{"title":"Antibody \/ Cell Therapy Targets","description":"\u003cp dir=\"ltr\"\u003e\u003cspan\u003eAntibody cell therapy targets play a crucial role in modern biomedical research and innovative disease treatments. These targets are specific molecules or proteins on cell surfaces that are recognized by antibodies or engineered cells, allowing for precise action against diseased or cancerous cells. By focusing on these targets, therapies can disrupt disease mechanisms, activate the immune response, and support the elimination of harmful cells while sparing healthy tissue.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eThe advancement of targeted antibody and cell therapies has opened new pathways for treating complex conditions, particularly in oncology and immunology. Beta LifeScience offers a carefully curated selection of high-quality \u003c\/span\u003e\u003cspan\u003eantibody cell therapy targets\u003c\/span\u003e\u003cspan\u003e to help researchers and developers achieve greater precision and efficacy in their therapeutic innovations.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eThe Role of Antibody Cell Therapy Targets in Treatment\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eTargeted therapies are designed to identify and bind to specific antigens or receptors that are overexpressed on diseased cells. These interactions can either directly inhibit disease progression or recruit the body's immune system to attack the affected cells.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eIn antibody therapies, monoclonal antibodies are created to recognize these targets with high specificity. In cell therapies, like CAR-T cell treatments, patient-derived T-cells are genetically modified to express receptors that seek out and destroy targeted cells. In both cases, the success of the therapy heavily depends on the selection of accurate and biologically relevant targets.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eApplications of Antibody and Cell Therapy Targets\u003c\/span\u003e\u003c\/h2\u003e\n\u003ch3 dir=\"ltr\"\u003e\u003cspan\u003eCancer Therapy\u003c\/span\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eOne of the most prominent uses of \u003c\/span\u003e\u003cspan\u003eantibody cell therapy targets\u003c\/span\u003e\u003cspan\u003e is in cancer treatment. Tumor cells often express unique or excessive levels of certain proteins, making them ideal targets for antibody or cell-based interventions. By attacking these specific proteins, therapies can effectively reduce tumor growth, limit metastasis, and improve patient survival rates.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eCommon cancer therapy targets include:\u003c\/span\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cspan\u003eImmune checkpoint molecules\u003c\/span\u003e\u003cspan\u003e such as PD-1, PD-L1, and CTLA-4\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cspan\u003eTumor-specific antigens\u003c\/span\u003e\u003cspan\u003e like HER2, EGFR, and CD19\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cspan\u003eTumor microenvironment factors\u003c\/span\u003e\u003cspan\u003e that influence tumor growth and immune evasion\u003c\/span\u003e\n\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch3 dir=\"ltr\"\u003e\u003cspan\u003eAutoimmune Disease Research\u003c\/span\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eIn autoimmune diseases, where the immune system mistakenly attacks healthy tissues, targeted therapies can help modulate the immune response. Identifying key regulatory proteins as therapy targets offers new hope for treating conditions like lupus, multiple sclerosis, and rheumatoid arthritis with greater precision and fewer side effects.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch3 dir=\"ltr\"\u003e\u003cspan\u003eInfectious Disease Treatment\u003c\/span\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eCell therapy targets are also being explored to treat persistent viral infections such as HIV and hepatitis. By designing therapies that seek out and destroy infected cells, researchers aim to clear chronic infections and improve immune system resilience.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eTypes of Antibody Cell Therapy Targets\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eDifferent categories of therapy targets support various treatment strategies, depending on the disease type and therapeutic goal. Some of the major categories include:\u003c\/span\u003e\u003c\/p\u003e\n\u003ch3 dir=\"ltr\"\u003e\u003cspan\u003eImmune Checkpoint Targets\u003c\/span\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eImmune checkpoints are regulatory pathways that control the strength and duration of immune responses. Tumors often exploit these checkpoints to avoid detection. Therapies targeting PD-1, PD-L1, and CTLA-4 have revolutionized cancer treatment, allowing T-cells to stay active and destroy cancer cells more effectively.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch3 dir=\"ltr\"\u003e\u003cspan\u003eTumor-Associated Antigens\u003c\/span\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eTumor-associated antigens are proteins that are more abundant or uniquely expressed in cancer cells compared to normal cells. Targeting molecules like HER2 in breast cancer or CD19 in certain blood cancers enables highly specific therapy with fewer off-target effects.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch3 dir=\"ltr\"\u003e\u003cspan\u003eCancer Stem Cell Markers\u003c\/span\u003e\u003c\/h3\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eSome therapies focus on markers found on cancer stem cells, which are responsible for tumor initiation, growth, and relapse. Targeting markers like CD44 and CD133 could lead to more durable cancer treatments and prevent recurrence.\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eAdvancing Research with Beta LifeScience Targets\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eAt Beta LifeScience, we are committed to supporting cutting-edge research by providing a diverse range of \u003c\/span\u003e\u003cspan\u003eantibody cell therapy targets\u003c\/span\u003e\u003cspan\u003e. Our products undergo rigorous quality control to ensure high biological activity, stability, and consistency across batches.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eResearchers working on antibody therapies, CAR-T therapies, bispecific antibodies, or checkpoint blockade treatments can rely on our validated targets to accelerate their studies and achieve better outcomes.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eChoosing the right target is critical to the success of your therapy development. Beta LifeScience makes it easier by offering reliable solutions tailored for research and clinical innovation\u003ca href=\"https:\/\/www.betalifesci.com\/pages\/betalifesci-product-sitemap-page-1\"\u003e.\u003c\/a\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eWhy Choose Beta LifeScience for Therapy Targets?\u003c\/span\u003e\u003c\/h2\u003e\n\u003cul\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eWide Range of Targets:\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e \u003c\/strong\u003eFrom immune checkpoints to tumor-specific markers, we offer an extensive catalog.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eSuperior Quality:\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e \u003c\/strong\u003eOur targets are produced under strict quality assurance guidelines to maintain high functionality.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eResearch-Driven:\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e \u003c\/strong\u003eWe stay ahead of emerging trends to offer the most relevant and in-demand targets for today's therapies.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003cli dir=\"ltr\" role=\"presentation\"\u003e\n\u003cstrong\u003eDedicated Support:\u003c\/strong\u003e\u003cspan\u003e\u003cstrong\u003e \u003c\/strong\u003eOur team is available to assist with product selection and technical questions to help streamline your research process.\u003c\/span\u003e\n\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch2 dir=\"ltr\"\u003e\u003cspan\u003eExplore and Advance with Confidence\u003c\/span\u003e\u003c\/h2\u003e\n\u003cp dir=\"ltr\"\u003e\u003cspan\u003eBeta LifeScience empowers researchers to transform groundbreaking ideas into real-world therapies. With our premium \u003c\/span\u003e\u003cspan\u003eantibody cell therapy targets\u003c\/span\u003e\u003cspan\u003e, you can drive forward innovation in cancer therapy, autoimmune treatment, and infectious disease solutions.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cb id=\"docs-internal-guid-799b9ad6-7fff-b45b-be21-e2769c638692\"\u003e\u003cspan\u003eExplore our full collection today\u003c\/span\u003e\u003cspan\u003e and discover the right targets to elevate your therapeutic research to new heights.\u003c\/span\u003e\u003c\/b\u003e\u003cbr\u003e\u003c\/p\u003e","products":[{"product_id":"recombinant-mouse-mag-protein-ecd-fc-tag-blpsn-3276","title":"Recombinant Mouse MAG Protein (ECD, Fc Tag)","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 data-mce-fragment=\"1\" class=\"font_9\"\u003e\n\u003cmeta charset=\"utf-8\"\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%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eTag\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eFc\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eHost Species\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eMouse\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eNP_034888.1\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eGma, siglec-4a\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eBackground\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eThe myelin-associated glycoprotein (MAG) contains five immunoglobulin-like domains and belongs to the sialic-acid-binding subgroup of the Ig superfamily. MAG is a transmembrane glycoprotein of 1kDa localized in myelin sheaths of periaxonal Schwann cell and oligodendroglial membranes where it functions in glia-axon interactions. It appears to function both as a receptor for an axonal signal that promotes the differentiation, maintenance and survival of oligodendrocytes and as a ligand for an axonal receptor that is needed for the maintence of myelinated axons. MAG contains a carbohydrate epitope shared with other glycoconjugates that is a target antigen in autoimmune peripheral neuropathy associated with IgM gammopathy and has been implicated in a dying back oligodendrogliopathy in multiple sclerosis. MAG is considered as a transmembrane protein of both CNS and PNS myelin and it strongly inhibits neurite outgrowth in both developing cerebellar and adult dosal root ganglion neurons. In contrast, MAG promotes neurite outgrowth from newborn DRG neurons. Thus, MAG may be responsible for the lack of CNS nerve regeneration and may influce both temporally and spatially regeneration in the PNS.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eA DNA sequence encoding the mouse Mag (NP_034888.1) (Met1-Pro516) was expressed with the Fc region of human IgG1 at the C-terminus.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eSource\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eHEK293\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003ePredicted N Terminal\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eGly 20\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eAA Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eMet1-Pro516\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eThe recombinant mouse Mag consists of 735 a.a. and predicts a molecular mass of 81.6 kDa.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003e\u0026gt;95% as determined by SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003e\u0026lt; 1.0 EU per μg protein as determined by the LAL method.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eBioactivity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003ePlease contact us for detailed information\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eLyophilized from sterile PBS, pH 7.4..\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eStability\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eThe recombinant proteins are stable for up to 1 year from date of receipt at -70°C.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eUsage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eStore the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"Default Title","offer_id":42875227078881,"sku":"BLPSN-3276","price":0.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-rhesus-monkey-tfpi-protein-bla-10386p","title":"Recombinant Rhesus monkey TFPI Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 data-mce-fragment=\"1\" class=\"font_9\"\u003e\n\u003cmeta charset=\"utf-8\"\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%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eHost Species\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eRhesus monkey\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eQ28864\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eAnti convertin EPI Extrinsic pathway inhibitor LACI Lipoprotein associated coagulation inhibitor Lipoprotein-associated coagulation inhibitor TFI TFPI TFPI 1 TFPI1 TFPI1_HUMAN Tissue factor pathway inhibitor Tissue factor pathway inhibitor (lipoprotein associated coagulation inhibitor)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eRecombinant Rhesus monkey TFPI Protein was expressed in HEK293. It is a Protein fragment\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eSource\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eHEK293\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eAA Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eDSEEDEEYTIITDTELPPLKLMHSFCAFKPDDGPCKAIMKRFFFNIFTRQ CEEFIYGGCGGNQNRFESMEECKKVCTRDNVHRIIQTALQQEKPDFCFLE EDPGICRGYITRYFYNNQSKQCERFKYGGCLGNMNNFETLEECKNTCEDG LNGFQVDNYGTQLNAVNNSQTPQSTKVPSFFEFHGPSWCLAPADRGLCRA NENRFYYNSVIGKCRPFKYSGCGGNENNFTSKRECLRACKKGFIQRISKG GLIK\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003e31 kDa including tags\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003ePurity\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003e\u0026gt;95% SDS-PAGE.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003e\u0026lt; 1.0 EU per μg of the protein as determined by the LAL method\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eLyophilised\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eStability\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eThe recombinant protein samples are stable for up to 12 months at -80°C\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eSee related COA\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eUnit Definition\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage Buffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eShipped at 4°C. Store at -20°C or -80°C. Avoid freeze \/ thaw cycle.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"Default Title","offer_id":42876151365857,"sku":"BLA-10386P","price":0.0,"currency_code":"USD","in_stock":true}]},{"product_id":"recombinant-human-collagen-i-col1a1-protein-bla-12935p","title":"Recombinant Human Collagen I \/ COL1A1 Protein","description":"\u003cmeta charset=\"utf-8\"\u003e\n\u003ch3 data-mce-fragment=\"1\" class=\"font_9\"\u003e\n\u003cmeta charset=\"utf-8\"\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%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eHost Species\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eHuman\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eAccession\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eP02452\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eSynonym\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eAlpha 1 type I collagen Alpha 2 type I collagen alpha 2 type I procollagen alpha 2(I) procollagen alpha 2(I)-collagen Alpha-1 type I collagen alpha1(I) procollagen CO1A1_HUMAN COL1A1 COL1A2 collagen alpha 1 chain type I Collagen alpha-1(I) chain collagen alpha-1(I) chain preproprotein Collagen I alpha 1 polypeptide Collagen I alpha 2 polypeptide collagen of skin, tendon and bone, alpha-1 chain collagen of skin, tendon and bone, alpha-2 chain Collagen type I alpha 1 Collagen type I alpha 2 EDSC OI1 OI2 OI3 OI4 pro-alpha-1 collagen type 1 type I proalpha 1 Type I procollagen type I procollagen alpha 1 chain\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eDescription\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eRecombinant Human Collagen I \/ COL1A1 Protein was expressed in Wheat germ. It is a Protein fragment\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eSource\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eWheat germ\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eAA Sequence\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKSGDRGETG PAGPAGPVGPVGARGPAGPQGPRGDKGETGEQGDRGIK\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eMolecular Weight\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003e35 kDa\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eEndotoxin\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003e\u0026lt; 1.0 EU per μg of the protein as determined by the LAL method\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eFormulation\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eLiquid Solution\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eStability\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eThe recombinant protein samples are stable for up to 12 months at -80°C\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eReconstitution\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eSee related COA\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eUnit Definition\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eFor Research Use Only\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd style=\"width: 30%;\" data-mce-style=\"width: 30%;\"\u003e\u003cstrong\u003eStorage Buffer\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"width: 70%;\" data-mce-style=\"width: 70%;\"\u003eShipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze \/ thaw cycle.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e","brand":"Beta LifeScience","offers":[{"title":"Default Title","offer_id":42876219392225,"sku":"BLA-12935P","price":0.0,"currency_code":"USD","in_stock":true}]},{"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-human-mmp-9-mmp9-protein-his-tag-bl-1600np","title":"Recombinant Human MMP-9 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 Matrix Metalloproteinase-9 is produced by our Mammalian expression system and the target gene encoding Ala19-Asp707 is expressed with a 6His tag at the C-terminus.The proenzyme needs to be activated by APMA for an activated form.\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=\"AAH06093.1\" target=\"_blank\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/protein\/AAH06093.1\"\u003eAAH06093.1\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%;\"\u003eMatrix metalloproteinase-9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; MMP9\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%;\"\u003eMatrix metallopeptidase 9 (MMP-9) is an enzyme encoded by the MMP9 gene. This protein, which is produced by normal alveolar macrophages and granulocytes, can be activated by 4-aminophenylmercuric acetate and phorbol ester and up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. MMP-9 is involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, angiogenesis, bone development, wound healing, cell migration, learning and memory, as well as in pathological processes, such as arthritis, intracerebral hemorrhage, and metastasis.\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%;\"\u003e77.4 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%;\"\u003e90 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, 2mM CaCl2, 150mM NaCl, 0.05% Brij35(w\/v), 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 0.1 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":43915019747553,"sku":"BL-1600NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLYqAA4EbAACh3lDvo1w132_1f5350b6-9c49-4e1b-b8e0-e13cce0053f4.jpg?v=1685850686"},{"product_id":"recombinant-human-endoglin-protein-his-trx-tag-bl-1685np","title":"Recombinant Human Endoglin Protein (N-Trx-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 Endoglin is produced by our E.coli expression system and the target gene encoding Glu26-Gln176(Gly40Asp) is expressed with a Trx, 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=\"P17813\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/P17813\/entry\"\u003eP17813\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%;\"\u003eEndoglin; END; CD105; ENG\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%;\"\u003eEndoglin is a single-pass type I membrane protein which restricted to endothelial cells in all tissues except bone marrow. Endoglin as major glycoprotein of vascular endothelium, it has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Homodimer forms a heteromeric complex with the signaling receptors for transforming growth factor-beta: TGFBR1 and\/or TGFBR2. It may have an important role in the binding of endothelial cells to integrins and\/or other RGD receptors. Defects in ENG are the cause of hereditary hemorrhagic telangiectasia type 1 (HHT1), which is an autosomal dominant multisystemic vascular dysplasia, characterized by recurrent epistaxis, muco-cutaneous telangiectases, gastro-intestinal hemorrhage, and pulmonary (PAVM), cerebral (CAVM) and hepatic arteriovenous malformations.\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%;\"\u003e33.6 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%;\"\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%;\"\u003eSupplied as 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%;\"\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":43915039539425,"sku":"BL-1685NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLX-ARqQfAAC0pqRV_n4618_891a432d-4077-4b32-bbc3-57f198f500e8.jpg?v=1685851213"},{"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-cynomolgus-fcrn-protein-his-flag-tag-bl-1836np","title":"Recombinant Cynomolgus FcRn Heterodimer Protein (C-Flag-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 Cynomolgus Beta-2-microglobulin\u0026amp;IgG Receptor FcRn Large Subunit P51 is produced by our Mammalian expression system and the target gene encoding Ile21-Met119\u0026amp;Ala24-Ser297 is expressed with a Flag tag at the C-terminus, 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%;\"\u003eQ8SPW0-1\u0026amp;Q8SPV9-1\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%;\"\u003eIgG receptor FcRn; Neonatal Fc receptor; FCRN\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%;\"\u003eβ-2-Microglobulin (B2M) is a secreted protein with 1 Ig-like C1-type (immunoglobulin-like) domain which belongs to the beta-2-microglobulin family. B2M component of major histocompatibility complex (MHC) class I molecules, involved in the presentation of peptide antigens to the immune system. Polymers of beta 2-microglobulin can be found in tissues from patients on long-term hemodialysis. B2M is a protein found on the surface of many cells and plentiful on the surface of white blood cells. Serum B2M concentration is increased in renal diseases, various malignant diseases and some inflammatory and autoimmune disorders. B2M may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. B2M has been shown as a marker for monitoring inflammatory disease activity and it appears likely to have a destructive role in amyloidosis-related arthritis. B2M might be involved in the OA (osteoarthritis) pathogenesis. Defects in B2M are the cause of hypercatabolic hypoproteinemia. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation. B2M could be a potential therapeutic target in ovarian cancer.\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%;\"\u003e12.6\u0026amp;31.3 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\u0026amp;33 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, 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%;\"\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":43915061395681,"sku":"BL-1836NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLVyAbNsWAADJ3Ca37Vg331_a7ee8b78-a2fa-4f19-b225-677168d90677.jpg?v=1685851926"},{"product_id":"recombinant-mouse-transferrin-r-protein-bl-1839np","title":"Recombinant Mouse TfR Protein (N-8His)","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 Transferrin Receptor Protein 1 is produced by our Mammalian expression system and the target gene encoding Cys89-Phe763 is expressed with a 8His 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%;\"\u003eQ62351\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%;\"\u003eTransferrin receptor protein 1; TR; TfR; TfR1; Trfr; CD71; Tfrc\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%;\"\u003eTransferrin receptor protein 1 (TFRC) belongs to the peptidase M28 family that is synthesized as a 172 amino acid (aa). TFRC regulated by cellular iron levels through binding of the iron regulatory proteins, IRP1 and IRP2, to iron-responsive elements in the 3'-UTR. It binds one transferrin or HFE molecule per subunit and binds the HLA class II histocompatibility antigen, DR1. It Interacts with SH3BP3 and STEAP3, facilitates TFRC endocytosis in erythroid precursor cells. Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. A second ligand, the heditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. It positively regulates T and B cell proliferation through iron uptake.\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%;\"\u003e77 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%;\"\u003e90 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, 5% Trehalose, 5% Mannitol, 0.01% tween80, 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%;\"\u003eCellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Upon stimulation, positively regulates T and B cell proliferation through iron uptake. Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway. When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion. When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2.\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 II membrane protein. Melanosome.\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%;\"\u003ePeptidase M28 family, M28B 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           KEGG:           \u003ca rel=\"nofollow\"\u003e            mmu:22042           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            10090.ENSMUSP00000023486           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28538180            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            role in the development of hypoxia-induced pulmonary vascular remodeling            \u003ca rel=\"nofollow\"\u003e             PMID:                        26419445            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Knock-out of TFR1 in Purkinje cells reduces mGlu1 expression at synapses and impairs motor coordination.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29054881            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            decreasing TfR1 expression during beta-thalassemic erythropoiesis, either directly via induced haploinsufficiency or via exogenous apotransferrin, decreases ineffective erythropoiesis and provides an endogenous mechanism to upregulate hepcidin, leading to sustained iron-restricted erythropoiesis and preventing systemic iron overload in beta-thalassemic mice            \u003ca rel=\"nofollow\"\u003e             PMID:                        28151426            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our study reveals that TFR functions as a novel regulator to control AMPA trafficking efficiency and synaptic plasticity            \u003ca rel=\"nofollow\"\u003e             PMID:                        26880306            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We found that iron assimilation via Tfr1 was critical for skeletal muscle metabolism, and that iron deficiency in muscle led to dramatic changes, not only in muscle, but also in adipose tissue and liver.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26870796            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mice lacking Tfr1 in the heart died in the second week of life and had cardiomegaly, poor cardiac function, failure of mitochondrial respiration, and ineffective mitophagy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26456827            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Transferrin Receptor 1 Facilitates Poliovirus Permeation of Mouse Brain Capillary Endothelial Cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26637351            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Erythrocytic iron deficiency enhances susceptibility to Plasmodium chabaudi infection in mice carrying a missense mutation in tfr1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26303393            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Tfr1 has a role in homeostatic maintenance of the intestinal epithelium, acting through a role that is independent of its iron-uptake function            \u003ca rel=\"nofollow\"\u003e             PMID:                        26324903            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Analysis by qPCR showed changes in mRNA levels of iron-responsive genes, indicating moderately increased iron in the RPE of 10-month HID mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26275132            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            characterization of erythropoiesis, iron status, and hepcidin expression in mice with global or hematopoietic cell-specific haploinsufficiency of transferrin receptor 1 provides initial supporting data for this model            \u003ca rel=\"nofollow\"\u003e             PMID:                        25782630            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            high levels of TfRs such as those found on activated lymphocytes were found to be associated with decreased KLRG1 inhibitory function, indicating that TfRs may sequester KLRG1 from interacting with cadherins.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24752778            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data further demonstrate that the inhibitory activity of KLRG1 is decreased in T cells expressing high levels of TfR, indicating that association of KLRG1 with TfR hinders KLRG1-mediated silencing.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24515870            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            high-affinity anti-TfR alters TfR trafficking, which dramatically impacts the capacity for TfR to mediate blood-brain barrier transcytosis            \u003ca rel=\"nofollow\"\u003e             PMID:                        24470444            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate increased levels of reactive oxygen species (ROS) were detected in bone marrow nucleated cells (BMNC) that express CD71 in in NUP98-HOXD13 (NHD13) transgenic mice, a murine model for myelodysplastic syndromes (MDS).            \u003ca rel=\"nofollow\"\u003e             PMID:                        23958061            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Knockdown of Rab12 increased transferrin receptor level and reduced M98K-induced cell death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23357852            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results suggest that TfR1 would be highly expressed by neurons rather than astroglia to play a negative role in the neurite outgrowth after the incorporation of circulating transferrin in the brain            \u003ca rel=\"nofollow\"\u003e             PMID:                        22019713            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In a model of celiac disease, gluten induces enterocyte CD71 overexpression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22330344            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TfR is constitutively degraded by a Rab12-dependent pathway (presumably from recycling endosomes to lysosomes), which is independent of the conventional degradation pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21718402            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            5-aza-2'-deoxycytidine activates iron uptake and heme biosynthesis by increasing c-Myc nuclear localization and binding to the E-boxes of transferrin receptor 1 (TfR1) and ferrochelatase (Fech) genes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21903580            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Vitamin C increases the expression of the iron-regulated hormone hepcidin and decreases transferrin receptor 1 (TfR1) expression in liver.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21078691            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TfR1 in colon cancer-bearing mice exhibited a 24-hour rhythm in mRNA and protein levels. Experiments suggest that the clock-controlled gene c-MYC rhythmically activated the transcription of the TfR1 gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20631077            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            used phenotypic screening of the T31 mouse\/hamster radiation hybrid panel to map the MMTV cell entry receptor gene and subsequently found that it is transferrin receptor 1            \u003ca rel=\"nofollow\"\u003e             PMID:                        12218182            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            soluble transferrin receptor represents a valuable quantitative assay of marrow erythropoietic activity as well as a marker of tissue iron deficiency            \u003ca rel=\"nofollow\"\u003e             PMID:                        12589962            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            both adult erythropoiesis and lymphopoiesis require TfR; TfR is necessary for the normal maturation of thymocytes, but that B-cell development is less severely affected by the absence of TfR            \u003ca rel=\"nofollow\"\u003e             PMID:                        12881306            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Direct binding of mouse mammary tumor virus to TLR4 up regulated expression of the MMTV entry receptor (CD71) on bone marrow derived dendritic cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        14694089            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            hepcidin transgene expression decreases transferrin receptor 1 mRNA level in placenta            \u003ca rel=\"nofollow\"\u003e             PMID:                        15358563            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Dcytb, DMT1, Ireg1 and transferrin receptor 1 have roles in iron transport and hemolysis            \u003ca rel=\"nofollow\"\u003e             PMID:                        15469906            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TfR1 expression is attenuated in a cell-density-dependent manner in human lung cancer H1299 cells and in murine B6 fibroblasts as the result of a marked decrease in mRNA content.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16092918            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the site of interaction with MMTV maps to two segments physically disparate from the TfR and HFE binding sites            \u003ca rel=\"nofollow\"\u003e             PMID:                        16481319            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HFE and TFR2 interact in cells; this interaction is not abrogated by disease-associated mutations of HFE and TFR2; and that TFR2 competes with TFR1 for binding to HFE            \u003ca rel=\"nofollow\"\u003e             PMID:                        16893896            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data indicate that rapid transferrin recycling is defective after pSec15l1 has mutated.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17087999            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Although expression of high levels of sTfR1 significantly increased serum iron levels, repeated experiments showed that neither hsTfR1 nor msTfR1 gene expression had any effect on iron absorption or hepcidin mRNA expression levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17119325            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mammalian cells utilize transferrin-dependent mechanisms to acquire iron via transferrin receptors 1 and 2 (TfR1 and TfR2) by receptor-mediated endocytosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17121833            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The modified vectors containing Q-dots demonstrated 32-fold greater tumor-targeting efficiency than wild-type HVJ-E.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17961511            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            comparison of the abilities of TfR1 orthologs from different species to support arenavirus entry found that the human and feline receptors were able to enhance entry of the pathogenic strains, but that neither the murine or canine forms were functional.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18003730            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Iron chelation alters expression of Tfrc.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18029550            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Suggest that Hfe induces hepcidin expression when it is not in complex with Tfr1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18316026            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            an interplay of the HIF-1 and NF-kappaB pathways controls TfR1 transcription in inflammation            \u003ca rel=\"nofollow\"\u003e             PMID:                        18519569            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            increased mitochondrial Fe in the myocardium of mutants was due to marked transferrin Fe uptake, which was the result of enhanced transferrin receptor 1 expression            \u003ca rel=\"nofollow\"\u003e             PMID:                        18621680            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Transferrin receptor can be used as a specific target for molecular imaging in CIA mouse, and 99mTc-Tf scintigraphy detects synovial inflammation prior to significant clinical findings in collagen-induced arthritis mouse.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18696076            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mouse mammary tumor virus uses TfR1 for all steps of entry: cell attachment, induction of the conformational changes in Env required for membrane fusion and internalization to an appropriate acidic compartment            \u003ca rel=\"nofollow\"\u003e             PMID:                        18829060            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate that TfR promotes glioma progression by two mechanisms, an increase in proliferation rate and glutamate production, the latter mechanism providing space for the progressing tumor mass.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19066835            \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":43915049271521,"sku":"BL-1839NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLWGAHT1iAACj5ltiFJo577_c0792038-55ef-4d10-bf57-7e76b4cc0798.jpg?v=1685851550"},{"product_id":"recombinant-human-snca-protein-bl-1871np","title":"Recombinant Human SNCA 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 Alpha-Synuclein is produced by our E.coli expression system and the target gene encoding Met1-Ala140 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%;\"\u003eP37840\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%;\"\u003eAlpha-Synuclein; Non-A Beta Component of AD Amyloid; Non-A4 Component of Amyloid Precursor; NACP; SNCA; NACP; PARK1\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%;\"\u003eAlpha-Synuclein (SNCA) is a member of the Synuclein family. SNCA is expressed principally in brain but also expressed in low concentrations in all tissues except liver. SNCA interacts with UCHL1, Phospholipase D and histones. SNCA can include beta- and gamma-synuclein. In addition, SNCA is an important regulatory component of vesicular transport in neuronal cells. It has been suggested that SNCA is related to the pathogenesis of Parkinson's Disease and neurodegenerative disorders. Defects in SNCA will lead to Dementia Lewy Body (DLB).\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%;\"\u003e14.46 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 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%;\"\u003eNeuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores. Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis. Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha\/DNAJC5. This chaperone activity is important to sustain normal SNARE-complex assembly during aging. Plays also a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its 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%;\"\u003eCytoplasm. Membrane. Nucleus. Cell junction, synapse. 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%;\"\u003eSynuclein 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            11138           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            127750           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:6622           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000338345           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        21309955            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            The molecular basis and clinical relevance of statistically decreased alphaSyn pathology in schizophrenic brain versus aged controls is unknown and needs further elucidation as will be necessary for its incidence and relevance in chronic affective disorders.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19198857            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Elevated levels of insoluble alpha-Syn seen in brains of patients with Parkinson's and dementia are higher than that of Parkinson brains, for insoluble and insoluble\/soluble alpha-Syn, respectively, with a highly significant difference between the two groups.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20599975            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that the key molecular scaffold most effective in inhibiting and destabilizing self-assembly by alphaS requires: (i) aromatic elements for binding to the alphaS monomer\/oligomer and (ii) vicinal hydroxyl groups present on a single phenyl ring.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21443877            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            [review] The role of alpha-syn is summarized in synaptic vesicle recycling, neurotransmitter synthesis and release and synaptic plasticity, as well as the possible relevance between the loss of normal alpha-syn functions in disease conditions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21167933            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Age-related accumulation of neuromelanin might induce alpha-synuclein over-expression and thereby make dopamine neurons more vulnerable to injuries.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21461961            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            alpha-Synuclein function in promoting cell proliferation is associated with its microtubule assembly activity with the functional domain localized in its carboxyl-terminal part.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21331461            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Association ofalpha-synuclein with Rab attachment receptor protein and soluble sensitive factor attachment receptors (SNAREs) highlights a key role for membrane transport defects in alpha-synuclein-mediated pathology.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21439320            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our result strongly indicates that Parkinson's disease, induced by alpha-SYN mutation, is evoked by deregulation of the AKT-signaling cascade.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21474915            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genetic mutations in the alpha-synuclein gene can lead to Parkinson's disease, but even in these patients, age-dependent physiological changes or environmental exposures appear to be involved in disease presentation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21238487            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our results imply that CSF alpha-synuclein is currently unsuitable as biomarker to differentiate between PD and AP.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21236518            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            [review] Presynaptic function is implicated in the function\/dysfunction of alpha-synuclein, the first gene shown to contribute to Parkinson's disease (PD), in this review of genetic models of PD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20969957            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In the Caucasian patient-control series examined, risk for Parkinson disease is influenced by variation in SNCA and tau proteins but not glycogen synthase kinase (GSK)beta3.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21159074            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Overexpression of alpha-Syn transgene alters dopamine efflux and dopamine D2 receptor modulation of corticostriatal glutamate release at a young age in mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21488084            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            An artificial microRNA-embedded human SNCA silencing vector is expressed lacks toxicity in rat PC12 cells in which rat SNCA is not silenced and has reduced toxicity in human SH-SY5Y cells in which hSNCA is silenced.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21338582            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Patients with multiple system atrophy may have a cerebrospinal fluid environment particularly favorable for alpha-synuclein fibril formation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21215793            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Iron up-regulates alpha-synuclein and induces aggregation through the predicted iron responsive element (IRE) in the 5'-untranslated region (UTR) of human alpha-synuclein mRNA.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20383623            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            an association of the two SNPs in 4q22\/SNCA with the age of onset of Parkinson's disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        21044948            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings suggest that alpha-synuclein pathology is associated with Tar DNA-binding protein-43 accumulation in Lewy body disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20669025            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Attenuation of nigral SNCA pathology and dopaminergic neurodegeneration by inhibition of NADPH oxidase and iNOS supports a causative relation between inflammation-mediated SNCA pathologic alterations and chronic dopaminergic neurodegeneration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21245015            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data describe spontaneous accumulation of hyperphosphorylated tau in striata of a mouse model of Parkinsonism, which overexpresses human a-Synuclein under the PDGF promoter.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21453448            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Direct replication of single nucleotide polymorphisms (SNPs) within SNCA and BST1 confirmed these two genes to be associated with the Parkinson's Disease in the Netherlands.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21248740            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Transgenic alpha-synuclein localizes to the mitochondrial membranes under conditions of proteasomal inhibitory stress; this localization coincides with selective age-related mitochondrial complex I inhibition.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20887775            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Synphilin-1 inhibits alpha-synuclein degradation by the proteasome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21103907            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            From crystal structures of fusions between maltose-binding protein and four segments of alpha-synuclein, the study traces a virtual model of the first 72 residues of alpha -synuclein.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21462277            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In transgenic mice, the norepinephrine systems may be more vulnerable than dopamine systems to toxic effects of aberrant alpha-synuclein; this is in line with the major damage to the noradrenaline system that occurs in patients with Parkinson's disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19152986            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In patients diagnosed with dementia with Lewy bodies, lower cerebrospinal fluid alpha-synuclein levels may perhaps be associated with lower cognitive performance, in comparison to patients who are diagnosed with Alzheimer's disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20847452            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A novel function for BAG5 as a modulator of CHIP E3 ubiquitin ligase activity with implications for CHIP-mediated regulation of alpha-syn oligomerization.