tumor necrosis factor (TNF)-alpha, receptor activator of nuclear factor-KB ligand (RANKL), and OPG levels were determined in GCF and serum. Baseline clinical parameters were similar in all periodontitis groups (P \u0026gt; 0.05) but were higher than that in controls            \u003ca rel=\"nofollow\"\u003e             PMID:                        28904316            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Adipose-derived stem cell-released osteoprotegerin protects cardiomyocytes from reactive oxygen species-induced cell death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28931423            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            down-regulated miR-143-5p promotes the differentiation of DPSCs into odontoblasts by enhancing Runx2 expression via the OPG\/RANKL signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28608628            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPG and OPG\/TRAIL ratio expression were significantly increased in rheumatoid arthritis patients compared to controls (fold change = 1.79, p = 0.013 and 2.07, p = 0.030, respectively), RANKL\/OPG ratio was significantly decreased (fold change = 0.50, p = 0.020). No significant differences were found between patients and controls in RANKL and TRAIL expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27403809            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Elevated OPG was a strong and independent predictor of longterm cardiovascular mortality, even after adjustment for traditional risk factors. Low levels of both OPG and act vWF were associated with a 99 % survival rate during the follow-up of five years.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28726980            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study revealed a significant elevation of circulating OPG in septic patients with different levels of severity and those who progressed to AKI.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28840836            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studied association between osteoprotegerin gene polymorphisms and osteoporosis in Roma and non-Roma postmenopausal women in Eastern Slovakia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27859736            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In type 2 diabetes patients HMGB-1 and OPG serum levels are higher in patients affected by peripheral arterial disease and independently associated with its occurrence and clinical severity            \u003ca rel=\"nofollow\"\u003e             PMID:                        28789654            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The epicardial adipose tissue expresses the mRNA of osteopontin, osteoprotegerin, and osteonectin genes that have been implicated in the calcification process; such expression is statistically associated with some components of HDL subclasses in coronary artery disease patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28821297            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum osteoprotegerin level is significantly associated with both the presence and severity of peripheral arterial disease in patients with type 2 diabetes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29313442            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum osteoprotegerin was the strongest risk factor associated with new development and rapid progression of arterial calcification in incident peritoneal dialysis patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28614819            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            concluded that in Mexican-Mestizo female patients with rheumatoid arthritis, the rs2073618 polymorphism of the TNRFS11B gene is not associated with low bone mineral density            \u003ca rel=\"nofollow\"\u003e             PMID:                        28758134            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Osteoprotegerin was associated with chronic kidney disease in hypertensive patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28683789            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that, in children with type I diabetes, serum levels of osteoprotegerin are up-regulated, serum levels of RANKL are unchanged, and serum levels of fetuin-A are down-regulated. (RANKL = receptor activator of nuclear factor kappa B ligand)            \u003ca rel=\"nofollow\"\u003e             PMID:                        27028343            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate a significant inverse relationship between plasma osteoprotegerin (OPG) levels and breast cancer risk among women with an inherited BRCA1 or BRCA2 mutation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27893411            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Progressive calcification of atherosclerotic plaques is accompanied by insignificant accumulation of calcitonin and osteoprotegerin, whereas the osteocalcin expression significantly increased during calcification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28429221            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Elevated serum ferritin concentrations and bone remodeling marker, osteoprotegerin, are independent predictors of hip fracture in postmenopausal women hospitalized for fragility fracture.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27503623            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results showed that colorectal liver metastasis tissues exhibited significantly reduced expression of osteoprotegerin compared to primary colorectal carcinomas and normal colorectal mucosa. This reduced expression was significantly associated with the extent of colorectal liver metastasis, including multiplicity of metastatic tumors, involvement of the bilateral hepatic lobes, and higher histological grade.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27764814            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that the RANKL\/RANK\/OPG system is deregulated in post-menopausal women at high risk for breast cancer and in women with circulating tumor cells. Thus, serum levels of RANKL\/OPG are potentially indicative of predisposition and progression of breast cancer in humans.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28002811            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High OPG expression is associated with triple negative breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27015557            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            show for the first time that OPG improves risk stratification for cardiovascular events in a non-dialysis chronic kidney disease population            \u003ca rel=\"nofollow\"\u003e             PMID:                        27016924            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPG has a role in cancer progression, especially breast cancer [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27072583            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPG rs2073618 polymorphism could be a possible genetic marker for the prediction of increased risk for carotid plaque burden as a measure of advanced subclinical atherosclerosis in T2DM subjects.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28593808            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The compound with greatest potential is E05657 with high activity and low effective concentration in the HTS system. It increases the OPG\/RANKL ratio and OPG secretion, decreases the NFATc1 expression, and reduces osteoclastogenesis in vitro            \u003ca rel=\"nofollow\"\u003e             PMID:                        27301430            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPG T950C polymorphism might be associated with an increased osteoporosis risk in the Chinese population            \u003ca rel=\"nofollow\"\u003e             PMID:                        29253005            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We have concluded that low OPG levels may be associated with osteoporosis in ulcerative colitis, but it is not correlated with the c.-223C \u0026gt; T polymorphism in the TNFRSF11B gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27639566            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RANKL\/Osteoprotegerin have roles in bone turnover in Hashimoto Thyroiditis            \u003ca rel=\"nofollow\"\u003e             PMID:                        27328677            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High OPG expression is associated with colorectal carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26942563            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that elevated plasma levels of osteoprotegerin\/TNFRSF11B correlate with increased risk of cardiovascular comorbidities in children and adolescents with type 1 diabetes (as compared to healthy control subjects); thus, osteoprotegerin\/TNFRSF11B may serve as biomarker of cardiovascular risk in these patients. This study was conducted in Tunisia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27111559            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studies showed that the central hypothalamic-pituitary regulatory system, via it's relative hormones, seems to control OPG\/RANKL\/RANK system function, and the pulsatility and circadian rhythmicity of these hormones may induce an oscillatory fluctuation of the OPG\/ RANKL ratio. Also, psycological characteristics may provoke a shift of the OPG\/ RANKL ratio towards an unbalanced or a balanced status. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27862210            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915102585057,"sku":"BL-0229NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLZOAO_ZQAACW-oArFpw368_1374a61b-0c95-4c0e-8056-abda7b222c3c.jpg?v=1685853348"},{"product_id":"recombinant-human-relt-protein-fc-tag-bl-0237np","title":"Recombinant Human RELT Protein (C-Fc)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Receptor Expressed in Lymphoid Tissues is produced by our Mammalian expression system and the target gene encoding Ser26-Ala160 is expressed with a human IgG1 Fc tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eQ969Z4\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTumor necrosis factor receptor superfamily member 19L; TNFRSF19L; Receptor expressed in lymphoid tissues; RELT\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTumor necrosis factor receptor superfamily member 19L (TNFRSF19L), also known as Receptor expressed in lymphoid tissues and RELT, is a member of the TNF-receptor superfamily. TNFRSF19L is a single-pass type membrane protein and contains one TNFR-Cys repeat. TNFRSF19L is highly expressed in spleen, lymph node, thymus, peripheral blood leukocytes, bone marrow and fetal liver. It has been shown TNFRSF19L activates the NF-kappaB pathway and selectively binds TNF receptor-associated factor 1 (TRAF1). TNFRSF19L is capable of stimulating T-cell proliferation in the presence of CD3 signaling, which suggests its regulatory role in immune response.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e41.4 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e40-60 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSupplied as a 0.2 μm filtered solution of PBS, pH7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eStore at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped on dry ice\/polar packs.