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21358815            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Single-nucleotide polymorphisms in SNCA (rs356219; P = 5.5 x 10(-4) ) is significantly associated with Parkinson's disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        21425343            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            alpha-Synuclein thus exerts a primary and direct effect on the morphology of an organelle long implicated in the pathogenesis of Parkinson disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21489994            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            evidence that alpha-synuclein is a cellular ferrireductase, responsible for reducing iron (III) to bio available iron (II)            \u003ca rel=\"nofollow\"\u003e             PMID:                        21249223            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study found a significant association between the NACP-Rep1 length polymorphism and Beck Depression Inventory (BDI) score; analysis revealed no further association between the In4 polymorphism or between the mRNA expression of SNCA and the BDI score            \u003ca rel=\"nofollow\"\u003e             PMID:                        21271299            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            mechanistic insights on the role alpha-synuclein in modulating neurodegenerative phenotypes by regulation of Akt-mediated cell survival signaling in vivo            \u003ca rel=\"nofollow\"\u003e             PMID:                        21304957            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            overexpression of alpha-syn may cause mitochondrial defects in dopaminergic neurons of the substantia nigra through an association with adenylate translocator and activation of mitochondria-dependent cell death pathways            \u003ca rel=\"nofollow\"\u003e             PMID:                        21310263            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data demonstrate an elevated state of tauopathy in striata of the A53T alpha-Syn mutant mice, suggesting that tauopathy is a common feature of synucleinopathies            \u003ca rel=\"nofollow\"\u003e             PMID:                        21445308            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            REVIEW: alpha-Synuclein in Parkinson disease and other neurodegenerative disorders            \u003ca rel=\"nofollow\"\u003e             PMID:                        21342025            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that membrane lipid modification in oligodendroglial cells containing SUMO-1 promotes the formation of alpha-synuclein inclusion bodies resembling protein aggregates in neurodegenerative disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20725866            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that low SMN levels are associated with significantly lower alpha-synuclein expression, and that alpha-synuclein may be a genetic modifier or biomarker of spinal muscular atrophy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20640532            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SNCA locus duplication carriers: from genetics to Parkinson disease phenotypes            \u003ca rel=\"nofollow\"\u003e             PMID:                        21412942            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ubiquitin ligase parkin promotes Mdm2-arrestin interaction but inhibits arrestin ubiquitination            \u003ca rel=\"nofollow\"\u003e             PMID:                        21466165            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            analysis of the mechanism of membrane permeabilization by oligomeric alpha-synuclein            \u003ca rel=\"nofollow\"\u003e             PMID:                        21179192            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the relation between membrane physical properties and AS binding affinity and dynamics that presumably define protein localization in vivo and, thereby, the role of AS in the physiopathology of Parkinson disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21330368            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MMP3 digestion of alpha-synuclein in DA neurons plays a pivotal role in the progression of Parkinson disease through modulation of alpha-synuclein in aggregation, Lewy body formation, and neurotoxicity            \u003ca rel=\"nofollow\"\u003e             PMID:                        21330369            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Coordination features and affinity of the Cu(2)+ site in the alpha-synuclein protein of Parkinson's disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        21319811            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study confirms the association between PD and both SNCA SNPs and the H1 MAPT haplotype.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21391235            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this work Cu(ii) coordination to peptide fragments encompassing residues 45-55 of synuclein alpha has been exhaustively characterized, including systems containing the inherited mutations E46K and A53T, as model peptides of the His-50 site.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21212878            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results support the hypothesis that WT and A53T alpha-synuclein has an important role in the initiation and maintenance of inflammation in Parkinson's disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        21255620            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The combined data indicate that the A30P mutation does not cause changes in the number, location and overall arrangement of beta-strands in amyloid fibrils of alpha-synuclein.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21280130            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that mutations in alpha-synuclein may impair specific functional domains, leaving others intact.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21272100            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Single locus analysis showed that G\/G SNCA and H1\/H1 MAPT risk genotypes were over-represented in patients with Parkinson disease compared with controls            \u003ca rel=\"nofollow\"\u003e             PMID:                        21054681            \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":43915018830049,"sku":"BL-1871NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLXqAJyYkAADDfBju9Iw000_229e380b-e42e-40fb-86ef-e4c537df8bdc.jpg?v=1685850660"},{"product_id":"recombinant-human-tslp-protein-bl-1908np","title":"Recombinant Human TSLP 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 Thymic Stromal Lymphopoietin is produced by our E.coli expression system and the target gene encoding Tyr29-Gln159 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%;\"\u003eQ969D9\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%;\"\u003eThymic stromal lymphopoietin; TSLP\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%;\"\u003eThymic stromal lymphopoietin (TSLP) is a novel member of the hemopoietic cytokine family that promotes the development of B cells and shares overlapping activity with IL-7. The human TSLP protein comprises a 28 amino acids (aa) signal sequence and 131 aa mature region. Human TSLP has two isoforms lfTSLP and sfTSLP produced by alternative splicing . lfTSLP is expressed in a number of tissues including heart, liver and prostate, and sfTSLP (63aa) is predominantly expressed in keratinocytes of oral mucosa, skin and in salivary glands. In aa sequence level, Human TSLP displays about 43% identity with mouse TSLP.TSLP is a cytokine that functions mainly on myeloid cells; it induces the release of T cell-attracting chemokines from monocytes and enhances the maturation of CD11c(+) dendritic cells.TSLP has proliferative effects on the myeloid cell line and may initiate asthma or atopic dermatitis responses by directly activating mast cells . TSLP signals cells via the interleukin-7 receptor-α chain (IL-7Rα),shared with IL-7, together with the TSLP receptor (TSLPR) subunit. Recent studies indicate that TSLP and its receptor are novel therapeutic targets for rheumatoid arthritis,for increased intraarticular TSLP concentrations in patients has caused chemotaxis and activation of arthritogenic T cells.\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%;\"\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 0.1 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%;\"\u003eCytokine that induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c(+) dendritic cells. Can induce allergic inflammation by directly activating mast cells.; May act as an antimicrobial peptide in the oral cavity and on the skin.\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            30743           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            607003           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:85480           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000339804           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28368013            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Effects of Linalyl Acetate on Thymic Stromal Lymphopoietin Production in Mast Cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30011850            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            presence of epithelium-derived TSLP in the eustachian tubes plays important role in the onset of eosinophilic otitis media            \u003ca rel=\"nofollow\"\u003e             PMID:                        29272985            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a new mechanism of T cell stimulation in human skin was identified, demonstrating the direct induction of T cell migration by TSLP in the absence of DCs.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28377574            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the secretion of TSLP by keratinocytes is induced by the HIV-1 viral synapse in a miR-375 controlled manner            \u003ca rel=\"nofollow\"\u003e             PMID:                        28443609            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            production increased at skin sites of ovalbumin sensitization            \u003ca rel=\"nofollow\"\u003e             PMID:                        27992078            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Sera of patients with infantile eosinophilic gastroenteritis showed a specific increase in both thymic stromal lymphopoietin and IL-33 levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26948075            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            short and long thymic stromal lymphopoietin isoforms have roles in house dust mite-induced asthmatic airway epithelial barrier disruption            \u003ca rel=\"nofollow\"\u003e             PMID:                        27996052            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            DeltaNp73 was abundantly expressed in the atopic dermatitis epidermis and increased the release of TSLP via NF-kappaB activation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28655470            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study shows that long form of thymic stromal lymphopoietin of keratinocytes is induced by protein allergens            \u003ca rel=\"nofollow\"\u003e             PMID:                        28720058            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we found that activation of the protease-activated receptor 1 (PAR1) induced secretion of TSLP by the corneal stromal cells... we proposed that TSLP might function as the link between increased protease activity and inflammatory responses or itch sensation in the corneas            \u003ca rel=\"nofollow\"\u003e             PMID:                        28631887            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TSLP-HOTAIR axis also plays a protective role in low-density lipoprotein (ox-LDL)-induced Endothelial cells' injury.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28615347            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The aim of this study was to determine the influence of human rhinovirus on the genes involved in airway remodeling and to examine the impact of TSLP and contribution of oxidative stress on airway remodeling in the context of HRV infection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28545810            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TSLP-induced phosphorylation of l-plastin is increased in atopic dermatitis and increases eosinophil migration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27304220            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a hit expansion exercise yielded additional active compounds that could be amenable to further optimization, providing an opportunity to dissociate TSLP inhibition from other non-desired activities. This study illustrates the potential of phenotypic drug discovery to complement target based approaches by providing new chemistry and biology leads            \u003ca rel=\"nofollow\"\u003e             PMID:                        29320511            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study found that among patients with atopic dermatitis (AD), common FLG null mutations are associated with earlier AD onset in a dose-dependent manner, whereas TSLP rs1898671 appears unrelated to the timing of AD onset            \u003ca rel=\"nofollow\"\u003e             PMID:                        28479194            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            lactobacilli from the omnivorous group and all bifidobacteria significantly down-regulated IL-8. Notably, both genera also lowered the TSLP expression in stimulated Caco-2 cells, regardless of the diet regimen.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27863334            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this review focuses on recent advances on the effects of TSLP on obstetrical and gynecological diseases, including pregnancy failure, endometriosis, and cervical cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        27976427            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The increase in TSLP and TNF-alpha level observed in IS fluid was found to correlate with disease severity. The increased TSLP production from asthma sputum cells was abrogated by the addition of rIL-37. Regulation of TSLP pathway may be a therapeutic approach for asthma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27528425            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            House dust mite sublingual immunotherapy downregulated Th2-type immune responses mediated by the TSLP-OX40L signaling pathway in patients with persistent moderate to severe allergic rhinitis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27012942            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggest that IL-1beta may be an early key mediator for the acquisition of an Atopic dermatitis (AD) phenotype through induction of thymic stromal lymphopoietin (TSLP) and alteration of the epidermal homeostasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28191908            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            House dust mite exposure increases the expression of TSLP through PI3K\/Akt signaling pathway in human bronchial epithelial 16HBE cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28400057            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Posttranslational modifications control the functional activity of TSLP in humans and overproduction of TSLP may be a key trigger for the amplification of type 2 inflammation in diseases            \u003ca rel=\"nofollow\"\u003e             PMID:                        27744031            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study provides evidence for the hypothesis that TSLP could reflect the histological severity of lumbar disc degeneration (LDD), and TSLP-siRNA and TSLPR-siRNA could inhibit apoptosis of nucleus pulposus cells. The evident information obtained from the investigation could lead the way for new therapeutic approaches regarding LDD treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28746197            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            periostin-mediated TSLP production by keratinocytes directly stimulates cutaneous T-cell lymphoma (CTCL) tumor cell growth in addition to inducing a Th2-dominant tumor environment in CTCL.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27634769            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study shows that TSLP may be involved in the pathogenesis of asthma and rhinitis; dust mite and mugwort allergy could increase it significantly            \u003ca rel=\"nofollow\"\u003e             PMID:                        28303765            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum TSLP levels were significantly increased in systemic sclerosis patients compared to healthy donors, and were associated with a higher frequency of vasculopathy. The proportion of TSLP-positive dermal cells was increased in the skin of SSc patients compared with healthy donors, and was correlated with fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27429171            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study shows that NOD2 is an asthma-related factor that can promote cell proliferation and inflammatory response by mediated expression of TSLP in human airway smooth muscle cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27889082            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the effects of TSLP on myeloid cells are crucial in reducing the multiple organ failure that is associated with systemic inflammation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26934097            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            interactions between TSLP in follicular dendritic cells and IgA production in tonsils may be an important mechanism contributing to the pathogenesis of Immunoglobulin A (IgA) nephropathy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27187742            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study demonstrated that naturally occurring severe infections by the most common respiratory viruses in hospitalized infants induce nasal airway secretion of TSLP, IL-33, and periostin when compared with healthy controls            \u003ca rel=\"nofollow\"\u003e             PMID:                        28471975            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Variations in FLG and TSLP genotype were associated with differences in self-reported skin clearance, TCI usage, and steroid usage.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27902816            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A possible role of TSLP in immune homeostasis in HIV infection:higher plasma TSLP was found in individuals with primary HIV infection compared to both chronic HIV infection and healthy controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27769179            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The polymorphism was further reproducibly associated with a DNA methylation signature in whole blood (P = 4.5x10-40) that also associated with allergic sensitization and expression in blood of the cytokine TSLP (P = 1.1x10-4). Knockdown of the transcription factor predicted to bind the enhancer region (NHLH1) in a human cell line (HEK293) expressing NHLH1 resulted in lower TSLP expression            \u003ca rel=\"nofollow\"\u003e             PMID:                        27149122            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TSLP level was significantly higher in asthmatic than in nonasthmatic children. TSLP level was significantly different between allergic asthmatic and nonallergic nonasthmatic groups.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26999524            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            While serum TSLP levels were unaffected by concomitant allergies and atopic comorbidities, serum levels of IL-31, IL-33 and sST2 were affected to a small extent. We found a positive correlation between TSLP, IL-31 and IL-33, and an inverse relationship between IL-33 and sST2            \u003ca rel=\"nofollow\"\u003e             PMID:                        27152943            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results showed that TSLP promoted the production of alpha-SMA and collagen I (P\u0026lt;0.001), suggesting that it can accelerate MRC-5 cell fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27385084            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TSLP is a key mediator in the pathogenesis of inflammatory bowel diseases and that further studies are needed to evaluate its role. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27697608            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Letter: report decreased salivary gland TSLP expression in primary Sjogren's syndrome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27494755            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A novel mouse xenograft model to study the role of TSLP-induced CRLF2 signals in normal and malignant human B lymphopoiesis has been developed.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26611474            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Heat stress-induced HSPs can significantly reduce the production and secretion of TSLP from keratinocytes cultured under Th2 environment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26419317            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TSLP expression in the skin is mediated via RARgamma-RXR pathways.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26531761            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Epidermal thymic stromal lymphopoietin predicts the development of atopic dermatitis during infancy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26879860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study shows that specific food antigens can trigger innate immune mediated esophageal TSLP secretion            \u003ca rel=\"nofollow\"\u003e             PMID:                        26992000            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            production by monocyte-derived dendritic cells requires the integration of signals from dectin-1, the IL-1 receptor, and endoplasmic reticulum stress response stress signaling pathways            \u003ca rel=\"nofollow\"\u003e             PMID:                        26573878            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The association of TSLP polymorphism rs2289278 with atopic dermatitis (AD) was stronger in children with allergic sensitization than in children without atopy, and TSLP polymorphisms also increased the risk of asthma in children with AD            \u003ca rel=\"nofollow\"\u003e             PMID:                        26712523            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The positive feedback loop between TSLP, IL-33 and their receptors, and Th2 cytokines may facilitate Th2-skewed inflammation in eosinophilic CRSwNP.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26095319            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results show that rs1837253 polymorphism may be directly involved in the regulation of TSLP secretion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25515628            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Upon TSLP stimulation, the cells with the highest TSLPR expression level showed enhanced proliferation and JAK\/STAT-mediated gene regulation in a dose-dependent manner            \u003ca rel=\"nofollow\"\u003e             PMID:                        26652578            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Thymic stromal lymphopoietin activation of basophils in patients with allergic asthma is IL-3 dependent            \u003ca rel=\"nofollow\"\u003e             PMID:                        25962901            \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":43915015979233,"sku":"BL-1908NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/rB9Eh2P43GWAU0DmAACfFYmhC38783_a6a87df9-9edf-4127-b1a1-66423241f8ed.jpg?v=1685850589"},{"product_id":"recombinant-mouse-snca-protein-bl-1921np","title":"Recombinant Mouse SNCA 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 Alpha-Synuclein is produced by our E.coli expression system and the target gene encoding Met1-Ala140 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%;\"\u003eO55042\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%;\"\u003eAlpha-synuclein; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP; Snca\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%;\"\u003eAlpha-Synuclein (SNCA) is a member of the Synuclein family. SNCA is expressed principally in brain but also expressed in low concentrations in all tissues except liver. SNCA interacts with UCHL1, Phospholipase D and histones. SNCA can include beta- and gamma-synuclein. In addition, SNCA is an important regulatory component of vesicular transport in neuronal cells. It has been suggested that SNCA is related to the pathogenesis of Parkinson's Disease and neurodegenerative disorders. Defects in SNCA will lead to Dementia Lewy Body (DLB).