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMay play a role in apoptosis. Induces activation of MAPK14\/p38 and MAPK8\/JNK MAPK cascades, when overexpressed. Involved in dental enamel formation.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eCell membrane; Single-pass type I membrane protein. Cytoplasm. Cytoplasm, perinuclear region.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRELT family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            13764           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            611211           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:84957           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000064780           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28688764            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            report that overexpression of RELT or its homologues RELL1 and RELL2 in HEK 293 epithelial cells results in cell death with morphological characteristics consistent with the activation of an apoptotic pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19969290            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Receptor expressed in lymphoid tissue (RELT) and its novel homologues RELL1 and RELL2 co-localize with one another at the plasma membrane.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16389068            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915105698017,"sku":"BL-0237NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/rB9Eh2Q2vnaAUBwJAACuOF9cIxA036_5ac97d75-4e7a-4e19-9483-d77ee0837bf8.jpg?v=1685853463"},{"product_id":"recombinant-human-opg-protein-his-tag-bl-0300np","title":"Recombinant Human OPG Protein (C-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Osteoprotegerin is produced by our Mammalian expression system and the target gene encoding Glu22-Leu401 is expressed with a 6His tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eO00300\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTumor Necrosis Factor Receptor Superfamily Member 11B; Osteoclastogenesis Inhibitory Factor; Osteoprotegerin; TNFRSF11B; OCIF; OPG\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eTNFRSF11B is a secreted protein, containing 2 death domains and 4 TNFR-Cys repeats. TNFRSF11B is a decoy receptor for the receptor activator of nuclear factor kappa B ligand (RANKL). By binding RANKL, TNFRSF11B inhibits nuclear kappa B (NF-κB) which is a central and rapid acting transcription factor for immune-related genes, and a key regulator of inflammation, innate immunity, and cell survival and differentiation. TNFRSF11B levels are influenced by voltage-dependent calcium channelsCav1.2. TNFRSF11B can reduce the production of osteoclasts by inhibiting the differentiation of osteoclast precursors (osteoclasts are related to monocytes\/macrophages and are derived from granulocyte\/macrophage-forming colony units (CFU-GM)) into osteoclasts and also regulates the resorption of osteoclasts in vitroand in vivo. TNFRSF11B binding to RANKL on osteoblast\/stromal cells, blocks the RANKL-RANK ligand interaction between osteoblast\/stromal cells and osteoclast precursors. This has the effect of inhibiting the differentiation of the osteoclast precursor into a mature osteoclast.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e44.65 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e57 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eActs as decoy receptor for TNFSF11\/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10\/TRAIL and protect against apoptosis. TNFSF10\/TRAIL binding blocks the inhibition of osteoclastogenesis.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            11909           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            239000           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4982           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000297350           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28867452            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            OPG is one promising susceptibility gene of bone mineral density or osteoporotic fractures.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28496203            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The concentration of circulating osteoprotegerin can be a biomarker for both medial artery calcification and atherosclerosis in patients with chronic kidney disease (CKD); OPG might be an early indicator of all-cause mortality in CKD patients with advanced medial arterial calcification            \u003ca rel=\"nofollow\"\u003e             PMID:                        29974642            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We conclude that non-small cell lung cancer patients have a higher content of OPG in bronchoalveolar lavage fluid than healthy people.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29052177            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            positive correlation of OPG with age and an inverse correlation with IGF-I favor the compensatory response of OPG against bone loss in the aging skeleton            \u003ca rel=\"nofollow\"\u003e             PMID:                        29895074            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results indicated that mice treated with low levels of human recombinant OPG may have a more stable aneurysmal phenotype due to compensatory production of collagen and increased vessel wall thickness of the aorta, potentially protecting the aneurysm from rupture.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29749489            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TNF-alpha, DKK1, and OPG have roles in pathogenesis of knee osteoarthritis            \u003ca rel=\"nofollow\"\u003e             PMID:                        28676900            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPG mRNA expression was higher in tumour tissue from patients with metastatic prostate cancer compared to local disease. The RANKL\/OPG ratio was low in normal prostate tissue and high in tumours with bone metastases. Expression was high in BPH tissue but did not exceed as much as in the tumour tissue.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29204705            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results of this study concluded that the RANK, RANK-L and OPG system participates in bone remodeling after RME            \u003ca rel=\"nofollow\"\u003e             PMID:                        29297549            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In cardiovascular risks, OPG serum level might increase as a preventive compensatory mechanism to neutralize the RANKL level increment. The determination of the OPG-RANKL system is a diagnostic indicator for the intensity of vascular calcification and atherosclerosis in SSc patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29336616            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Demonstrate that rs3134069 in TNFRSF11B increases risk of ischemic stroke by decreasing TNFRSF11B expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29501268            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            sRANKL and OPG may play a role in the pathogenesis of diabetes as well as metabolic disturbance            \u003ca rel=\"nofollow\"\u003e             PMID:                        28146138            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The study revealed an enhanced sensitivity of aortic valve interstitial cells to osteogenic inductors in aortic stenosis patients, which indicates probable implication of OPN, OPG, and BMP2 genes in pathogenesis of aortic valve calcification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29308559            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Patients with metabolic syndrome have increased osteoprotegerin serum levels than healthy individuals; osteoprotegerin plays an important role in the development of arteriosclerosis, and the effect of osteoprotegerin on intima media thickness strongly depends on the extent of arteriosclerotic changes in metabolic syndrome            \u003ca rel=\"nofollow\"\u003e             PMID:                        29077157            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In African-Americans, higher OPG levels were associated with characteristics common in patients with heart failure with preserved ejection fraction (HFpEF) and were significantly associated with known precursors to HFpEF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28787318            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            rs2073618 not associated with bone mineral density            \u003ca rel=\"nofollow\"\u003e             PMID:                        28488893            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TRACP-5b level is significantly associated with the OPG level and with the severity and extent of coronary atherosclerosis in coronary artery disease patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        28428481            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Vascular smooth cells are a significant source of osteoprotegerin within the vasculature but that RANKL, once present, downregulates this production and appears capable of preventing the \"protective\" upregulation of OPG seen with VSMCs exposed to physiological levels of cyclic strain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29635231            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            higher serum OPG levels represent an independent risk factor for cardiovascular and fracture risk.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28677166            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            For the OPG gene, an association was observed between the group with chronic arthralgia and joint TMD and the control group (P=0.04). There was also a tendency towards an association of the haplotype CGCCAA with an increased risk of developing chronic joint pain, even in the absence of TMD (P=0.06).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28464982            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Vitamin D, tumor necrosis factor (TNF)-alpha, receptor activator of nuclear factor-KB ligand (RANKL), and OPG levels were determined in GCF and serum. Baseline clinical parameters were similar in all periodontitis groups (P \u0026gt; 0.05) but were higher than that in controls            \u003ca rel=\"nofollow\"\u003e             PMID:                        28904316            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Adipose-derived stem cell-released osteoprotegerin protects cardiomyocytes from reactive oxygen species-induced cell death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28931423            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            down-regulated miR-143-5p promotes the differentiation of DPSCs into odontoblasts by enhancing Runx2 expression via the OPG\/RANKL signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28608628            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPG and OPG\/TRAIL ratio expression were significantly increased in rheumatoid arthritis patients compared to controls (fold change = 1.79, p = 0.013 and 2.07, p = 0.030, respectively), RANKL\/OPG ratio was significantly decreased (fold change = 0.50, p = 0.020). No significant differences were found between patients and controls in RANKL and TRAIL expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27403809            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Elevated OPG was a strong and independent predictor of longterm cardiovascular mortality, even after adjustment for traditional risk factors. Low levels of both OPG and act vWF were associated with a 99 % survival rate during the follow-up of five years.