\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%;\"\u003e14.5 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%;\"\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 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%;\"\u003eNeuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores. Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis. Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha\/DNAJC5. This chaperone activity is important to sustain normal SNARE-complex assembly during aging. Plays also a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its 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%;\"\u003eCytoplasm. Membrane. Nucleus. Cell junction, synapse. 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%;\"\u003eSynuclein 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:20617           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            10090.ENSMUSP00000109907           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29367610            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            oligodendrocytes but not neurons transform misfolded alpha-Syn into a glial cytoplasmic inclusions-like strain, highlighting the fact that distinct alpha-Syn strains are generated by different intracellular milieus            \u003ca rel=\"nofollow\"\u003e             PMID:                        29743672            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Cardiolipin exposure on the outer mitochondrial membrane modulates alpha-synuclein in Parkinson's disease and cultured cardiomyocyte models.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29483518            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A53T SNCA missense mutation caused impaired light entrainment of the circadian system in mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29865270            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Induction of the Immunoproteasome Subunit Lmp7 Links Proteostasis and Immunity in alpha-Synuclein Aggregation Disorders            \u003ca rel=\"nofollow\"\u003e             PMID:                        29759483            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this study, we assessed the spread of pathology following a localized induction of alphaS inclusions in the lumbar spinal cord following a unilateral injection in the sciatic nerve. Using this paradigm, we demonstrated the ability for alphaS inclusion spread and\/or induction along neuroanatomical tracts within the CNS of two alphaS-overexpressing mouse models.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29976670            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results indicated that integrin CD11b mediates alpha-synuclein-induced NOX2 activation through a RhoA-dependent pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29154191            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SNCA expression is associated with Parkinson's disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28923922            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Snca regulates bone network homeostasis and ovariectomy-induced bone loss            \u003ca rel=\"nofollow\"\u003e             PMID:                        27378017            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings provide evidence for a novel mechanism underlying the protective effects of PINK1 against alpha-syn-induced neurodegeneration and highlight a novel therapeutic target for Parkinson's disease treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28933786            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study demonstrates that PLK-2 activity can rapidly change cellular alpha-synuclein levels in cell models and in mice brains, but this process does not require phosphorylation of S129. Instead, it operates via regulation of alpha-synuclein mRNA transcription in an open reading frame-dependent manner            \u003ca rel=\"nofollow\"\u003e             PMID:                        28648742            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the presented data link the Parkinson's disease-associated gene alpha-synuclein to the neuronal cell fate determinant TRIM32.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27339877            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            alpha-synuclein levels can be reduced in neurons without impairing (or improving) mitochondrial bioenergetics or distribution            \u003ca rel=\"nofollow\"\u003e             PMID:                        28462393            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study shows that the age-dependent alpha-syn accumulation is correlated with an elevation of TRPC3 in the mitochondrial fractions isolated from monkey and mouse brains. In animal and cell models, alpha-syn overexpression was accompanied by an elevation of alpha-syn and TRPC3 in the mitochondrial fractions, and alpha-syn downregulation was associated with a reduction of the mitochondrial alpha-syn and TRPC3.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27904950            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            plasma concentrations of alpha-synuclein were significantly higher in exercising mice compared to control mice. Our results suggest that exercise may slow the progression of Parkinson's disease by preventing abnormal protein aggregation in brain            \u003ca rel=\"nofollow\"\u003e             PMID:                        29272304            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            revealed a prominent modulating effect of alpha-synuclein on the developing DA neurons in substantia nigra (SN) which is the most affected region in PD patients. Yet, alpha-synuclein had no effect on the formation of DA neurons in ventral tegmental area which is much less susceptible to degeneration in PD patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29243900            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These new mouse lines are invaluable for fast identification of cells with inactivation of Snca by Cre-recombination and represent useful tools for in vivo studies of alpha-synuclein function and dysfunction.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27838898            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Retinal iron dyshomeostasis due to impaired or altered function of alpha-syn contributes to the visual symptoms associated with Parkinson disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27343690            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results obtained with immuno-spin trapping and immunoprecipitation experiments confirmed formation of alpha-synuclein radicals in dopaminergic neurons of maneb and paraquat exposed mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25952542            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study showed that intracerebral injection of synthetic alpha-synuclein fibrils into adult wild-type marmoset brains (caudate nucleus and\/or putamen) resulted in spreading of abundant alpha-synuclein pathologies, which were positive for various antibodies to alpha-synuclein, including phospho Ser129-specific antibody, anti-ubiquitin and anti-p62 antibodies, at three months after injection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28148299            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Trehalose was also able to restore cell viability to control levels, but pre-formed fibrils (PFFs)still exhibited toxic effects on the cells. These data provide essential information regarding effects of trehalose on alphaSyn accumulation and neuronal survival on exposure to PFF            \u003ca rel=\"nofollow\"\u003e             PMID:                        28068606            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results suggest that synucleins are important orchestrators of presynaptic terminal topography.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28052246            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            C57BL\/6J-OlaHsd mice, a substrain of C57BL\/6J carrying mutated alpha-synuclein and multimerin-1 genes, have an altered bone phenotype.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28266709            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings of this study indicated a functional role of alpha-synuclein in early experimental autoimmune encephalomyelitis by increasing Th1 cell-mediated immune response.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27565429            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            synuclein is required for efficient maintenance of animal's balance and coordination in old age.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27614017            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data show that neurodegenerative processes associated with lysosomal dysfunction may be presynaptically initiated by a concomitant reduction in alpha-synuclein and CSPalpha levels at nerve terminals.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27881461            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            synuclein exerts dose-dependent effects on dilation of the exocytotic fusion pore.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28288128            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that endocytosis is the principal mechanism by which proteopathic alpha-synuclein aggregates are internalized in primary hippocampal neurons in culture; aggregates are rapidly trafficked along endosomal\/lysosomal pathway, where most of the material remains for days as proposed in neurodegenerative synucleinopathies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28611062            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            LRRK2 negatively regulates the clearance of alphaSYN accompanied by down-regulation of the endocytosis pathway; LRRK2 in microglia may function as the offending molecule responsible for neurodegeneration, in terms of down-regulation of alphaSYN clearance.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27903237            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            sideroflexin 3 (SFXN3) was found to be a mitochondrial protein localized to the inner mitochondrial membrane.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28049716            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The ability of monomeric alpha-synuclein to enhance ATP synthase efficiency under physiological conditions may be of importance when alpha-synuclein undergoes the misfolding and aggregation            \u003ca rel=\"nofollow\"\u003e             PMID:                        27733604            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Rab7 accumulated in GCase deficient cells, supporting the notion that lysosomal recycling is impaired.  Since recombinant GCase can reverse ALR impairment, we anticipate that strategies to restore GCase activity in the brains of both sporadic patients with PD and those with GBA1 mutations will improve autophagy lysosomal pathway, preventing the accumulation of a-synuclein and spread of pathology.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27378698            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study showed that apoptosis is an important form of cellular degeneration in lipopolysaccharide (LPS-sensitized hypoxic-ischemic (HI) injury in the immature brain. Loss of PINK1 can protect the immature brain against cell apoptosis induced by LPS-sensitized HI injury. Moreover, alpha-Syn plays a neuroprotective role in LPS-sensitized HI brain damage in PINK1-knockout neonatal mice            \u003ca rel=\"nofollow\"\u003e             PMID:                        27742469            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genetic manipulation of sirtuin 2 levels in vitro and in vivo modulates the levels of alpha-synuclein acetylation, its aggregation, and autophagy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28257421            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results indicate that fragmented amyloid-like aggregates of short alpha-syn fibrils are the key pathogenic seeds that trigger prion-like conversion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27382062            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In summary, we have combined multiple data sets to identify transcripts, which are strong candidates for being phenotypic modifiers, and demonstrated SNCA is a modifier of pathology in motor neuron disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28362802            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In alpha-synuclein knock-out mice there was a decrease in neuronal glucose metabolism in cerebral cortex gray matter.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28039592            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            alpha-synuclein may have a varying modulating effect on the growth dynamics and the fate of populations of DA neurons.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27021360            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In the olfactory bulb, globus pallidus and substantia nigra pars compacta, alpha-synuclein was expressed, but not in the cerebral cortex, subthalamic nucleus or thalamus.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26358191            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            identified alpha-synuclein as a new transcriptional target of p53            \u003ca rel=\"nofollow\"\u003e             PMID:                        26833254            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High SNCA expression is associated with epilepsy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26689812            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest the produced mouse lines represent a set of useful tools for studies of alpha-synuclein normal function and the role of this protein in disease pathogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26564109            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            that loss of glucocerebrosidase function may contribute to SNCA accumulation through inhibition of autophagy via PPP2A inactivation            \u003ca rel=\"nofollow\"\u003e             PMID:                        26378614            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            provides evidence for a novel interaction of alpha-synuclein and SOD1 that might be relevant for neurodegenerative diseases            \u003ca rel=\"nofollow\"\u003e             PMID:                        26643113            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            It found that chromosome 1 harbors an expression quantitative trait locus that modulates Sncg expression in the mouse retina, and identified the prefoldin-2 (PFDN2) gene as the candidate upstream modulator of Sncg expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26663874            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RNA virus-induced Asyn localizes to endoplasmic reticulum-derived membranes, modulates virus-induced endoplasmic reticulum stress signaling, and inhibits viral replication, growth, and injury in the central nervous system.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26719256            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The response of CPLX1 and Foxp1 levels to SNCA deficiency supports the notion that these factors are regulated by altered physiological function of alpha-synuclein.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25112678            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The pattern of expression and distribution of alpha-synuclein during the development of ciliary body and iris of mice, chick and fish data concluded that alpha-synuclein has important cellular function during eye development of studied animals.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25997379            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Longitudinal Metabolomics Profiling of Parkinson's Disease-Related alpha-Synuclein A53T Transgenic Mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26317866            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This would suggest that as complex I-deficient cells have already adapted to their mitochondrial defect, the subsequent toxic effects of alpha-synuclein are reduced.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26181201            \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":43915042750689,"sku":"BL-1921NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLZiAYvlRAACqz3oz7uA550_5412b156-cc49-46aa-bc85-ba3a2c2e99cd.jpg?v=1685851308"},{"product_id":"recombinant-human-dll4-protein-his-tag-bl-1949np","title":"Recombinant Human DLL4 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 Delta-like Protein 4 is produced by our Mammalian expression system and the target gene encoding Ser27-Pro524 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=\"Q9NR61\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/Q9NR61\/entry\"\u003eQ9NR61\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%;\"\u003eDelta-like protein 4; Drosophila Delta homolog 4; Delta4; DLL4\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%;\"\u003eDelta-like protein 4 (DLL4) is a type I membrane protein belonging to the Delta\/Serrate\/Lag2 (DSL) family of Notch ligands. In mammals, four Notch homologs (Notch 1 to4) and five ligands (DLL 1, 3 and 4, Jagged 1 and 2) have been identified. DLL4 is expressed highly and selectively within the arterial endothelium and has been shown to function as a ligand for Notch 1 and Notch 4. Human and mouse DLL4 shares 86% amino acid sequence identity. Notch ligands are transmembrane proteins with a DSL motif necessary for Notch binding, tandem EGF repeats, a transmembrane region and a short intracellular domain (ICD). Notch ligands are categorized into two subfamilies based on the presence of an extracellular cysteinerich domain and insertions that interrupt some EGF repeats in the Jagged but not the Delta ligand family. Interactions of Notch receptors with their ligands result in reciprocal regulated intramembrane proteolysis (RIP). RIP is a mechanism for transmembrane signal transduction that involves the sequential processing by a disintegrin metalloprotease (ADAM) and then by presenilin\/ γ secretase, resulting in shedding of the extracellular domains and the generation of the soluble ICD signaling fragments, 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%;\"\u003e81.2 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%;\"\u003e85-100 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 20mM Tris-HCl, 6% Trehalose, 4% Mannitol, 50mM NaCl, 0.05% Tween80, pH8.5.\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 0.1 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":43915048059105,"sku":"BL-1949NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLSmAMbdhAACBZ9VriiA174_d4935ba5-c3ae-4be7-a1ca-227d0ce376e8.jpg?v=1685851495"},{"product_id":"recombinant-mouse-p-selectin-protein-his-avi-tag-bl-2004np","title":"Biotinylated Mouse P-selectin Protein (C-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 Mouse P-selectin is produced by our Mammalian expression system and the target gene encoding Trp42­Ala709 is expressed with a Avi, 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=\"Q01102\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/Q01102\/entry\"\u003eQ01102\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%;\"\u003eP-selectin; CD62 antigen-like family member P; Granule membrane protein 140; GMP-140; Leukocyte-endothelial cell adhesion molecule 3; LECAM3; PADGEM\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%;\"\u003eP-selectin\/CD62P is a single-pass type I membrane protein which is a member of the Selectin family. It consists 768 amino acid (aa). P-selectin is a cell surface glycoprotein expressed by activated platelets and endothelial cells. It induced expression in lung, liver, kidney and heart after endotoxin treatment. Ca2+-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. It mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. it also mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1. P-selectin interacts with SNX17, PSGL1\/SEPL, PODXL2, mediates neutrophil adhesion and leukocyte rolling. This interaction requires the sialyl-Lewis X epitope of PSGL1 and PODXL2, and specific tyrosine sulfation on PSGL1.\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%;\"\u003e75.2 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%;\"\u003e110-130 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 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","brand":"Beta LifeScience","offers":[{"title":"20μg","offer_id":43915091149025,"sku":"BL-2004NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLa-AGTdRAADg7haW9HQ017_05ca4a39-ed50-4737-97e3-11304a1d0c45.jpg?v=1685852873"},{"product_id":"biotinylated-recombinant-human-pcsk9-protein-avi-tag-bl-2048np","title":"Biotinylated Human PCSK9 Protein (C-Avi)","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 Proprotein Convertase Subtilisin\/Kexin Type 9 is produced by our Mammalian expression system and the target gene encoding  Gln31-Gln692(Val474Ile,Gly670Glu) is expressed with a Avi 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%;\"\u003eQ8NBP7\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%;\"\u003eProprotein Convertase Subtilisin\/Kexin Type 9; Neural Apoptosis-Regulated Convertase 1; NARC-1; Proprotein Convertase 9; PC9; Subtilisin\/Kexin-Like Protease PC9; PCSK9; NARC1\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 Proprotein Convertase Subtilisin\/Kexin Type 9 (PCSK9) is a secretory subtilase belonging to the proteinase K subfamily. PCSK9 is synthesized as a soluble zymogen that undergoes autocatalytic intramolecular processing in the ER , the pro domain and mature chain secrete together through noncovalent interactions. PCSK9 binds with low-density lipoprotein receptor (LDLR) and plays a major regulatory role in cholesterol homeostasis. Inhibition of PCSK9 function by preventing PCSK9\/LDLR interaction is currently being explored as a means of lowering cholesterol levels. PCSK9 also binds to apolipoprotein receptor 2 (ApoER2), and play a role in the 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%;\"\u003e14\u0026amp;59 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\u0026amp;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%;\"\u003eSupplied as a 0.2 μm filtered solution of 50mM HEPES, 150mM NaCl, 20% 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%;\"\u003eCrucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1\/APOER) and apolipoprotein receptor 2 (LRP8\/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1\/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome\/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8\/APOER2 levels and related anti-apoptotic 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%;\"\u003eCytoplasm. Secreted. Endosome. Lysosome. Cell surface. Endoplasmic reticulum. Golgi apparatus. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes\/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation.\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%;\"\u003ePeptidase S8 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            20001           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            603776           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:255738           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000303208           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30205809            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            In Japanese male subjects, the concentrations of serum PCSK9 and TBIL were correlated with periodontal parameters.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29516504            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            C679X loss-of-function PCSK9 variant lowers fasting glucose levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30227170            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There was no protective or no deleterious effect of carrying PCSK9 LOF mutations on AD [Alzheimer disease]prevalence nor on age of onset, even when stratified by apolipoprotein E epsilon 4 genotype or by gender. Conclusion: Our data indicate that carrying PCSK9 LOF mutations has a neutral effect on neurocognitive health and the prevalence of AD [Alzheimer disease].            \u003ca rel=\"nofollow\"\u003e             PMID:                        29562810            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High serum PCSK9 levels predict acute coronary syndrome occurrence at 24-month follow-up after carotid endarterectomy in patients with severe carotid artery stenosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29754909            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Taken together, the present study provides evidence of a pro-inflammatory action of PCSK9 on macrophages, mainly dependent by the LDLR.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29396513            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HepG2 cell lines transfected with siRNA directed to PCSK9 were challenged with Hcy, homocysteine thiolactone (HTL), testosterone, 5alpha-dihydroxytestosterone (5alpha-DHT), or estradiol for 24h, leading to an overt expression of PCSK9 and down-regulated expression of LDLR.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29660344            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Plasma PCSK9 levels and lipoprotein distribution are preserved in hypolipoproteinemia carriers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29852278            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Inverse correlation between PCSK9 and CD36 in hypertrophic adipocytes may be associated with AAA development.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30210081            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Plasma Lp(a) level was associated with PCSK9 in patients with heterozygous familial hypercholesterolemia            \u003ca rel=\"nofollow\"\u003e             PMID:                        29129821            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors performed an analysis of public databases and literature for every variant published associated with FH, in the genes LDLR, APOB, and PCSK9.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29261184            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 levels increase as glucose metabolism deteriorated. Serum PCSK9 levels positively correlated with 2-hPG (2-h postchallenge plasma glucose) in Chinese Han patients with glucose metabolic diseases.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29343301            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9i-treated patients had higher rates of cardiovascular comorbidities.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28849360            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 overexpression in the aorta may promote acute aortic dissection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29197601            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High PCSK9 expression is associated with metabolic syndrome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28283395            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A positive association between plasma PCSK9 concentration and coronary artery calcification in untreated patients with angina-like chest pain was observed in our study, suggesting that further investigation may be needed in order to confirm our primary findings and explore the clinical implications            \u003ca rel=\"nofollow\"\u003e             PMID:                        28166668            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In conclusion, PCSK9 inhibitors such as alirocumab may be an excellent lipid lowering agent in patients with statin intolerance and myotonic dystrophy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29056268            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Obesity and type 2 diabetes were associated with significantly higher serum levels in young women, but not in young men            \u003ca rel=\"nofollow\"\u003e             PMID:                        28093849            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Reduction of LDL-C With PCSK9 Inhibition in Heterozygous Familial Hypercholesterolemia Disorder (RUTHERFORD; phase 2) and RUTHERFORD-2 (phase 3).            \u003ca rel=\"nofollow\"\u003e             PMID:                        29066265            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We present a case of homozygous familial defective apolipoprotein B-100 due to APOB R3500Q (rs5742904) treated with evolocumab ..Identification of a patient homozygous for familial defective apolipoprotein B-100(FDB) and successful treatment with PCSK9 inhibition            \u003ca rel=\"nofollow\"\u003e             PMID:                        28988723            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A complex link between hepatitis C virus infection and PCSK9 has emerged, in which a bidirectional loop of interactions is conceivable. (Review)            \u003ca rel=\"nofollow\"\u003e             PMID:                        28722331            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genetically determined PCSK9 deficiency might be associated with ectopic fat accumulation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28758421            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results suggest that PCSK9 rs7552841 is associated with plasma lipids profiles only in female adolescents, but not in male students. This association can be modified and negated by posttraumatic stress disorder.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29081489            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 carriers tended to be associated with an increased response to simvastatin therapy            \u003ca rel=\"nofollow\"\u003e             PMID:                        28851085            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 polymorphism may affect HIV pathogenesis, particularly in HIV\/hepatitis C coinfected women. A likely mechanism for this effect is PCSK9-mediated regulation of cholesterol metabolism.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29120899            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There was no relationship between plasma PCSK9 levels and arterial stiffness.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28816230            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 variants associated with lower LDL cholesterol were also associated with circulating higher fasting glucose concentration, body weight and an increased risk of type 2 diabetes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27908689            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ABGL4, LRP8 and PCSK9 polymorphisms and gene interactions increase cardiometabolic risk.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27853278            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these results provide insights into a novel coordinated interplay among three important molecular players in lipid homeostasis - circulating miR-24, miR-223 and PCSK9 - whose regulation is affected by HCV infection and treatment-based viral cure.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28864162            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study aimed to explore the direct toxicity of proprotein convertase subtilisin\/kexin type 9 (PCSK9) to atherosclerosis (AS) and its association with apoptotic endothelial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28656218            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The minor allele frequency of the PCSK9 A443T, I474V, E670G, and C679X polymorphisms in healthy and malaria-infected Malian children was 0.12, 0.20, 0.26, and 0.02, respectively. 17.6% of subjects carried two of the four SNPs examined. Carriers of the minor allele of the E670G PCSK9 polymorphism might be more susceptible to severe malaria.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29447211            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Circulating PCSK9 concentration as a continuous variable was not significantly associated with the risk of cardiovascular events. More well-designed studies are needed to clarify the role of PCSK9 in cardiovascular risk.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28413188            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that the elevation in plasma apoB-48 levels associated with FH is independent of PCSK9 levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28619117            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we discuss current experimental and clinical evidence of the role of PCSK9 and its inhibition on lipid metabolism and several pathologic conditions with a focus on clinical outcomes--{REVIEW}            \u003ca rel=\"nofollow\"\u003e             PMID:                        27533061            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The E670G polymorphism of the PCSK9 gene is associated with the lipid levels and risk for coronary heart disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28981947            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Here, we assess the available evidence for the association of PCSK9 status with the incidence and control of diabetes mellitus in preclinical and clinical studies, and identify molecular mechanisms regulating PCSK9 expression in the diabetic state. [Review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        28111330            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results demonstrated the molecular mechanisms of how HCV modulates PCSK9 promoter activity and advanced our understanding on the mutual interactions between HCV and PCSK9.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29397939            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings provide useful information for researchers interested in the fields of PCSK9 genetics and cardiovascular risk prediction not only for designing future studies, but also for clinical and public health applications            \u003ca rel=\"nofollow\"\u003e             PMID:                        28606094            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Circulating PCSK9 is significantly related to arterial stiffness, independent of sex and menopausal status in women.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28468788            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study demonstrated PCSK9 as a direct target of miR-224 and increased miR-224 or decreased PCSK9 could promote apoptosis and suppress proliferation, invasion of tumor cell line in pancreatic neuroendocrine neoplasms.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28036293            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There are no associations between PCSK9 levels and either glucose or lipid homeostasis parameters. Nevertheless, a statistically significant link was observed between PCSK9 and markers of insulin homeostasis, solely in CF patients who presented normal glucose tolerance.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28447578            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 interacts with heparan sulfate proteoglycans.Heparan sulfate proteoglycans binding is required for PCSK9-induced LDLR degradation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28894089            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study suggest that these biomarker PCSK9 can serve as a potential non-invasive early diagnosis platform reflecting PiB-PET imaging for Mild Cognitive Impairment and Alzheimer's Disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27392853            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 is not altered specifically in PCOS.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29109005            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A high-throughput time-resolved fluorescence resonance energy transfer assay for autocleavage has been developed using a PCSK9 monoclonal antibody that is sensitive to the conformational changes that occur upon maturation of the proprotein.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27412534            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These studies provide a definitive characterization of the composition and activity of the truncated form of PCSK9 found in human serum            \u003ca rel=\"nofollow\"\u003e             PMID:                        24776539            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 loss-of-function variants were associated with a pooled odds ratio for coronary heart disease of 0.51 in blacks and 0.82 in whites.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28768753            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mature PCSK9 associated with atheroma volume and impaired vessel remodeling in HeFH patients with coronary artery disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        28502498            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Despite having lower LDL-C, circulating PCSK9 levels were increased in patients coinfected with HIV and HCV in parallel with elevations in the inflammatory, proatherogenic cytokine interleukin-6.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27130349            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Circulating PCSK9 is associated with New-onset diabetes after transplantation (NODAT) in renal transplant recipients. The PCSK9 pathway may contribute to the pathogenesis of NODAT.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28461454            \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":43915185357025,"sku":"BL-2048NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLWWAR9eaAACnYuRzlFQ543_281104d0-52d7-4188-9f05-3b5cbe8cbfb7.jpg?v=1685851232"},{"product_id":"recombinant-human-pcsk9-protein-his-avi-tagi-bl-2049np","title":"Biotinylated Human PCSK9 Protein (C-8His-HA-Avi)","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 Proprotein Convertase Subtilisin\/Kexin Type 9 is produced by our Mammalian expression system and the target gene encoding  Gln31-Gln692(Val474Ile,Gly670Glu) is expressed with a 8His, HA, Avi 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%;\"\u003eQ8NBP7\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%;\"\u003eProprotein Convertase Subtilisin\/Kexin Type 9; Neural Apoptosis-Regulated Convertase 1; NARC-1; Proprotein Convertase 9; PC9; Subtilisin\/Kexin-Like Protease PC9; PCSK9; NARC1\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 Proprotein Convertase Subtilisin\/Kexin Type 9 (PCSK9) is a secretory subtilase belonging to the proteinase K subfamily. PCSK9 is synthesized as a soluble zymogen that undergoes autocatalytic intramolecular processing in the ER , the pro domain and mature chain secrete together through noncovalent interactions. PCSK9 binds with low-density lipoprotein receptor (LDLR) and plays a major regulatory role in cholesterol homeostasis. Inhibition of PCSK9 function by preventing PCSK9\/LDLR interaction is currently being explored as a means of lowering cholesterol levels. PCSK9 also binds to apolipoprotein receptor 2 (ApoER2), and play a role in the 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%;\"\u003e14\u0026amp;62 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\u0026amp;58-70\u0026amp;90-150 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 50mM HEPES, 150mM NaCl, 20% 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%;\"\u003eCrucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1\/APOER) and apolipoprotein receptor 2 (LRP8\/APOER2), and promotes their degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1\/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome\/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8\/APOER2 levels and related anti-apoptotic 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%;\"\u003eCytoplasm. Secreted. Endosome. Lysosome. Cell surface. Endoplasmic reticulum. Golgi apparatus. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes\/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation.\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%;\"\u003ePeptidase S8 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            20001           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            603776           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:255738           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000303208           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30205809            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            In Japanese male subjects, the concentrations of serum PCSK9 and TBIL were correlated with periodontal parameters.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29516504            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            C679X loss-of-function PCSK9 variant lowers fasting glucose levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30227170            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There was no protective or no deleterious effect of carrying PCSK9 LOF mutations on AD [Alzheimer disease]prevalence nor on age of onset, even when stratified by apolipoprotein E epsilon 4 genotype or by gender. Conclusion: Our data indicate that carrying PCSK9 LOF mutations has a neutral effect on neurocognitive health and the prevalence of AD [Alzheimer disease].            \u003ca rel=\"nofollow\"\u003e             PMID:                        29562810            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High serum PCSK9 levels predict acute coronary syndrome occurrence at 24-month follow-up after carotid endarterectomy in patients with severe carotid artery stenosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29754909            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Taken together, the present study provides evidence of a pro-inflammatory action of PCSK9 on macrophages, mainly dependent by the LDLR.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29396513            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HepG2 cell lines transfected with siRNA directed to PCSK9 were challenged with Hcy, homocysteine thiolactone (HTL), testosterone, 5alpha-dihydroxytestosterone (5alpha-DHT), or estradiol for 24h, leading to an overt expression of PCSK9 and down-regulated expression of LDLR.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29660344            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Plasma PCSK9 levels and lipoprotein distribution are preserved in hypolipoproteinemia carriers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29852278            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Inverse correlation between PCSK9 and CD36 in hypertrophic adipocytes may be associated with AAA development.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30210081            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Plasma Lp(a) level was associated with PCSK9 in patients with heterozygous familial hypercholesterolemia            \u003ca rel=\"nofollow\"\u003e             PMID:                        29129821            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors performed an analysis of public databases and literature for every variant published associated with FH, in the genes LDLR, APOB, and PCSK9.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29261184            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 levels increase as glucose metabolism deteriorated. Serum PCSK9 levels positively correlated with 2-hPG (2-h postchallenge plasma glucose) in Chinese Han patients with glucose metabolic diseases.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29343301            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9i-treated patients had higher rates of cardiovascular comorbidities.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28849360            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 overexpression in the aorta may promote acute aortic dissection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29197601            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High PCSK9 expression is associated with metabolic syndrome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28283395            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A positive association between plasma PCSK9 concentration and coronary artery calcification in untreated patients with angina-like chest pain was observed in our study, suggesting that further investigation may be needed in order to confirm our primary findings and explore the clinical implications            \u003ca rel=\"nofollow\"\u003e             PMID:                        28166668            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In conclusion, PCSK9 inhibitors such as alirocumab may be an excellent lipid lowering agent in patients with statin intolerance and myotonic dystrophy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29056268            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Obesity and type 2 diabetes were associated with significantly higher serum levels in young women, but not in young men            \u003ca rel=\"nofollow\"\u003e             PMID:                        28093849            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Reduction of LDL-C With PCSK9 Inhibition in Heterozygous Familial Hypercholesterolemia Disorder (RUTHERFORD; phase 2) and RUTHERFORD-2 (phase 3).            \u003ca rel=\"nofollow\"\u003e             PMID:                        29066265            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We present a case of homozygous familial defective apolipoprotein B-100 due to APOB R3500Q (rs5742904) treated with evolocumab ..Identification of a patient homozygous for familial defective apolipoprotein B-100(FDB) and successful treatment with PCSK9 inhibition            \u003ca rel=\"nofollow\"\u003e             PMID:                        28988723            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A complex link between hepatitis C virus infection and PCSK9 has emerged, in which a bidirectional loop of interactions is conceivable. (Review)            \u003ca rel=\"nofollow\"\u003e             PMID:                        28722331            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genetically determined PCSK9 deficiency might be associated with ectopic fat accumulation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28758421            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results suggest that PCSK9 rs7552841 is associated with plasma lipids profiles only in female adolescents, but not in male students. This association can be modified and negated by posttraumatic stress disorder.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29081489            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 carriers tended to be associated with an increased response to simvastatin therapy            \u003ca rel=\"nofollow\"\u003e             PMID:                        28851085            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 polymorphism may affect HIV pathogenesis, particularly in HIV\/hepatitis C coinfected women. A likely mechanism for this effect is PCSK9-mediated regulation of cholesterol metabolism.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29120899            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There was no relationship between plasma PCSK9 levels and arterial stiffness.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28816230            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 variants associated with lower LDL cholesterol were also associated with circulating higher fasting glucose concentration, body weight and an increased risk of type 2 diabetes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27908689            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ABGL4, LRP8 and PCSK9 polymorphisms and gene interactions increase cardiometabolic risk.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27853278            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these results provide insights into a novel coordinated interplay among three important molecular players in lipid homeostasis - circulating miR-24, miR-223 and PCSK9 - whose regulation is affected by HCV infection and treatment-based viral cure.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28864162            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study aimed to explore the direct toxicity of proprotein convertase subtilisin\/kexin type 9 (PCSK9) to atherosclerosis (AS) and its association with apoptotic endothelial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28656218            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The minor allele frequency of the PCSK9 A443T, I474V, E670G, and C679X polymorphisms in healthy and malaria-infected Malian children was 0.12, 0.20, 0.26, and 0.02, respectively. 17.6% of subjects carried two of the four SNPs examined. Carriers of the minor allele of the E670G PCSK9 polymorphism might be more susceptible to severe malaria.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29447211            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Circulating PCSK9 concentration as a continuous variable was not significantly associated with the risk of cardiovascular events. More well-designed studies are needed to clarify the role of PCSK9 in cardiovascular risk.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28413188            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that the elevation in plasma apoB-48 levels associated with FH is independent of PCSK9 levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28619117            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we discuss current experimental and clinical evidence of the role of PCSK9 and its inhibition on lipid metabolism and several pathologic conditions with a focus on clinical outcomes--{REVIEW}            \u003ca rel=\"nofollow\"\u003e             PMID:                        27533061            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The E670G polymorphism of the PCSK9 gene is associated with the lipid levels and risk for coronary heart disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28981947            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Here, we assess the available evidence for the association of PCSK9 status with the incidence and control of diabetes mellitus in preclinical and clinical studies, and identify molecular mechanisms regulating PCSK9 expression in the diabetic state. [Review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        28111330            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results demonstrated the molecular mechanisms of how HCV modulates PCSK9 promoter activity and advanced our understanding on the mutual interactions between HCV and PCSK9.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29397939            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings provide useful information for researchers interested in the fields of PCSK9 genetics and cardiovascular risk prediction not only for designing future studies, but also for clinical and public health applications            \u003ca rel=\"nofollow\"\u003e             PMID:                        28606094            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Circulating PCSK9 is significantly related to arterial stiffness, independent of sex and menopausal status in women.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28468788            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study demonstrated PCSK9 as a direct target of miR-224 and increased miR-224 or decreased PCSK9 could promote apoptosis and suppress proliferation, invasion of tumor cell line in pancreatic neuroendocrine neoplasms.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28036293            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There are no associations between PCSK9 levels and either glucose or lipid homeostasis parameters. Nevertheless, a statistically significant link was observed between PCSK9 and markers of insulin homeostasis, solely in CF patients who presented normal glucose tolerance.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28447578            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 interacts with heparan sulfate proteoglycans.Heparan sulfate proteoglycans binding is required for PCSK9-induced LDLR degradation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28894089            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of this study suggest that these biomarker PCSK9 can serve as a potential non-invasive early diagnosis platform reflecting PiB-PET imaging for Mild Cognitive Impairment and Alzheimer's Disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27392853            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 is not altered specifically in PCOS.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29109005            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A high-throughput time-resolved fluorescence resonance energy transfer assay for autocleavage has been developed using a PCSK9 monoclonal antibody that is sensitive to the conformational changes that occur upon maturation of the proprotein.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27412534            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These studies provide a definitive characterization of the composition and activity of the truncated form of PCSK9 found in human serum            \u003ca rel=\"nofollow\"\u003e             PMID:                        24776539            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PCSK9 loss-of-function variants were associated with a pooled odds ratio for coronary heart disease of 0.51 in blacks and 0.82 in whites.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28768753            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mature PCSK9 associated with atheroma volume and impaired vessel remodeling in HeFH patients with coronary artery disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        28502498            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Despite having lower LDL-C, circulating PCSK9 levels were increased in patients coinfected with HIV and HCV in parallel with elevations in the inflammatory, proatherogenic cytokine interleukin-6.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27130349            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Circulating PCSK9 is associated with New-onset diabetes after transplantation (NODAT) in renal transplant recipients. The PCSK9 pathway may contribute to the pathogenesis of NODAT.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28461454            \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":43915032133857,"sku":"BL-2049NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLWWAQjY-AADJF1t2Lug694_a60427bf-baef-45a4-81ef-c9b11fe46673.jpg?v=1685850983"},{"product_id":"recombinant-mouse-mmp-9-mmp9-protein-his-tag-bl-2050np","title":"Recombinant Mouse MMP-9 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 Matrix Metalloproteinase-9 is produced by our Mammalian expression system and the target gene encoding Ala20-Pro730 is expressed with a 10His tag at the C-terminus.The proenzyme needs to be activated by APMA for an activated form.\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=\"P41245\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/P41245\/entry\"\u003eP41245\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%;\"\u003eMatrix metalloproteinase-9; MMP-9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; GELB\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%;\"\u003eMatrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 may be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain.\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%;\"\u003e80.2 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%;\"\u003e100 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, 150mM NaCl, 20% Glycerol, pH7.5.\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 0.1 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":43915033542881,"sku":"BL-2050NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLW2ASyDeAACeSmcHwNo880_dc4b77cb-b51e-4bcd-8bac-77b4c74632fb.jpg?v=1685851030"},{"product_id":"recombinant-mouse-baffr-protein-fc-tag-bl-2199np","title":"Recombinant Mouse BAFFR 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 Tumor Necrosis Factor Receptor Superfamily Member 13C is produced by our Mammalian expression system and the target gene encoding Ser10-Ala 71 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=\"Q9D8D0\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/Q9D8D0\/entry\"\u003eQ9D8D0\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%;\"\u003eBAFF R; BAFFR; BR3; CD268; TNFRSF13C\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 13C (TNFRSF13C) also known as B-cell-activating factor receptor (BAFFR) and CD268 antigen, is a member of the tumor necrosis factor receptor superfamily. BAFF promotes the survival of B cells and is essential for B cell maturation. BAFF binds to three TNF receptor superfamily members: B-cell maturation antigen (BCMA\/TNFRSF17), transmembrane activator and calcium-modulator and cyclophilin ligand interactor (TACI\/TNFRSF13B) and BAFF receptor (BAFF R\/BR3\/TNFRSF13C). These receptors are type III transmembrane proteins that lack a signal peptide. BAFF R is highly expressed in spleen, lymph node and resting B cells. It is also expressed at lower levels in activated B cell, in resting CD4+ T cells, in thymus and peripheral blood leukocytes. BAFF knockout mice lack mature B cells. Similarly, A\/WySnJ mice that are defective in BAFF-R intracellular signaling also lack mature B cells, suggesting that BAFF R is the critical receptor for BAFF during B lymphopoiesis. It has been proposed that abnormally high levels of BAFFR\/TNFRSF13C (CD268) may contribute to the pathogenesis of autoimmune diseases by enhancing the survival of autoreactive B cells.\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%;\"\u003e33.8 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%;\"\u003e40-55 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":43915063558369,"sku":"BL-2199NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLQ2AUSKRAACLdn6X1S8144_a0942b7d-9657-4c6b-bc40-b895569111a8.jpg?v=1685851983"},{"product_id":"recombinant-human-baff-protein-his-tag-bl-2200np","title":"Recombinant Human BAFF 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 TNF Ligand Superfamily Member 13B is produced by our Mammalian expression system and the target gene encoding Ala134-Leu285 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%;\"\u003eQ9Y275\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 ligand superfamily member 13B; B lymphocyte stimulator; BLyS; B-cell-activating factor; BAFF; Dendritic cell-derived TNF-like molecule; TNF- and APOL-related leukocyte expressed ligand 1; TALL-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%;\"\u003eTNFSF13B\/TNFSF20 belongs to the tumor necrosis factor family. It abundantly is expressed in peripheral blood Leukocytes and is specifically expressed in monocytes and macrophages. Also found in the spleen, lymph node, bone marrow, T-cells and dendritic cells. A lower expression seen in placenta, heart, lung, fetal liver, thymus, and pancreas. Isoform 2 is expressed in many myeloid cell lines. Cytokine that binds to TNFRSF13B\/TACI and TNFRSF17\/BCMA. TNFSF13\/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR\/BR3) promotes the survival of mature B-cells and the B-cell response. Isoform 2 seems to inhibit isoform 1 secretion and bioactivity. Isoform 3 acts as a transcription factor for its own parent gene, in association with NF-kappa-B p50 subunit, at least in autoimmune and proliferative B-cell diseases. The presence of Delta4BAFF is essential for soluble BAFF release by IFNG\/IFN-gamma-stimulated monocytes and for B-cell survival. It can directly or indirectly regulate the differential expression of a large number of genes involved in the innate immune response and the regulation of apoptosis. Isoform 2 heteromultimerizes with isoform 1, probably limiting the amount of functional isoform 1 on the cell surface. Isoform 3 is unlikely form trimers or bind to BAFF receptors. Mature human BAFF consists of a 46 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 218 aa extracellular domain (ECD) with a stalk region and one TNF-like domain. Within aa 134-285 of the ECD, human BAFF shares 72% aa sequence identity with mouse BAFF.\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%;\"\u003e19.3 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%;\"\u003e22 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 \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%;\"\u003eCytokine that binds to TNFRSF13B\/TACI and TNFRSF17\/BCMA. TNFSF13\/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR\/BR3) promotes the survival of mature B-cells and the B-cell response.; Isoform 2 seems to inhibit isoform 1 secretion and bioactivity.; Acts as a transcription factor for its own parent gene, in association with NF-kappa-B p50 subunit, at least in autoimmune and proliferative B-cell diseases. The presence of Delta4BAFF is essential for soluble BAFF release by IFNG\/IFN-gamma-stimulated monocytes and for B-cell survival. It can directly or indirectly regulate the differential expression of a large number of genes involved in the innate immune response and the regulation of apoptosis.\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 II membrane protein.; [Tumor necrosis factor ligand superfamily member 13b, soluble 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%;\"\u003eTumor necrosis factor 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            11929           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            603969           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:10673           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000365048           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29572442            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            analysis of how BAFF is neutralized by belimumab gives insight into treatment of systemic lupus erythematosus            \u003ca rel=\"nofollow\"\u003e             PMID:                        29572471            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study uncovers a previously unrecognized regulation of BAFF by testosterone and raises important questions about BAFF in testosterone-mediated protection against autoimmunity. Among healthy men, serum BAFF levels are higher in men with low testosterone.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29802242            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High BAFF expression is associated with systemic lupus erythematosus.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28992184            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Co-immunoprecipitation analysis and siRNA-mediated suppression of CREB expression indicated that phospho-CREB has a positive effect on pro-inflammatory gene expression in the crosstalk between BAFF- and TLR4-mediated signaling by forming trimeric complexes containing NF-kappaB, CBP, and CREB            \u003ca rel=\"nofollow\"\u003e             PMID:                        28374824            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study shows that BAFF augments IgA2 and IL-10 production by TLR7\/8 stimulated total peripheral blood B cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        28921509            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            elevated pretransplant serum BAFF levels negatively affect renal allograft survival and represent a risk factor for allosensitization and subsequent antibody-mediated rejection            \u003ca rel=\"nofollow\"\u003e             PMID:                        29277566            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Increased BAFF expression is associated with B cell class switching in patients with tuberculous pleural effusion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29845274            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression patterns of BAFF and its receptors differ according to lupus nephritis class.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29087261            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum BAFF levels are elevated in idiopathic inflammatory myositis, more so in children.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29516280            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Post-transplant antibody mediated rejection in kidney transplantation recipients can be predicted by perioperative elevations in serum BAFF level.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27888573            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results of the present study revealed a correlation between BAFF and the PI3K\/Akt\/mTOR signaling pathway, and it is hypothesized that they are involved in the pathogenesis of lupus nephritis            \u003ca rel=\"nofollow\"\u003e             PMID:                        28849060            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggest that increased levels of BAFF and APRIL produced in the central nervous system may influence the development of anti-neutrophil cytoplasmic antibody-hypertrophic pachymeningitis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28847534            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Blood B lymphocyte stimulator (BLyS)\/BAFF levels of HIV-uninfected commercial sex workers (CSWs) were lower than those observed in both HIV-infected CSW and HIV-uninfected non-CSW groups.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27561453            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our study throws light on the crosstalk between BAFF and BCR signaling pathways in neoplastic B cells, and provides insights into the mechanistic effects of SYK inhibitors in CLL.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28838991            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            genetic polymorphisms of BAFF may increase the risk of posttransplant development of donor specific antibodies in kidney allograft recipients            \u003ca rel=\"nofollow\"\u003e             PMID:                        28624489            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            P\\pre-sensitized patients had significantly higher BAFF levels before transplantation and suffered significantly more often from early steroid-resistant, mainly antibody-mediated rejections            \u003ca rel=\"nofollow\"\u003e             PMID:                        28867309            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Elevated blood BAFF levels could be associated with a more stable disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27383531            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF rs9514828 polymorphism may be associated with the chronic hepatitis and the combinatorial action of rs9514828 and rs12583006 may confer susceptibility to chronic HBV infection and the resolution of the infection, suggesting that host genetic factors associated with B cell mediated immune responses are involved in chronic HBV infection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28627389            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrated that An Increase of Cerebrospinal Fluid B-cell Activating Factor Level in Pediatric Patients With Acute Viral Encephalitis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28259511            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data show that BAFF levels at the time of cGvHD diagnosis are associated with non-relapse-mortality, and also are potentially useful for risk stratification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28481353            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF-R was consistently expressed on B cells infected by HCMV. Enhancement of BAFF\/BAFF-R signaling decreased the apoptosis rate and extended the survival of B cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28442365            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            soluble BCMA sequesters circulating BAFF, thereby preventing it from performing its signaling to stimulate normal B-cell and plasma cell development, resulting in reduced polyclonal antibody levels in multiple myeloma patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26960399            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            up-regulated expression in intractable temporal lobe epilepsy            \u003ca rel=\"nofollow\"\u003e             PMID:                        28441631            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results showed that serum BAFF in nasal type, extranodal NK\/T cell lymphoma patients was significantly higher than that in control group and negatively correlated with patients' survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27668971            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF has a role in inducing IL35 production by regulatory B cells in lupus            \u003ca rel=\"nofollow\"\u003e             PMID:                        28844943            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Inhibition of ADAM10 augments BAFF-dependent survival of primary human B cells, whereas inhibition of ADAM17 increases BAFFR expression levels            \u003ca rel=\"nofollow\"\u003e             PMID:                        28249164            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data presented show that B-cell activating factor (BAFF) plays a central role in the induction and maintenance of cigarette smoke-induced pulmonary antinuclear antibodies and suggest a therapeutic potential for BAFF blockade in limiting autoimmune processes associated with smoking.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28039405            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Among the BAFF receptors in a cohort of rheumatoid arthritis (RA) patients, the AA have shown, by fluorescence activated cell sorter (FACS) analysis of median fluorescence intensity (MFI), that transmembrane activator and calcium-modulating cyclophilin ligand interactor (TACI) and B cell maturation antigen (BCMA) do not change            \u003ca rel=\"nofollow\"\u003e             PMID:                        28834574            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The BAFF promoter increased in response to TNF-alpha treatment or overexpression of HIF-1alpha. However, TNF-alpha-induced BAFF expression and promoter activity decreased after treatment with the ERK inhibitor PD98059.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28383556            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study indicates that orbital fibroblasts from Graves' orbitopathy can express BAFF and mediate the intraorbital survival of B cells via BAFF mechanism.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28087387            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Rapamycin attenuates excessive hsBAFF-induced cell proliferation\/survival via blocking mTORC1\/2 signaling in normal and neoplastic B-lymphoid cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28300280            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Inhibition of B cell plasmablast differentiation by reduction of Aiolos and Ikaros may have utility in the treatment of systemic lupus erythematosus , where elevated levels of BAFF and Aiolos may prime CD27(+) memory and double negative memory-like B cells to become Ab-producing plasmablasts in the presence of BAFF and proinflammatory cytokines.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28848067            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BCMA has other contributors for ligands binding except DxL motif. The affinity of BCMA for APRIL higher than for BAFF may be caused by the segment outside of the conservative DxL motif. Moreover, the exposition of new binding modes of BCMA2 interacting with APRIL may establish the foundation of designing novel drugs in the future            \u003ca rel=\"nofollow\"\u003e             PMID:                        28260502            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study demonstrated a high prevalence of endogenous antibodies to BAFF in a multi-ethnic Asian systemic lupus erythematosus (SLE) cohort; while levels of serum BAFF correlated positively with disease activity, levels of anti-BAFF antibody were correlated negatively with levels of its target cytokine, anti-dsDNA antibody and clinical disease activity            \u003ca rel=\"nofollow\"\u003e             PMID:                        28388832            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study provides new useful information about the increased levels of BAFF observed during HIV-1 infection and highlights the importance of macrophages as a source of BAFF            \u003ca rel=\"nofollow\"\u003e             PMID:                        27022194            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The novel association between BAFF and inflammatory bowel disease (IBD) seems to identify that BAFF might regulate the inflammatory process in these diseases and it appears to be a potential marker of IBD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27056038            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In BAFF, rs2893321 may be a susceptible genetic variant for the development of GD and AITDs. Associations of rs2893321 with susceptibility to GD and AITDs and the correlation between rs2893321 and TAb exhibit a dimorphic pattern. Additional studies with larger sample sizes are required to confirm our findings.