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28726980            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study revealed a significant elevation of circulating OPG in septic patients with different levels of severity and those who progressed to AKI.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28840836            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studied association between osteoprotegerin gene polymorphisms and osteoporosis in Roma and non-Roma postmenopausal women in Eastern Slovakia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27859736            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In type 2 diabetes patients HMGB-1 and OPG serum levels are higher in patients affected by peripheral arterial disease and independently associated with its occurrence and clinical severity            \u003ca rel=\"nofollow\"\u003e             PMID:                        28789654            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The epicardial adipose tissue expresses the mRNA of osteopontin, osteoprotegerin, and osteonectin genes that have been implicated in the calcification process; such expression is statistically associated with some components of HDL subclasses in coronary artery disease patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28821297            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum osteoprotegerin level is significantly associated with both the presence and severity of peripheral arterial disease in patients with type 2 diabetes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29313442            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum osteoprotegerin was the strongest risk factor associated with new development and rapid progression of arterial calcification in incident peritoneal dialysis patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28614819            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            concluded that in Mexican-Mestizo female patients with rheumatoid arthritis, the rs2073618 polymorphism of the TNRFS11B gene is not associated with low bone mineral density            \u003ca rel=\"nofollow\"\u003e             PMID:                        28758134            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Osteoprotegerin was associated with chronic kidney disease in hypertensive patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28683789            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that, in children with type I diabetes, serum levels of osteoprotegerin are up-regulated, serum levels of RANKL are unchanged, and serum levels of fetuin-A are down-regulated. (RANKL = receptor activator of nuclear factor kappa B ligand)            \u003ca rel=\"nofollow\"\u003e             PMID:                        27028343            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate a significant inverse relationship between plasma osteoprotegerin (OPG) levels and breast cancer risk among women with an inherited BRCA1 or BRCA2 mutation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27893411            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Progressive calcification of atherosclerotic plaques is accompanied by insignificant accumulation of calcitonin and osteoprotegerin, whereas the osteocalcin expression significantly increased during calcification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28429221            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Elevated serum ferritin concentrations and bone remodeling marker, osteoprotegerin, are independent predictors of hip fracture in postmenopausal women hospitalized for fragility fracture.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27503623            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results showed that colorectal liver metastasis tissues exhibited significantly reduced expression of osteoprotegerin compared to primary colorectal carcinomas and normal colorectal mucosa. This reduced expression was significantly associated with the extent of colorectal liver metastasis, including multiplicity of metastatic tumors, involvement of the bilateral hepatic lobes, and higher histological grade.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27764814            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that the RANKL\/RANK\/OPG system is deregulated in post-menopausal women at high risk for breast cancer and in women with circulating tumor cells. Thus, serum levels of RANKL\/OPG are potentially indicative of predisposition and progression of breast cancer in humans.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28002811            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High OPG expression is associated with triple negative breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27015557            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            show for the first time that OPG improves risk stratification for cardiovascular events in a non-dialysis chronic kidney disease population            \u003ca rel=\"nofollow\"\u003e             PMID:                        27016924            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPG has a role in cancer progression, especially breast cancer [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27072583            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPG rs2073618 polymorphism could be a possible genetic marker for the prediction of increased risk for carotid plaque burden as a measure of advanced subclinical atherosclerosis in T2DM subjects.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28593808            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The compound with greatest potential is E05657 with high activity and low effective concentration in the HTS system. It increases the OPG\/RANKL ratio and OPG secretion, decreases the NFATc1 expression, and reduces osteoclastogenesis in vitro            \u003ca rel=\"nofollow\"\u003e             PMID:                        27301430            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPG T950C polymorphism might be associated with an increased osteoporosis risk in the Chinese population            \u003ca rel=\"nofollow\"\u003e             PMID:                        29253005            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We have concluded that low OPG levels may be associated with osteoporosis in ulcerative colitis, but it is not correlated with the c.-223C \u0026gt; T polymorphism in the TNFRSF11B gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27639566            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RANKL\/Osteoprotegerin have roles in bone turnover in Hashimoto Thyroiditis            \u003ca rel=\"nofollow\"\u003e             PMID:                        27328677            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High OPG expression is associated with colorectal carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26942563            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that elevated plasma levels of osteoprotegerin\/TNFRSF11B correlate with increased risk of cardiovascular comorbidities in children and adolescents with type 1 diabetes (as compared to healthy control subjects); thus, osteoprotegerin\/TNFRSF11B may serve as biomarker of cardiovascular risk in these patients. This study was conducted in Tunisia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27111559            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studies showed that the central hypothalamic-pituitary regulatory system, via it's relative hormones, seems to control OPG\/RANKL\/RANK system function, and the pulsatility and circadian rhythmicity of these hormones may induce an oscillatory fluctuation of the OPG\/ RANKL ratio. Also, psycological characteristics may provoke a shift of the OPG\/ RANKL ratio towards an unbalanced or a balanced status. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27862210            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915103928545,"sku":"BL-0300NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLUCATk9tAACe3bMjRig370_88104d51-43f8-487d-9124-fc2bc59b3ae9.jpg?v=1685853396"},{"product_id":"recombinant-human-rspo1-protein-his-tag-bl-0319np","title":"Recombinant Human RSPO1 Protein (C-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human R-spondin-1 is produced by our Mammalian expression system and the target gene encoding Ser21-Ala263 is expressed with a 6His tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eQ2MKA7\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRSPO1; R-spondin1; RP11-566C13.1; CRISTIN3; FLJ40906; RSPO Rspo1; R-spondin; Rspondin; RP23-325M14.2; Roof plate-specific spondin-1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRSPO1 is a secreted protein,containing 2 FU(furin-like) repeats and 1 TSP type-1 domain and belonging to the R-spondin family. RSPO1 is required for the early development of gonads, regardless of sex. It has been found in mice only eleven days after fertilization. To induce cell proliferation, it acts synergistically with WNT4. They help stabilize β catenin, which activates downstream targets. RSPO1 is necessary in female sex development. It augments the WNT\/β catenin pathway to oppose male sex development. In critical gonadal stages, between six and nine weeks after fertilization, the ovaries upregulate it while the testes downregulate it. RSPO1 can potentially aid in the treatment of mucositis, which is characterized by inflammation of the oral cavity. This unfortunate condition often accompanies chemotherapy and radiation in cancer patients with head and neck tumors.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e27.8 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e40 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.01 EU\/µg as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eBiologically active. Please contact us to obtain bioactivity data.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eActivator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt\/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. Has a essential roles in ovary determination. Regulates Wnt signaling by antagonizing DKK1\/KREM1-mediated internalization of LRP6 through an interaction with KREM1.