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27136204            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF and IL-17A are associated with different subphenotypes of primary Sjogren's syndrome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25941062            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The expression levels of serum BAFF and the three receptors (TACI, BCMA and BAFF-R) in non-Hodgkin lymphoma patients were significantly higher than in healthy controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28028945            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Plasma BAFF levels were positively associated with serum creatinine, proteinuria, uric acid and group A Streptococcus infection index in patients with IgA nephropathy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28260100            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study shows that chicoric acid suppresses BAFF expression by inhibiting NF-kappaB activity, and chicoric acid may serve as a novel therapeutic agent to down-regulate excessive BAFF expression in autoimmune diseases            \u003ca rel=\"nofollow\"\u003e             PMID:                        28122293            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings indicate that BAFF expression is significantly increased in chronic rhinosinusitis with nasal polyps patients and may orchestrate inflammatory load in polyp tissues by regulating T and B cell-mediated response.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28035475            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Urinary APRIL (uAPRIL) and BAFF (uBAFF) levels were raised significantly in AN.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27804111            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF levels are lower in patients with antibody-mediated kidney rejection and also in patients with concurrent humoral and cellular rejection compared with patients without rejection            \u003ca rel=\"nofollow\"\u003e             PMID:                        28083608            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The BLyS level is increased in some lupus patients. There was a moderate correlation with titers of anti-DNA antibody and disease activity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27100979            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In Sjogren's syndrome (SS) patients, EULAR Sjogren's syndrome disease activity index (ESSDAI) is negatively associated with serum levels of 25(OH)-D3 and positively associated with BAFF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28074193            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results suggest that miR-202 functions as a modulator that can negatively regulate BAFF by inhibiting multiple myeloma tumor cell survival, growth, and adhesion in the bone marrow microenvironment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25971527            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Variants in BAFF gene is associated with chronic lymphocytic leukemia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27468724            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results demonstrated that BAFF has an important role in the pathogenesis of newly diagnosed childhood immune thrombocytopenia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24911453            \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":43915023122657,"sku":"BL-2200NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLQ2AKHj-AACR7K4TuXE433_8a803983-4d95-4c9a-a726-358b778759c8.jpg?v=1685850768"},{"product_id":"recombinant-human-tslp-protein-his-tag-bl-2201np","title":"Recombinant Human TSLP 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 Human Thymic Stromal lymphopoietin is produced by our Mammalian expression system and the target gene encoding Tyr29-Gln159 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%;\"\u003eQ969D9\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%;\"\u003eThymic stromal lymphopoietin; TSLP\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%;\"\u003eThymic stromal lymphopoietin (TSLP) is a novel member of the hemopoietic cytokine family that promotes the development of B cells and shares overlapping activity with IL-7. The human TSLP protein comprises a 28 amino acids (aa) signal sequence and 131 aa mature region. Human TSLP has two isoforms lfTSLP and sfTSLP produced by alternative splicing . lfTSLP is expressed in a number of tissues including heart, liver and prostate, and sfTSLP (63aa) is predominantly expressed in keratinocytes of oral mucosa, skin and in salivary glands. In aa sequence level, Human TSLP displays about 43% identity with mouse TSLP.TSLP is a cytokine that functions mainly on myeloid cells; it induces the release of T cell-attracting chemokines from monocytes and enhances the maturation of CD11c(+) dendritic cells.TSLP has proliferative effects on the myeloid cell line and may initiate asthma or atopic dermatitis responses by directly activating mast cells . TSLP signals cells via the interleukin-7 receptor-α chain (IL-7Rα),shared with IL-7, together with the TSLP receptor (TSLPR) subunit. Recent studies indicate that TSLP and its receptor are novel therapeutic targets for rheumatoid arthritis,for increased intraarticular TSLP concentrations in patients has caused chemotaxis and activation of arthritogenic T cells.\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%;\"\u003e16.3 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%;\"\u003e8-10\u0026amp;16-24 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 \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%;\"\u003eCytokine that induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c(+) dendritic cells. Can induce allergic inflammation by directly activating mast cells.; May act as an antimicrobial peptide in the oral cavity and on the skin.\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            30743           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            607003           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:85480           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000339804           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28368013            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Effects of Linalyl Acetate on Thymic Stromal Lymphopoietin Production in Mast Cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30011850            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            presence of epithelium-derived TSLP in the eustachian tubes plays important role in the onset of eosinophilic otitis media            \u003ca rel=\"nofollow\"\u003e             PMID:                        29272985            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a new mechanism of T cell stimulation in human skin was identified, demonstrating the direct induction of T cell migration by TSLP in the absence of DCs.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28377574            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the secretion of TSLP by keratinocytes is induced by the HIV-1 viral synapse in a miR-375 controlled manner            \u003ca rel=\"nofollow\"\u003e             PMID:                        28443609            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            production increased at skin sites of ovalbumin sensitization            \u003ca rel=\"nofollow\"\u003e             PMID:                        27992078            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Sera of patients with infantile eosinophilic gastroenteritis showed a specific increase in both thymic stromal lymphopoietin and IL-33 levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26948075            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            short and long thymic stromal lymphopoietin isoforms have roles in house dust mite-induced asthmatic airway epithelial barrier disruption            \u003ca rel=\"nofollow\"\u003e             PMID:                        27996052            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            DeltaNp73 was abundantly expressed in the atopic dermatitis epidermis and increased the release of TSLP via NF-kappaB activation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28655470            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study shows that long form of thymic stromal lymphopoietin of keratinocytes is induced by protein allergens            \u003ca rel=\"nofollow\"\u003e             PMID:                        28720058            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we found that activation of the protease-activated receptor 1 (PAR1) induced secretion of TSLP by the corneal stromal cells... we proposed that TSLP might function as the link between increased protease activity and inflammatory responses or itch sensation in the corneas            \u003ca rel=\"nofollow\"\u003e             PMID:                        28631887            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TSLP-HOTAIR axis also plays a protective role in low-density lipoprotein (ox-LDL)-induced Endothelial cells' injury.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28615347            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The aim of this study was to determine the influence of human rhinovirus on the genes involved in airway remodeling and to examine the impact of TSLP and contribution of oxidative stress on airway remodeling in the context of HRV infection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28545810            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TSLP-induced phosphorylation of l-plastin is increased in atopic dermatitis and increases eosinophil migration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27304220            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a hit expansion exercise yielded additional active compounds that could be amenable to further optimization, providing an opportunity to dissociate TSLP inhibition from other non-desired activities. This study illustrates the potential of phenotypic drug discovery to complement target based approaches by providing new chemistry and biology leads            \u003ca rel=\"nofollow\"\u003e             PMID:                        29320511            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study found that among patients with atopic dermatitis (AD), common FLG null mutations are associated with earlier AD onset in a dose-dependent manner, whereas TSLP rs1898671 appears unrelated to the timing of AD onset            \u003ca rel=\"nofollow\"\u003e             PMID:                        28479194            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            lactobacilli from the omnivorous group and all bifidobacteria significantly down-regulated IL-8. Notably, both genera also lowered the TSLP expression in stimulated Caco-2 cells, regardless of the diet regimen.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27863334            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this review focuses on recent advances on the effects of TSLP on obstetrical and gynecological diseases, including pregnancy failure, endometriosis, and cervical cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        27976427            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The increase in TSLP and TNF-alpha level observed in IS fluid was found to correlate with disease severity. The increased TSLP production from asthma sputum cells was abrogated by the addition of rIL-37. Regulation of TSLP pathway may be a therapeutic approach for asthma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27528425            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            House dust mite sublingual immunotherapy downregulated Th2-type immune responses mediated by the TSLP-OX40L signaling pathway in patients with persistent moderate to severe allergic rhinitis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27012942            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggest that IL-1beta may be an early key mediator for the acquisition of an Atopic dermatitis (AD) phenotype through induction of thymic stromal lymphopoietin (TSLP) and alteration of the epidermal homeostasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28191908            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            House dust mite exposure increases the expression of TSLP through PI3K\/Akt signaling pathway in human bronchial epithelial 16HBE cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28400057            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Posttranslational modifications control the functional activity of TSLP in humans and overproduction of TSLP may be a key trigger for the amplification of type 2 inflammation in diseases            \u003ca rel=\"nofollow\"\u003e             PMID:                        27744031            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study provides evidence for the hypothesis that TSLP could reflect the histological severity of lumbar disc degeneration (LDD), and TSLP-siRNA and TSLPR-siRNA could inhibit apoptosis of nucleus pulposus cells. The evident information obtained from the investigation could lead the way for new therapeutic approaches regarding LDD treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28746197            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            periostin-mediated TSLP production by keratinocytes directly stimulates cutaneous T-cell lymphoma (CTCL) tumor cell growth in addition to inducing a Th2-dominant tumor environment in CTCL.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27634769            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study shows that TSLP may be involved in the pathogenesis of asthma and rhinitis; dust mite and mugwort allergy could increase it significantly            \u003ca rel=\"nofollow\"\u003e             PMID:                        28303765            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum TSLP levels were significantly increased in systemic sclerosis patients compared to healthy donors, and were associated with a higher frequency of vasculopathy. The proportion of TSLP-positive dermal cells was increased in the skin of SSc patients compared with healthy donors, and was correlated with fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27429171            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study shows that NOD2 is an asthma-related factor that can promote cell proliferation and inflammatory response by mediated expression of TSLP in human airway smooth muscle cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        27889082            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the effects of TSLP on myeloid cells are crucial in reducing the multiple organ failure that is associated with systemic inflammation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26934097            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            interactions between TSLP in follicular dendritic cells and IgA production in tonsils may be an important mechanism contributing to the pathogenesis of Immunoglobulin A (IgA) nephropathy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27187742            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study demonstrated that naturally occurring severe infections by the most common respiratory viruses in hospitalized infants induce nasal airway secretion of TSLP, IL-33, and periostin when compared with healthy controls            \u003ca rel=\"nofollow\"\u003e             PMID:                        28471975            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Variations in FLG and TSLP genotype were associated with differences in self-reported skin clearance, TCI usage, and steroid usage.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27902816            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A possible role of TSLP in immune homeostasis in HIV infection:higher plasma TSLP was found in individuals with primary HIV infection compared to both chronic HIV infection and healthy controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27769179            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The polymorphism was further reproducibly associated with a DNA methylation signature in whole blood (P = 4.5x10-40) that also associated with allergic sensitization and expression in blood of the cytokine TSLP (P = 1.1x10-4). Knockdown of the transcription factor predicted to bind the enhancer region (NHLH1) in a human cell line (HEK293) expressing NHLH1 resulted in lower TSLP expression            \u003ca rel=\"nofollow\"\u003e             PMID:                        27149122            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TSLP level was significantly higher in asthmatic than in nonasthmatic children. TSLP level was significantly different between allergic asthmatic and nonallergic nonasthmatic groups.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26999524            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            While serum TSLP levels were unaffected by concomitant allergies and atopic comorbidities, serum levels of IL-31, IL-33 and sST2 were affected to a small extent. We found a positive correlation between TSLP, IL-31 and IL-33, and an inverse relationship between IL-33 and sST2            \u003ca rel=\"nofollow\"\u003e             PMID:                        27152943            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results showed that TSLP promoted the production of alpha-SMA and collagen I (P\u0026lt;0.001), suggesting that it can accelerate MRC-5 cell fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27385084            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TSLP is a key mediator in the pathogenesis of inflammatory bowel diseases and that further studies are needed to evaluate its role. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        27697608            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Letter: report decreased salivary gland TSLP expression in primary Sjogren's syndrome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27494755            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A novel mouse xenograft model to study the role of TSLP-induced CRLF2 signals in normal and malignant human B lymphopoiesis has been developed.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26611474            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Heat stress-induced HSPs can significantly reduce the production and secretion of TSLP from keratinocytes cultured under Th2 environment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26419317            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TSLP expression in the skin is mediated via RARgamma-RXR pathways.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26531761            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Epidermal thymic stromal lymphopoietin predicts the development of atopic dermatitis during infancy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26879860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study shows that specific food antigens can trigger innate immune mediated esophageal TSLP secretion            \u003ca rel=\"nofollow\"\u003e             PMID:                        26992000            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            production by monocyte-derived dendritic cells requires the integration of signals from dectin-1, the IL-1 receptor, and endoplasmic reticulum stress response stress signaling pathways            \u003ca rel=\"nofollow\"\u003e             PMID:                        26573878            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The association of TSLP polymorphism rs2289278 with atopic dermatitis (AD) was stronger in children with allergic sensitization than in children without atopy, and TSLP polymorphisms also increased the risk of asthma in children with AD            \u003ca rel=\"nofollow\"\u003e             PMID:                        26712523            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The positive feedback loop between TSLP, IL-33 and their receptors, and Th2 cytokines may facilitate Th2-skewed inflammation in eosinophilic CRSwNP.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26095319            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results show that rs1837253 polymorphism may be directly involved in the regulation of TSLP secretion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25515628            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Upon TSLP stimulation, the cells with the highest TSLPR expression level showed enhanced proliferation and JAK\/STAT-mediated gene regulation in a dose-dependent manner            \u003ca rel=\"nofollow\"\u003e             PMID:                        26652578            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Thymic stromal lymphopoietin activation of basophils in patients with allergic asthma is IL-3 dependent            \u003ca rel=\"nofollow\"\u003e             PMID:                        25962901            \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":43915035181281,"sku":"BL-2201NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLQ6AZGX2AACKGQMnUZs625_29cfced9-100e-4bc8-95df-204cdeee064b.jpg?v=1685851087"},{"product_id":"recombinant-mouse-5t4-protein-his-tag-bl-2202np","title":"Recombinant Mouse 5T4 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 Mouse Trophoblast Glycoprotein is produced by our Mammalian expression system and the target gene encoding Ser32-Ser361 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=\"Q9Z0L0\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/Q9Z0L0\/entry\"\u003eQ9Z0L0\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%;\"\u003eTPBG; 5T4; 5T4AG; M6P1; WAIF1\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%;\"\u003eTrophoblast glycoprotein, also known as TPBG and 5T4, it belongs to the LRR family of proteins. The C-terminus of LRR N-terminal cap (LRRNT) and LRR 1 are essential for the inhibition of the Wnt signaling pathway. TPBG may function as an inhibitor of Wnt\/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6 internalization. It expressed by all types of trophoblasts as early as 9 weeks of development. In adult tissues, the expression is limited to a few epithelial cell types but is found on a variety of carcinoma.\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%;\"\u003e36.6 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%;\"\u003e50-70 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":43915033936097,"sku":"BL-2202NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLQ6AZh6GAACLLtTd_sM445_6ca52a3c-da92-43ba-80bb-8cc33e68edbb.jpg?v=1685851043"},{"product_id":"recombinant-rhesus-macaque-gpc3-protein-his-tag-bl-2203np","title":"Recombinant Rhesus Macaque GPC3 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 Rhesus Macaque Glypican-3 is produced by our Mammalian expression system and the target gene encoding Gln25-His559 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=\"XP_005594665.1\" target=\"_blank\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/protein\/XP_005594665.1\"\u003eXP_005594665.1\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%;\"\u003eGlypican-3; GTR2-2; Intestinal protein OCI-5; MXR7; GPC3; OCI5\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%;\"\u003eGlypican-3\/GPC3 is a member of the glypican family. It belongs to the glypican family and is highly expressed in lung, liver, and kidney. It is a heparan sulfate proteoglycan, which is overexpressed in various neoplasms such as hepatocellular carcinoma, malignant melanoma, and testicular yolk sac tumor, and plays an important role in cell growth and differentiation. GPC3 function is tissue dependent. In some tissues, GPC3 acts as a tumor suppressor gene, whereas in others, it acts as an oncofetal protein. GPC3 is a reliable marker for hepatocellular carcinoma. The sensitivity and specificity exceeds both alpha-fetoprotein and hepatocyte-paraffin1. GPC3 immunohistochemistry can aid in the differentiation of testicular germ cell tumors, being expressed in all yolk sac tumors but not in seminomas. GPC3 expression has also been identified in some squamous cell carcinomas of the lung and clear cell carcinomas of the ovary. Glypican-3 is currently regarded as a tumor marker and potential target for immunotherapy.