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted. Nucleus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eR-spondin family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            21679           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            609595           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:284654           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000348944           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29262419            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Rspo1 increases the number of Lgr5(+) liver stem cells in human liver fibrosis tissues, and once they are isolated, these cells are able to form organoids, and treatment with HGF\/Rspo1 promotes their expansion            \u003ca rel=\"nofollow\"\u003e             PMID:                        29079780            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RSPOs facilitate HSC activation and promote liver fibrogenesis by enhancing the Wnt pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        27572318            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Role of RSPO1 in gastric cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        28219935            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results showed that Rspo1 expression is downregulated in adult follicles but its activation is sufficient in promoting ovarian tumors supporting its direct involvement in the initiation of ovarian cancers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27270435            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We highlight the cooperation of WNT4, RSPO1 and FOXL2 within a regulatory network and the need for further research to better understand their role in defining and maintaining ovarian identity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27604691            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Rspo1 glycosylation at Asn137 is essential for secretion and stability but not for heparin binding.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27314333            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            DPY19L3-mediated C-mannosylation of Rspo1 at tryptophan(156) is required for Rspo1 secretion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26764097            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genetic variants in ZC3H11B, RSPO1, and GJD2 are associated with susceptibility to the development of high myopia in a Han Chinese population.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26485405            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            R-Spondin1 has an effect on radiosensitivity of glioma cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        25865226            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ZNRF3 and LGR4-binding sites in RSPO1 are required for Wnt signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24165923            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Changes in the expression levels of IRS1, IRS2, RIPK2, RSPO1, and DNA JC15 genes might contribute to the development of insulin resistance and glucose intolerance in the obese boys.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26040030            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the LGR4-Rspo1 complex crystal structure shows divergent mechanisms of ligand recognition by leucine-rich repeat G-protein-coupled receptors            \u003ca rel=\"nofollow\"\u003e             PMID:                        25480784            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ZNRF3 binds RSPO1 and LGR5-RSPO1 with micromolar affinity via RSPO1 furin-like 1 (Fu1) domain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24349440            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            overexpressed in fibrotic liver tissue            \u003ca rel=\"nofollow\"\u003e             PMID:                        25218283            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Loss of RSPO1 expression is associated with invasive ductal carcinoma of the breast.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24373193            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RSPO-LGR4 not only induces the clearance of RNF43\/ZNRF3 to increase Wnt receptor levels but also recruits IQGAP1 into the Wnt signaling complex.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24639526            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Crystal structures of the Lgr4 ectodomain alone and bound to Rspo1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23891289            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In conclusion, present study highlights the role of Rspo 1 in bone remodeling where it activates Wnt signaling to induce differentiation, as shown in human as well murine in vitro osteoblast cell models.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23617070            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Recent developments have demonstrated that ovarian development is an active process (rather than a default process); ovarian development\/function requires expression of RSPO1, WNT4, and FOXL2. [REVIEW]            \u003ca rel=\"nofollow\"\u003e             PMID:                        23044875            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            R-Spondin potentiates Wnt\/beta-catenin signaling through orphan receptors LGR4 and LGR5            \u003ca rel=\"nofollow\"\u003e             PMID:                        22815884            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study provides new mechanistic insights into the regulation of Wnt receptor turnover, and reveals ZNRF3 as a tractable target for therapeutic exploration            \u003ca rel=\"nofollow\"\u003e             PMID:                        22575959            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            R-spondin1 is upregulated during critical stages of early human ovary development and may function as a tissue-specific amplifier of beta-catenin signaling to oppose testis determination.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21297984            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            identified a gene, R-spondin1, with potent and specific proliferative effects on intestinal crypt cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        16109882            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Human R-spondin1 (RSPO1) is the gene disrupted in a recessive syndrome characterized by XX sex reversal, palmoplantar hyperkeratosis and predisposition to squamous cell carcinoma of the skin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17041600            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RSPO1 regulates Wnt signaling by inhibiting internalization of LRP6.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17804805            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mutational analysis of the RSPO1 gene in a 46,XX woman with true hermaphroditism, palmoplantar keratoderma, congenital bilateral corneal opacities, onychodystrophy, and hearing impairment, is reported.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18085567            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            R-sponin1 (Rspo1) acted synergistically with Wnt3A to activate Wnt\/beta-catenin signaling in the uncommitted mesenchymal C2C12 cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18242177            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SRY represses the transcriptional of the Rspo1\/Wnt target genes involved in ovarian determination.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19376480            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mice treated with R-spondin1 showed increased intestinal epithelial healing, providing a protective effect against chemotherapy-induced intestinal mucositis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16306530            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915096719585,"sku":"BL-0319NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLb6AcEAHAACpaIwQyNc576_791eaa44-1cc6-4b0d-9a7d-ea5fe8f1c7c8.jpg?v=1685853112"},{"product_id":"recombinant-human-hmgb1-protein-his-tag-bl-0424np","title":"Recombinant Human HMGB1 Protein (C-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human High Mobility Group Protein B1 is produced by our Mammalian expression system and the target gene encoding Gly2-Glu215 is expressed with a 6His tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP09429\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHigh Mobility Group Protein B1; High Mobility Group Protein 1; HMG-1; HMGB1; HMG1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHigh mobility group protein B1 is a member of the HMGB family consisting of three members, HMGB1, HMGB2 and HMGB3.It  Contains 2 HMG box DNA-binding domains entitled box A and box B and It is a highly negative-charged C terminus. As a nuclear protein, HMGB1 stabilizes nucleosomes and allows bending of DNA that facilitates gene transcription which is essential for individual survival. Meanwhile, it is revealed that HMGB1 can also act as a cytokine extracellularlly and regulates monocyte, T cell, dendritic cell activities in inflammatory responses.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e25.8 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e25-30 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSupplied as a 0.2 μm filtered solution of  PBS, 10% Glycerol, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eStore at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped on dry ice\/polar packs.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMultifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability (Ref.71). Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and\/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2\/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogdenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins such as huntingtin (HTT) or TBP.; Nuclear functions are attributed to fully reduced HGMB1. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA, DNA-containing cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and\/or bringing distant regulatory sequences into close proximity. May have an enhancing role in nucleotide excision repair (NER). However, effects in NER using in vitro systems have been reported conflictingly. May be involved in mismatch repair (MMR) and base excision repair (BER) pathways. May be involved in double strand break repair such as non-homologous end joining (NHEJ). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). In vitro can displace histone H1 from highly bent DNA. Can restructure the canonical nucleosome leading to relaxation of structural constraints for transcription factor-binding. Enhances binding of sterol regulatory element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA sequences and increases their transcriptional activities. Facilitates binding of TP53 to DNA. Proposed to be involved in mitochondrial quality control and autophagy in a transcription-dependent fashion implicating HSPB1; however, this function has been questioned. Can modulate the activity of the telomerase complex and may be involved in telomere maintenance.; In the cytoplasm proposed to dissociate the BECN1:BCL2 complex via competitive interaction with BECN1 leading to autophagy activation. Involved in oxidative stress-mediated autophagy. Can protect BECN1 and ATG5 from calpain-mediated cleavage and thus proposed to control their proautophagic and proapoptotic functions and to regulate the extent and severity of inflammation-associated cellular injury. In myeloid cells has a protective role against endotoxemia and bacterial infection by promoting autophagy. Involved in endosomal translocation and activation of TLR9 in response to CpG-DNA in macrophages.; In the extracellular compartment (following either active secretion or passive release) involved in regulation of the inflammatory response. Fully reduced HGMB1 (which subsequently gets oxidized after release) in association with CXCL12 mediates the recruitment of inflammatory cells during the initial phase of tissue injury; the CXCL12:HMGB1 complex triggers CXCR4 homodimerization. Induces the migration of monocyte-derived immature dendritic cells and seems to regulate adhesive and migratory functions of neutrophils implicating AGER\/RAGE and ITGAM. Can bind to various types of DNA and RNA including microbial unmethylated CpG-DNA to enhance the innate immune response to nucleic acids. Proposed to act in promiscuous DNA\/RNA sensing which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. Promotes extracellular DNA-induced AIM2 inflammasome activation implicating AGER\/RAGE. Disulfide HMGB1 binds to transmembrane receptors, such as AGER\/RAGE, TLR2, TLR4 and probably TREM1, thus activating their signal transduction pathways. Mediates the release of cytokines\/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10. Promotes secretion of interferon-gamma by macrophage-stimulated natural killer (NK) cells in concert with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the primary receptor promoting macrophage activation and signaling through TLR4 seems to implicate LY96\/MD-2. In bacterial LPS- or LTA-mediated inflammatory responses binds to the endotoxins and transfers them to CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes. Contributes to tumor proliferation by association with ACER\/RAGE. Can bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex. Binding to class A CpG activates cytokine production in plasmacytoid dendritic cells implicating TLR9, MYD88 and AGER\/RAGE and can activate autoreactive B cells. Via HMGB1-containing chromatin immune complexes may also promote B cell responses to endogenous TLR9 ligands through a B-cell receptor (BCR)-dependent and ACER\/RAGE-independent mechanism. Inhibits phagocytosis of apoptotic cells by macrophages; the function is dependent on poly-ADP-ribosylation and involves binding to phosphatidylserine on the cell surface of apoptotic cells. In adaptive immunity may be involved in enhancing immunity through activation of effector T cells and suppression of regulatory T (TReg) cells. In contrast, without implicating effector or regulatory T-cells, required for tumor infiltration and activation of T-cells expressing the lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant progression. Also reported to limit proliferation of T-cells. Released HMGB1:nucleosome complexes formed during apoptosis can signal through TLR2 to induce cytokine production. Involved in induction of immunological tolerance by apoptotic cells; its pro-inflammatory activities when released by apoptotic cells are neutralized by reactive oxygen species (ROS)-dependent oxidation specifically on Cys-106. During macrophage activation by activated lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes.; (Microbial infection) Critical for entry of human coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus NL63\/HCoV-NL63. Regulates the expression of the pro-viral genes ACE2 and CTSL through chromatin modulation.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNucleus. Chromosome. Cytoplasm. Secreted. Cell membrane; Peripheral membrane protein; Extracellular side. Endosome. Endoplasmic reticulum-Golgi intermediate compartment.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eHMGB family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca href=\"https:\/\/www.genenames.org\/cgi-bin\/gene_symbol_report?hgnc_id=HGNC:4983\" rel=\"nofollow\"\u003e            4983           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca href=\"https:\/\/www.omim.org\/entry\/163905\" rel=\"nofollow\"\u003e            163905           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca href=\"https:\/\/www.genome.jp\/dbget-bin\/www_bget?hsa:3146\" rel=\"nofollow\"\u003e            hsa:3146           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca href=\"https:\/\/string-db.org\/network\/9606.ENSP00000343040\" rel=\"nofollow\"\u003e            9606.ENSP00000343040           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/UniGene\/clust.cgi?ORG=Hs\u0026amp;CID=434102\"\u003e            Hs.434102           \u003c\/a\u003e \u003c\/p\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTissue Specificity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eUbiquitous. Expressed in platelets.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e \u003ch3\u003eGene Functions References\u003c\/h3\u003e\u003col\u003e \u003cli\u003e            Based on these findings, ischemia\/reperfusion-induced MCPIP1 expression regulates the migration and apoptosis of human vascular endothelial cells via HMGB1 and CaSR, respectively.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29379093\" rel=\"nofollow\"\u003e             PMID:                        29379093            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studied association of plasma levels of high mobility group box 1 (HMGB1) in critically ill patients.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29862569\" rel=\"nofollow\"\u003e             PMID:                        29862569            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The high-mobility group box (HMGB) proteins, particularly HMGB1, are self-derived innate immune activators that have multiple functions in the regulation of immunity and inflammation. Recent discoveries have illustrated the close link between HMGB1 and heart allograft rejection.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29198620\" rel=\"nofollow\"\u003e             PMID:                        29198620            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-193a plays a suppressive role in osteogenic differentiation of human bone marrow-derived stroma cell via targeting HMGB1.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29787753\" rel=\"nofollow\"\u003e             PMID:                        29787753            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Platelet HMGB1 mediated neutrophil-extracellular traps release is a primary regulator of deep vein thrombosis in mice.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29391442\" rel=\"nofollow\"\u003e             PMID:                        29391442            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study findings suggested that TCTP promotes colorectal cancer metastasis through regulating the behaviors of HMGB1 and the downstream activation of the NF-kappaB signaling pathway.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30066846\" rel=\"nofollow\"\u003e             PMID:                        30066846            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            in the present study we explore the characteristic binding mode and energetics of Act D binding to 21 nt mimed CpG sequence in the positive regulatory region of hmgb1 gene to identify areas of pressing experimental need..            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28033959\" rel=\"nofollow\"\u003e             PMID:                        28033959            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study demonstrated that serum HMGB1 was upregulated and the expression levels of miR-381 were downregulated in patients with polymyositis (PM). Furthermore, high HMGB1 expression was associated with poor survival rate in patients with PM. A luciferase activity assay was used to confirm the binding of miR-381 and HMGB1 3' untranslated region.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29956737\" rel=\"nofollow\"\u003e             PMID:                        29956737            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High mobility group box 1 (HMGB1) and OV-6 antigen (OV-6) positive staining are promising prognostic parameters for hepatocellular carcinoma (HCC), suggesting that HMGB1 and OV-6 may cooperate with each other and predict poor prognosis of HCC.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29441453\" rel=\"nofollow\"\u003e             PMID:                        29441453            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results demonstrate that non-oxidizable HMGB1 induce a sustained cardiac fibroblasts migration despite the redox state of the environment and by altering CXCL12\/CXCR4 axis. This affects proper cardiac remodeling after an infarction.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28716707\" rel=\"nofollow\"\u003e             PMID:                        28716707            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High HMGB1 expression is associated with reduced chemosensitivity in the pleural effusion of non-small cell lung cancer.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28885675\" rel=\"nofollow\"\u003e             PMID:                        28885675            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This work indicates that NELL-1, HMGB1, and CCN2 might enhance bone defect healing via the recruitment of endogenous cells and induction of vascularization and act via different processes than BMP2.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28463604\" rel=\"nofollow\"\u003e             PMID:                        28463604            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            comparison of inhibitory potential of the already known inhibitors of Head and neck squamous cell carcinoma against HMGB1-binding pocket using simulations and docking.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/27900730\" rel=\"nofollow\"\u003e             PMID:                        27900730            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            identified 2 novel miR-193a-3p targets, the high mobility group box-1 (HMGB1) and the hypoxia upregulated-1 (HYOU1) gene products. HMGB1 silencing in cord blood ECFC-derived cells confirmed its role in regulating vascular function.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28276476\" rel=\"nofollow\"\u003e             PMID:                        28276476            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that HMGB1 is highly expressed in prostate cancer (PC) tissues. Highly expressed HMGB1 activates RAGE\/NF-kappaB signaling pathways, which facilitates the metastasis of prostate cancer.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29845254\" rel=\"nofollow\"\u003e             PMID:                        29845254            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 was identified as a down-stream target of miR-204. The miR-204\/HMGB1 axis mediated ZEB2-AS1's effect on pancreatic cancer.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29753015\" rel=\"nofollow\"\u003e             PMID:                        29753015            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study demonstrated that HMGB1 and TLR4 could contribute to the inflammatory lichen planus process in skin.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29728859\" rel=\"nofollow\"\u003e             PMID:                        29728859            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our research shows that HMGB1 participates in autophagy and DNA damage repair and that downregulation of HMGB1 enhances the sensitivity of multiple myeloma (MM)cells to Dex, suggesting that HMGB1 may serve as a target for MM treatment.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30157958\" rel=\"nofollow\"\u003e             PMID:                        30157958            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 plays a critical role in mitochondrial autophagy in cardiomyocytes. miR-410 targets its 3'UTR and regulates its transcription.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28914970\" rel=\"nofollow\"\u003e             PMID:                        28914970            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 is a good diagnostic biomarker for differentiating refractory M. pneumoniae pneumonia and non-refractory M. pneumoniae pneumonia.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30157804\" rel=\"nofollow\"\u003e             PMID:                        30157804            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 promoted lung cancer invasion and metastasis by upregulating the expression and activity of MMP-2 in an NF-kappaB-dependent manner.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29850505\" rel=\"nofollow\"\u003e             PMID:                        29850505            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            meta-analysis exploring the association of four HMGB1 polymorphisms with cancer.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29730397\" rel=\"nofollow\"\u003e             PMID:                        29730397            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            levels of serum HMGB1 were positively associated with 10-year CHD risk            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29704473\" rel=\"nofollow\"\u003e             PMID:                        29704473            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            high mobility group box 1-receptor for advanced glycation end-products (HMGB1-RAGE) signaling pathway may be involved in the pathogenesis of preterm premature rupture of membranes (pPROM)            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29673663\" rel=\"nofollow\"\u003e             PMID:                        29673663            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MiR-106 interacted with the 3'-UTR of HMGB1 and inhibited HMGB1 expression.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30055307\" rel=\"nofollow\"\u003e             PMID:                        30055307            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            It is a 30 kDa protein that is a lethal mediator in sepsis and is a recognized therapeutic target.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/30135341\" rel=\"nofollow\"\u003e             PMID:                        30135341            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 knockdown and miR-505 overexpression promoted ADM-induced DNA damage in HCC cells.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29803174\" rel=\"nofollow\"\u003e             PMID:                        29803174            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings indicated that HMGB1 likely regulates autophagy in LO2 cells exposed to anoxia-reoxygenation injury            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29880383\" rel=\"nofollow\"\u003e             PMID:                        29880383            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            extracellular functions of HMGB1 in cellular and immune homeostasis at the airway mucosal surface            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28976774\" rel=\"nofollow\"\u003e             PMID:                        28976774            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our results indicate that genetic variations in the HMGB1 gene may serve as an important predictor of breast cancer progression and metastasis.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29725248\" rel=\"nofollow\"\u003e             PMID:                        29725248            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            soluble CD52 exerts a concerted immunosuppressive effect by first sequestering HMGB1 to nullify its proinflammatory Box B, followed by binding to the inhibitory Siglec-10 receptor, triggering recruitment of SHP1 to the intracellular immunoreceptor tyrosine-based inhibitory motif of Siglec-10 and its interaction with the TCR.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29997173\" rel=\"nofollow\"\u003e             PMID:                        29997173            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In lung cancer patients, circulating HMGB1-containing nucleosome is higher in those under chemotherapy, predicting poorly cancer cell differentiation state, enhanced cancer invasion and advanced TNM stages.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29679570\" rel=\"nofollow\"\u003e             PMID:                        29679570            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a number of microRNAs (miRNAs) are identified as a class of regulators for broad control of HMGB1-mediated biological actions in eukaryotic cells.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29651425\" rel=\"nofollow\"\u003e             PMID:                        29651425            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The study indicated polymorphisms in HMGB1 may be a novel biomarker for female lung adenocarcinoma risk.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29617336\" rel=\"nofollow\"\u003e             PMID:                        29617336            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Glycyrrhizin reduced the activity of JAK\/STAT signaling pathway, which is the upstream regulator of HMGB1.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29568761\" rel=\"nofollow\"\u003e             PMID:                        29568761            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 may be a useful prognostic biomarker in malignant pleural mesothelioma when detected by immunohistochemistry, but cannot be considered a diagnostic biomarker in histological samples of mesothelioma            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29356044\" rel=\"nofollow\"\u003e             PMID:                        29356044            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the present study indicates that PBX 3'UTR may induce inflammatory responses and sepsis via acting as a competing endogenous RNA for HMGB1.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29484406\" rel=\"nofollow\"\u003e             PMID:                        29484406            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            overexpression of HMGB1 potentially promoted epileptogenesis. CLinduced activation of glial cells may act via upregulation of HMGB1 and TLR4\/RAGE receptors, and the downstream transcription factor NFkappaB.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29393419\" rel=\"nofollow\"\u003e             PMID:                        29393419            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that HMGB1 is highly expressed in osteosarcoma tissues. Its expression is negatively regulated by miR-505 inhibiting proliferation, migration and invasion in osteosarcoma cells.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29251324\" rel=\"nofollow\"\u003e             PMID:                        29251324            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This review demonstrated the increased expression of HMGB-1 in thrombosis-related diseases, including coronary artery disease, stroke, peripheral arterial disease, disseminated intravascular coagulation, and venous thrombosis.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29940562\" rel=\"nofollow\"\u003e             PMID:                        29940562            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study shows elevated serum level of HMGB1 in patients with the antiphospholipid syndrome            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29410969\" rel=\"nofollow\"\u003e             PMID:                        29410969            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Chronic periodontitis nonsmokers had elevated levels of HMGB1 in gingival crevicular fluid. The levels of HMGB1 were correlated with severity of periodontitis. Chronic periodontitis smokers exhibited lower levels of HMGB1 than chronic periodontitis nonsmokers.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/28209360\" rel=\"nofollow\"\u003e             PMID:                        28209360            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum HMGB1 levels in patients with inflamed appendix were significantly higher than in patients with normal appendix, and this could be a useful biomarker in improving the diagnostic accuracy of appendicitis.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/27922766\" rel=\"nofollow\"\u003e             PMID:                        27922766            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 silencing promoted the susceptibility of retinoblastoma cells to chemotherapeutic drugs through downregulating NF-kappaB.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29328447\" rel=\"nofollow\"\u003e             PMID:                        29328447            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 possesses beneficial actions, such as endothelial activation, enhancement of neurite outgrowth, and neuronal survival in ischemic stroke. [review]            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29054968\" rel=\"nofollow\"\u003e             PMID:                        29054968            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1 mediates fibroblast activity via RAGE-MAPK and NF-kappaB signaling in keloid scar formation.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29283384\" rel=\"nofollow\"\u003e             PMID:                        29283384            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum HMGB1 may be a potential marker to monitor the surgical course in patients undergoing surgery for colorectal cancer.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/27834305\" rel=\"nofollow\"\u003e             PMID:                        27834305            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the promotive effects of HuR overexpression on the inflammatory response were attenuated when HUVECs were cotreated with HMGB1 short hairpin RNA. Therefore, the present results indicated that the ectopic expression of HuR may induce inflammatory responses and thus sepsis by activating the HMGB1 signaling pathway.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29115544\" rel=\"nofollow\"\u003e             PMID:                        29115544            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This is the first report to examine the risk factors associated with HMGB1 SNPs in the development of Rheumatoid arthritis disease in the Chinese Han population.            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29200952\" rel=\"nofollow\"\u003e             PMID:                        29200952            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HMGB1\/IL-1beta complexes released after burn injuries can modulate immune responses            \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/29601597\" rel=\"nofollow\"\u003e             PMID:                        29601597            \u003c\/a\u003e \u003c\/li\u003e \u003c\/ol\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915100192993,"sku":"BL-0424NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLUKAepcHAACmN5s06kM962_f6bc257b-4873-4560-a3ed-9b60137e6a8d.jpg?v=1685853245"},{"product_id":"recombinant-human-wif-1-protein-his-tag-bl-0446np","title":"Recombinant Human WIF-1 Protein (C-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Wnt Inhibitory Factor 1 is produced by our Mammalian expression system and the target gene encoding Gly29-Trp379 is expressed with a 6His tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"AAH18037.1\" target=\"_blank\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/protein\/AAH18037.1\"\u003eAAH18037.1\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eWnt Inhibitory Factor 1; WIF-1; WIF1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eWnt Inhibitory Factor 1 (WIF1) is a secreted protein, which binds WNT proteins and inhibits their activities. WNT proteins are extracellular signaling molecules involved in the control of embryonic development. WIF1 contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. is found to be present in fish, amphibia and mammals. WIF1 is a recurrent target in human salivary gland oncogenesis.WIF1 may be involved in mesoderm segmentation. WIF1 is a tumor suppressor, specifically in nonfunctioning pituitary tumors.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e39.47 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e45 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 10mM HAc-NaAc, 150mM NaCl, 0.5% CHAPS, pH 4.0.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915101405409,"sku":"BL-0446NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLUWASW53AACmA5R0iRI432_5b7c065f-ec65-49ae-af6c-81e252528781.jpg?v=1685853298"},{"product_id":"recombinant-human-reg1a-protein-his-tag-bl-0524np","title":"Recombinant Human REG1A Protein (C-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Regenerating Islet-Derived Protein 1-alpha is produced by our Mammalian expression system and the target gene encoding Gln23-Asn166 is expressed with a 6His tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003ca title=\"P05451\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/P05451\/entry\"\u003eP05451\u003c\/a\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLithostathine-1-Alpha; Islet Cells Regeneration Factor; ICRF; Islet of Langerhans Regenerating Protein; REG; Pancreatic Stone Protein; PSP; Pancreatic Thread Protein; PTP; Regenerating Islet-Derived Protein 1-Alpha; REG-1-Alpha; Regenerating Protein I Alpha; REG1A; PSPS; PSPS1; REG\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRegenerating Islet-Derived Protein 1-α (REG1A) belongs to the Reg family of secreted proteins with a C-type lectic domain. REG1A is highly expressed levels in fetal and infant brains, much lower in adult brains. REG1A promotes the maintenance and growth of pancreatic islet cells and intestinal villi. In addition to, REG1A Might act as an inhibitor of spontaneous calcium carbonate precipitation and be associated with neuronal sprouting in brain, and with brain and pancreas regeneration.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e17.31 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e18 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915104944353,"sku":"BL-0524NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLU6Aa3DUAACrbv_7H8E915_8474123b-66d0-4971-b3fa-aebdcc4e9648.jpg?v=1685853434"},{"product_id":"recombinant-human-spp1-protein-his-tag-bl-0536np","title":"Recombinant Human SPP1 Protein (C-6His)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 class=\"font_9\"\u003e\n\u003cspan\u003eProduct Overview\u003c\/span\u003e\n\u003c\/h3\u003e\n\u003ctable width=\"100%\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eRecombinant Human Secreted Phosphoprotein 1 is produced by our Mammalian expression system and the target gene encoding Ile17-Asn314 is expressed with a 6His tag at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eP10451\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eOsteopontin; Bone Sialoprotein 1; Nephropontin; Secreted Phosphoprotein 1; SPP-1; Urinary Stone Protein; Uropontin; SPP1; BNSP; OPN\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eGene Background\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted Phosphoprotein 1 (SPP1) is a secreted multifunctional glycoprotein. Its putative functions include roles in bone metabolism, immune regulation, wound healing, cell survival, and tumor progression. Based on gene structure and chromosomal location, SPP1 is a member of the small integrin-binding ligand N-linked glycoprotein (SIBLING) family that also includes bone sialoprotein (BSP), dentin matrix protein 1 (DMP1), dentin sialophosphoprotein (DSPP), enamelin (ENAM), and matrix extracellular phosphoglycoprotein (MEPE). SPP1 is expressed in bone, although it is also expressed in other tissues. SPP1 acts as a cytokine that is involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10. It is essential in the pathway that leads to type I immunity. Osteopontin has been implicated as an important factor in bone remodeling. Specifically, research suggests it plays a role in anchoring osteoclasts to the mineral matrix of bones. The fact that SPP1 interacts with multiple cell surface receptors which are ubiquitously expressed makes it an active player in many physiological and pathological processes including wound healing, bone turnover, tumorigenesis, inflammation and ischemia. Therefore, manipulation of plasma Osteopontin levels may be useful in the treatment of autoimmune diseases, cancer metastasis, osteoporosis and some forms of stress.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e34.75 KDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eApmol Mass\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e60-70 KDa, reducing conditions\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLess than 0.1 ng\/µg (1 EU\/µg) as determined by LAL test.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eGreater than 95% as determined by reducing SDS-PAGE. (QC verified)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eBiological Activity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eNot tested\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eAlways centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg\/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eLyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eShipping\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eThe product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e \u003ch3\u003eTarget Details\u003c\/h3\u003e\u003ctable width=\"100%\"\u003e\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eTarget Function\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eMajor non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.; Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eSubcellular Location\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eSecreted.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eProtein Families\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003eOsteopontin family\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\"\u003e\u003cstrong\u003eDatabase References\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\"\u003e\u003cdiv\u003e \u003cp\u003e           HGNC:           \u003ca rel=\"nofollow\"\u003e            11255           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            166490           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:6696           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000378517           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29463954            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Study demonstrated that osteopontin exerts an important role in the monocytes\/macrophage phenotypic differentiation from hypertensive patients with vascular calcification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28091516            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The expression of OPN was high in endometrium in secretory phase and in vitro decidualized endometrial stromal cells. Further analysis confirmed that OPN expression was upregulated by cAMP and C\/EBPbeta signal pathway, while downregulated by miR181b. Increased OPN expression could promote the expression of decidualization-related and angiogenesis-related genes            \u003ca rel=\"nofollow\"\u003e             PMID:                        29420252            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results of the study showed that low urinary OPN levels were correlated with increased kidney stone risk, and dietary habits can affect urinary OPN level            \u003ca rel=\"nofollow\"\u003e             PMID:                        30114399            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The serum levels of cystatin C and urine NGAL, urine OPN can be used as a good marker for assessing the renal effect of obesity which can lead end stage renal disease in pediatric population.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30035656            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            novel 9175th- (exon 7) position polymorphism of OPN and rs17524488 were related to susceptibility to ankylosing spondylitis in a Chinese population            \u003ca rel=\"nofollow\"\u003e             PMID:                        29581970            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Over-expressed and hypo-methylated SPP1 gene is associated with hepatocellular carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27760737            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum osteopontin concentrations were increased in acute pancreatitis (AP) compared with follow-up 3 months after discharge.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29424811            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our data provide evidence that leptin-mediated OPN upregulation promote TH2 inflammation in AR and this process is achieved through the alpha4 integrin and PI3K\/AKT signaling pathways.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29885866            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-129-5p level was decreased in fibrotic liver of human, and reduced by rOPN treatment. In contrast, miR-129-5p was induced in HSCs transfected by OPN siRNA. These data suggested that OPN induces Col 1 expression via suppression of miR-129-5p in hepatic stellate cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29196165            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High circulating osteopontin levels predict major adverse cardiovascular events in patients with severe carotid artery stenosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29317141            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SPP1 Expression is associated with Hepatocellular Carcinomas.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29693976            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum OPN and DKK1 levels of hepatocellular carcinoma patients could be considered as novel biomarkers showing prognostic significance after hepatectomy based on long-term survival data            \u003ca rel=\"nofollow\"\u003e             PMID:                        29753515            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Upregulation of ADIPOR1 and SPP1, among the adipokine gene family, in cancer tissue is associated with poor survival in CRC, suggesting a potential mechanism linking obesity and colorectal cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29761507            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Review\/Meta-analysis: report a significantly higher circulating OPN level in systemic lupus erythematosus patients, a trend of positive correlation between OPN levels and SLE activity, and a significant association between OPN 1239 C\/A and 9250 C\/T polymorphisms, and SLE development.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27307447            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPN is not only the pivotal protein controlling fibrosis, but may also serve as a biomarker associated with prognosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29120858            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our data show that the ability of AML cells to constitutively release high levels of osteopontin is associated with a favorable prognosis, and this is different from previous studies of osteopontin mRNA levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27739925            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            First report of OPN cleavage in THP-1 macrophages after PMA (phorbol 12-myristate 13-acetate) stimulation, and of enhanced cleavage induced by BCG infection (bovine tuberculosis).            \u003ca rel=\"nofollow\"\u003e             PMID:                        29385060            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggest that OPN, MMP9 and S100A8 all play a significant role in bladder cancer progression and are potential prognostic markers and therapeutic targets in bladder cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        29209142            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We demonstrated an important effect of the SPP1 rs4754 on subclinical markers of carotid atherosclerosis in subjects with T2DM; however, as demonstrated by the multiple linear regression analysis, neither rs4754 nor rs28357094 had an important impact on the progression of subclinical markers of carotid atherosclerosis in subjects with T2DM.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28990744            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these results showed that expression of tear OPN protein by perennial allergic conjunctivitis patients increased significantly compared with controls or seasonal allergic conjunctivitis patients out of the pollen season            \u003ca rel=\"nofollow\"\u003e             PMID:                        29279263            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The study revealed an enhanced sensitivity of aortic valve interstitial cells to osteogenic inductors in aortic stenosis patients, which indicates probable implication of OPN, OPG, and BMP2 genes in pathogenesis of aortic valve calcification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29308559            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Carriers of the risky genotype or haplotype also had increased gastric OPN expression (p = 0.038) and inflammation (p = 0.007).  SPP1 polymorphisms predispose to intestinal metaplasia development in H. pylori infected males.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28685609            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Respiratory syncytial virus infection leads to increased OPN expression.IL-1beta is involved in the regulation of OPN levels during respiratory syncytial virus infection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29677209            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            plasma level increases in pregnancy independently of asthma            \u003ca rel=\"nofollow\"\u003e             PMID:                        29200898            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Methylglyoxal-bis-guanylhydrazone may have potential therapeutic utility in reducing or normalizing OPN levels and regulating monocyte activation in diseases that involve chronic inflammation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29538412            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results might be considered a useful starting point to validate OPN as a prognostic and diagnostic marker of hepatocellular carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28711012            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study demonstrates that the OPN gene SNP rs1126616 is statistically associated with cerebral palsy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27114095            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LAMP3 promotes the invasion of osteosarcoma cells via SPP1 signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28849219            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Extended liver surgery is the only potentially curative treatment for patients with cholangiocarcinoma (CCA\/biliary cancer), but it is currently unclear which patients benefit most from surgery. Detecting serum levels of osteopontin - a specific secreted glycoprotein involved in multiple diseases - in CCA patients might help to identify those patients that particularly benefit from tumour resection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28668580            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MALAT1 could directly bind to miR-127-5p to inhibit its expression, so as to rescue OPN expression and promote chondrocyte proliferation through PI3K\/Akt pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28590075            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A linear negative correlation between serum OPN and total bone mineral density (BMD) of Type I diabetes mellitus patients compared to control group was noticed, indicating that the amount of serum OPN could be effective on BMD and a good predicting factor for osteoporosis            \u003ca rel=\"nofollow\"\u003e             PMID:                        28499311            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPN regulates CYP7A1 levels and the metabolic fate of liver acetyl-CoA as a result of CHOL and PC metabolism interplay            \u003ca rel=\"nofollow\"\u003e             PMID:                        28754826            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these findings demonstrated that OPN and VEGF were overproduced in nasal polyps and that OPN induced VEGF production, which indicated that OPN-VEGF axis might contribute to angiogenesis in nasal polyps            \u003ca rel=\"nofollow\"\u003e             PMID:                        28716167            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Osteopontin and CD44 play important roles in the development and progression of meningioma and can be used as prognostic markers for tumor recurrence and progression as well as therapeutic targets for the development of new drugs.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29504367            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPN play a role in pathogenesis of neurodegenerative diseases or in neuroprotection by regulating the activation and function of microglia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28698867            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            osteopontin has a role in DNA repair and impact on human glioblastoma radiosensitivity            \u003ca rel=\"nofollow\"\u003e             PMID:                        27563812            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SPP1 promoted the metastasis of CRC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28531945            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that osteopontin is positively associated with hepatocellular carcinoma (HCC) metastasis, and that OPN can activate CCR1 expression through the PI3K\/AKT\/HIF-1a signaling pathway to promote HCC progression and metastasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29285854            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This review presents the current knowledge on the expression profiles of OPN and its main splice variants in human cancers, as well as the potential implications in patient outcome.  [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        28440483            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Strong correlations between the expression of type I, II, IV collagen and osteopontin and the clinical stage of tympanosclerosis indicate the involvement of these proteins in excessive fibrosis and pathological remodeling of the tympanic membrane.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29068597            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            result of this study confirms that increased levels of OPN exist in CSF and peripheral blood of MS patients and strengthens the evidence regarding the clinical utility of OPN as a promising and validated biomarker for MS            \u003ca rel=\"nofollow\"\u003e             PMID:                        29346446            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPN overexpression was correlated with poor overall survival and clinical features reflecting high aggressiveness in patients with gastric cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27626167            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ITGbeta3 and CD44 expression levels determine whether OPN-a inhibits or enhances growth in lung cancer cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27487131            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study identified that miR-127-5p targets the 3' UTR of osteoarthritis (OA) mRNA to down-regulate the expression of OPN. In OA, the down-expressed miR-127-5p allows the expression of OPN, which mediates the establishment and development of OA.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27126955            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our study shows a strong effect of the rs28357094 G allele in increasing osteopontin expression in the presence of deflazacort, and adds to the evidence that rs28357094 polymorphism may predict response to glucocorticoids in Duchenne muscular dystrophy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28595270            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we described the expression pattern of osteopontin splice variants in papillary thyroid carcinoma samples and the key role of osteopontin-a expression on activating tumor progression features            \u003ca rel=\"nofollow\"\u003e             PMID:                        27409830            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In Osteoarthritis tissues, OPN mRNA, and NEAT1 expression was upregulated, whereas miR-181c expression was downregulated, indicating that targeting NEAT1 to rescue miR-181c expression so as to inhibit OPN expression and synoviocyte proliferation            \u003ca rel=\"nofollow\"\u003e             PMID:                        28379604            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            IL-6 and sIL-6R induced by IL-1beta may trigger IL-6 trans-signaling, contributing to the upregulation of OPN in THP-1 macrophages. Macrophages may be used as a source of IL-6 and sIL-6R and evoke IL-6 trans-signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27863335            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPN is a key mediator of intracerebral tumor growth, invasion, and dissemination in central nervous system lymphoma, and these effects depend upon activation of NF-kappaB.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27050077            \u003c\/a\u003e \u003c\/li\u003e \u003c\/div\u003e\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915101929697,"sku":"BL-0536NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLU-ACswMAACnMuvown8294_ec649725-1263-4b53-b378-eeecb8eb5688.jpg?v=1685853320"}],"url":"https:\/\/www.betalifesci.com\/collections\/cytokines.oembed?page=49","provider":"Beta LifeScience","version":"1.0","type":"link"}