\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%;\"\u003e61.6 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%;\"\u003e38\u0026amp;65-120 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, 5% Trehalose, 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":43915037999329,"sku":"BL-2203NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLQ-AC15XAACVVd0amyw504_dc2ab752-3ce8-42df-bcd6-b3a4f1cd3e28.jpg?v=1685851165"},{"product_id":"recombinant-mouse-gpc3-protein-his-tag-bl-2204np","title":"Recombinant Mouse GPC3 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 Mouse Glypican-3 is produced by our Mammalian expression system and the target gene encoding Gln25-Met557 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=\"Q8CFZ4\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/Q8CFZ4\/entry\"\u003eQ8CFZ4\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%;\"\u003eGlypican-3; GTR2-2; Intestinal protein OCI-5; MXR7; GPC3; OCI5\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%;\"\u003eGlypican-3\/GPC3 is a member of the glypican family. It belongs to the glypican family and is highly expressed in lung, liver, and kidney. It is a heparan sulfate proteoglycan, which is overexpressed in various neoplasms such as hepatocellular carcinoma, malignant melanoma, and testicular yolk sac tumor, and plays an important role in cell growth and differentiation. GPC3 function is tissue dependent. In some tissues, GPC3 acts as a tumor suppressor gene, whereas in others, it acts as an oncofetal protein. GPC3 is a reliable marker for hepatocellular carcinoma. The sensitivity and specificity exceeds both alpha-fetoprotein and hepatocyte-paraffin1. GPC3 immunohistochemistry can aid in the differentiation of testicular germ cell tumors, being expressed in all yolk sac tumors but not in seminomas. GPC3 expression has also been identified in some squamous cell carcinomas of the lung and clear cell carcinomas of the ovary. Glypican-3 is currently regarded as a tumor marker and potential target for immunotherapy.\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%;\"\u003e61.6 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%;\"\u003e38\u0026amp;65-150 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, 5% Trehalose, 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":43915078729953,"sku":"BL-2204NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLQ-AV0n8AACVjnCrrCY564_6ba919af-fa61-427c-83f6-1317aac37267.jpg?v=1685852407"},{"product_id":"recombinant-cynomolgus-5t4-protein-his-tag-bl-2205np","title":"Recombinant Cynomolgus 5T4 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 Cynomolgus Trophoblast Glycoprotein is produced by our Mammalian expression system and the target gene encoding Thr35-Ser355 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%;\"\u003eQ4R8Y9\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%;\"\u003eTPBG; 5T4; 5T4AG; M6P1; WAIF1\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%;\"\u003eTrophoblast glycoprotein, also known as TPBG and 5T4, it belongs to the LRR family of proteins. The C-terminus of LRR N-terminal cap (LRRNT) and LRR 1 are essential for the inhibition of the Wnt signaling pathway. TPBG may function as an inhibitor of Wnt\/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6 internalization. It expressed by all types of trophoblasts as early as 9 weeks of development. In adult tissues, the expression is limited to a few epithelial cell types but is found on a variety of carcinoma.\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%;\"\u003e35.7 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%;\"\u003e55-80 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%;\"\u003eMay function as an inhibitor of Wnt\/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6 internalization.\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.\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            mcf:102132149           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca href=\"https:\/\/www.ncbi.nlm.nih.gov\/UniGene\/clust.cgi?ORG=Mfa\u0026amp;CID=1408\"\u003e            Mfa.1408           \u003c\/a\u003e \u003c\/p\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":43915036983521,"sku":"BL-2205NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLQ-AZIZpAACTLDuM2IA803_1df0aeef-801a-4c98-8d71-3076cba57cfb.jpg?v=1685851133"},{"product_id":"recombinant-human-erbb3-her3-protein-his-tag-bl-2207np","title":"Recombinant Human HER3 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 Receptor Tyrosine-Protein Kinase ErbB-3 is produced by our Mammalian expression system and the target gene encoding Ser20-Thr643 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%;\"\u003eP21860\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%;\"\u003eProto-oncogene-like protein c-ErbB-3; Tyrosine kinase-type cell surface receptor HER3; ERBB3; HER3\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%;\"\u003eReceptor tyrosine-protein kinase erbB-3 is an enzyme that in humans is encoded by the ERBB3 gene. This gene encodes a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. ERBB3 belongs to the protein kinase superfamily,tyr protein kinase family and EGF receptor subfamily.It contains 1 protein kinase domain and it is expressed in Epithelial tissues and brain. This membrane-bound protein has a neuregulin binding domain but not an active kinase domain. It therefore can bind this ligand but not convey the signal into the cell through protein phosphorylation. However, it does form heterodimers with other EGF receptor family members which do have kinase activity.\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%;\"\u003e69.5 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%;\"\u003e85-100 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%;\"\u003eSupplied as a 0.2 μm filtered solution of PBS, 50% Glycerol, 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%;\"\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%;\"\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%;\"\u003eTyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. May also be activated by CSPG5. Involved in the regulation of myeloid cell 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%;\"\u003e[Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 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%;\"\u003eProtein kinase superfamily, Tyr protein kinase family, EGF 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            3431           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            190151           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:2065           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000267101           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29413684            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            identified P2RX2, KCNQ5, ERBB3 and SOCS3 to be associated with the progression of age-related hearing impairment            \u003ca rel=\"nofollow\"\u003e             PMID:                        29325454            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results demonstrate that 4-PBA promotes gastric cancer cells migration through upregulation of HER3\/HER4 subsequent to increased levels of acetyl-histone and activation of ERK signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28851073            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR152 was found to be involved in the proliferation and metastasis of ovarian cancer cells through repression of ERBB3 expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29286064            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This phase Ib study was designed to determine the MTD, safety, preliminary efficacy, and pharmacokinetics of the HER3 (ErbB3) mAb SAR256212 in combination with the oral PI3K inhibitor SAR245408 for patients with metastatic or locally advanced solid tumors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28031425            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            To determine additional resistance mechanisms to cetuximab treatment besides HER3 signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28910149            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study shows ErbB3 expression was markedly decreased in suicide completers compared to controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28675388            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EGFR expression is increased in oesophageal and gastric adenocarcinomas after neoadjuvant therapy and was significantly associated with a prolonged overall survival in univariable analysis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29138285            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Using time-resolved-fluorescence energy transfer (TR-FRET), we demonstrated that in the presence of recombinant NRG1, binding of 9F7-F11 to HER3 is increased, whereas that of ligand-competing anti-HER3 antibodies (H4B-121, U3-1287, Ab#6, Mab205.10.2, and MOR09825) is decreased.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28507002            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study uncovers a direct relationship between HPV infection and HER3 in head and neck squamous cell carcinomas and provides a rationale for the clinical evaluation of targeted HER3 therapy for the treatment of HPV(+) patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27986750            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Cetuximab treatment induced HER3 activation and HER2\/HER3 dimerization in head and neck squamous cell carcinoma cell lines. Cetuximab induces HER3 expression and activation in HNSCC cell lines. Upregulation of HER3 by cetuximab is one mechanism underlying resistance to EGFR inhibition in HNSCC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27358485            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High HER3 expression is associated with breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27582551            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            hematopoietic expression of ERBB3 appears to be highest in bone marrow common myeloid and megakaryocyte-erythrocyte progenitors. Identified ERBB3 as a candidate gene for predisposition to erythroid MDS\/AML            \u003ca rel=\"nofollow\"\u003e             PMID:                        27416908            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High LINC00052 levels predict activation of HER3-mediated signaling, promoting breast cancer growth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28036286            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we show that ErbB3 interacts with the ESCRT-0 subunit Hrs both in the presence and absence of heregulin. This indicates an ESCRT-mediated sorting of ErbB3 to late endosomes and lysosomes, and in line with this we show that impaired ESCRT function leads to an endosomal accumulation of ErbB3.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28867611            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our findings provide support for an autocrine signaling loop engaged by oncogenic K-Ras involving ErbB3 that contributes to the dedifferentiation of the intestinal epithelium during tumor initiation and progression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27447549            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate the feasibility by using a pharmacophore of the small molecular compound VS1 for designing and optimization of proto-oncogene protein erbB-3 (ERBB3) inhibitors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27188722            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The A\/A genotype of the ERBB3 rs2292239 SNP is associated with risk for T1DM in a white Brazilian population.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29109006            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results shows that HER3 mRNA is upregulated in hepatocellular carcinoma associated to chronic HBV infection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27514687            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that afatinib resistant clones were selectively killed by knock down of ERBB3 + c-MET + c-KIT, but not by the individual or doublet knock down combinations, and the combination of afatinib with the SRC family inhibitor dasatinib killed afatinib resistant H1975 cells in a greater than additive fashion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26934000            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results suggest that the combination of a histone deacetylase inhibitor (HDACi) plus an anti-ErbB3 MoAb represents a viable strategy that warrants further evaluation for the treatment of non-small cell lung cancer (NSCLC) patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26862736            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            observations suggest that Rtn4A counteracts the Nrdp1-mediated degradation of ErbB3 by sequestering the ubiquitin ligase into ER tubules.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27353365            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Engineered multivalency enhanced affibody-mediated HER3 downregulation in multiple cancer cell types.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28248115            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Pretreatment with the soluble ErbB3 N418Q mutant suppressed heregulin beta1-induced HIF-1alpha activation in MCF7 cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25451255            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            review and meta-analysis of essential role in clinicopathology and prognosis of gastric cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        27536774            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HER3 is frequently overexpressed in high-grade dysplastic lesions of the gastroesophageal junction and may be a marker of invasive progression            \u003ca rel=\"nofollow\"\u003e             PMID:                        27559738            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the mechanistic regulation and linkage of the ROR1-HER3 and Hippo-YAP pathway in a cancer-specific context            \u003ca rel=\"nofollow\"\u003e             PMID:                        28114269            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Detecting nuclear ErbB380kDa could constitute a useful marker of prostate cancer progression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27191720            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            YAP induces the expression of epidermal growth factor (EGF) receptors (EGFR, ERBB3) and production of EGF-like ligands (HBEGF, NRG1 and NRG2); YAP induces the expression of epidermal growth factor (EGF) receptors (EGFR, ERBB3) and production of EGF-like ligands (HBEGF, NRG1 and NRG2)            \u003ca rel=\"nofollow\"\u003e             PMID:                        25798835            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In high-grade serous ovarian carcinoma (HGSC), high HER3 mRNA expression was a favorable prognostic factor for survival, while for high HER3 protein expression, a trend towards better survival was seen. A subgroup of HGSC with negative HER3 staining and negative HER3 mRNA levels showed most unfavorable survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27913862            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ERBB3 and ERBB4 have roles in lung adenocarcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        26254096            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results suggest that silibinin is a potential anti-cancer drug to inhibit proliferative and invasive characteristics of the epithelial ovarian cancer (EOC) cells that exhibit an autocrine heregulin (HRG)\/HER3 protein (HRG\/HER3) pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26482609            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings suggest that HBx promotes the progression of hepatocellular carcinoma by decreasing the stability of Nrdp1, which results in up-regulation of ErbB3            \u003ca rel=\"nofollow\"\u003e             PMID:                        26846102            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High HER3 expression in colon cancer was associated to distal colon location and low-grade tumor.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26863446            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Correlate ERBB3 gene SNPs with rheumatoid arthritis susceptibility.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25530448            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Nrdp1S is a tumour suppressor that which potentiates the Nrdp1-mediated ubiquitination and degradation of ErbB3. An Nrdp1S deficiency may also be an important factor in the loss of Nrdp1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26612725            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In response to trastuzumab, both HER3 and the metalloprotease ADAM10 are simultaneously upregulated. The proteolytic activity of the latter then releases the HER3 ligand heregulin from the cell surface to activate HER3 and confer resistance to trastuzumab by inducing compensatory growth factor receptor signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26863569            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the identification of HER3-V855A and its functional properties for the first time clearly implicates genomic HER3 activation in the pathogenesis of lung cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26689995            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data indicate that erbB3 signaling is critical for both trastuzumab and lapatinib resistances mainly through the PI-3K\/Akt pathway, whereas IGF-1R-initiated Src activation results in trastuzumab resistance without affecting lapatinib sensitivity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26621843            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that heat shock protein 90 (HSP90) inhibitor 17-DMAG caused loss of ret proto-oncogene protein (RET) and proto-oncogene protein erbB-3 (ERBB3) phosphorylation and lead to rapid cell death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26595521            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate the role of proto-oncogene protein erbB-3 (ErbB3) in hepatitis B virus X protein (HBx)-mediated cell survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26595522            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our results suggest that HER3 over-expression may be associated with worse overall survival in gastric cancers            \u003ca rel=\"nofollow\"\u003e             PMID:                        26517355            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study shows that ERBB3 is a novel regulator of beta-cell apoptosis and found rs2292239 strongly correlated with residual b-cell function and metabolic control in children with type 1 diabetes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26450151            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors show experimental evidence for an ErbB3 gain-of-function point mutation located in the C-lobe asymmetric dimerization interface, which shows enhanced phosphorylation at low ligand dose associated with increased kinase activity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26378253            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HER2\/HER3 interaction and increased expression was linked to risk for poor outcome in lung cancer patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26678909            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that cotreatment with anti-ERBB3 proto-oncogene protein antibody seribantumab and letrozole had increased antitumor activity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26310543            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HPV 16 E2 can modulate ErbB-3 by interacting with Nrdp-1, which is involved in the regulation of this receptor, via ubiquitination and degradation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26963794            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings show that the local 3D tumor microenvironment can trigger reprograming and switching of ErbB family members and thereby influence ErbB3-driven tumor growth            \u003ca rel=\"nofollow\"\u003e             PMID:                        26073080            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ERa-dependent expression of LRIG1 dampens ErbB3 signaling in luminal breast cancer cells, and by blocking ERa activity with fulvestrant, LRIG1 is decreased thus permitting ErbB3 accumulation, enhanced ErbB3 signaling to cell survival pathways            \u003ca rel=\"nofollow\"\u003e             PMID:                        26148232            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that clathrin-mediated endocytosis of proto-oncogene protein erbB-3 (ErbB3) is depending on epsin-1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26975582            \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":43915024236769,"sku":"BL-2207NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLQ-AV-s3AACJwZJDAUk749_5997f9cc-5e81-425b-aa0f-b671f0b08df6.jpg?v=1685850795"},{"product_id":"recombinant-cynomolgus-bcma-protein-his-tag-bl-2210np","title":"Recombinant Cynomolgus BCMA 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 Cynomolgus B-cell maturation protein is produced by our Mammalian expression system and the target gene encoding Met1-Ala53 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=\"G7Q0I4\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/G7Q0I4\/entry\"\u003eG7Q0I4\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 17; B-cell maturation protein; CD269; Tnfrsf17; Bcm; Bcma\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%;\"\u003eB cell maturation antigen (BCMA) is a member of the TNF receptor superfamily. It has been designated TNFRSF17. BCMA is a type III membrane protein containing one extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs and mature B cell lines. Although some expression has been observed at the cell surface, BCMA appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells. This data suggests that BCMA may play an important role in B cell development,function and regulation.\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 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\u0026amp;15-20 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 50 mM Tris-HCl, 100 mM Glycine, 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 0.1 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","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915043635425,"sku":"BL-2210NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLRGAQNsvAACKv4Pr2pQ602_cd36a8d8-1264-40bf-9050-0dadc3532be6.jpg?v=1685851336"},{"product_id":"recombinant-human-tpbg-protein-fc-tag-bl-2215np","title":"Recombinant Human TPBG Protein (C-mFc)","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 Trophoblast glycoprotein is produced by our Mammalian expression system and the target gene encoding Ser32-Ser355 is expressed with a mouse 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%;\"\u003eQ13641\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%;\"\u003e5T4 Protein; 5T4AG Protein; M6P1 Protein; WAIF1 Protein; TPBG\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%;\"\u003eTrophoblast glycoprotein, also known as TPBG and 5T4, it belongs to the LRR family of proteins. The C-terminus of LRR N-terminal cap (LRRNT) and LRR 1 are essential for the inhibition of the Wnt signaling pathway. TPBG may function as an inhibitor of Wnt\/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6 internalization. It expressed by all types of trophoblasts as early as 9 weeks of development. In adult tissues, the expression is limited to a few epithelial cell types but is found on a variety of carcinoma.\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%;\"\u003e61.7 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%;\"\u003e80-110 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%;\"\u003eMay function as an inhibitor of Wnt\/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6 internalization.\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.\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            12004           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            190920           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:7162           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000358765           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28481180            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Collectively, these findings demonstrate that an anti-5T4 antibody-drug conjugate reduces the fraction of cancer stem cells (CSC), and prevents local recurrence and suggest a novel therapeutic approach for patients with head and neck squamous cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27780858            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We obtained GWS evidence (P \u0026lt; 2.7 x 10(-6)) for gene-based association in the total sample with a novel locus, TPBG (P = 1.8 x 10(-6)).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28183528            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In conclusion, the present study provided evidence that TPBG is involved in PDAC metastasis, and that TPBG and its associated signaling pathways may be a suitable target for pancreatic ductal adenocarcinoma therapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25738465            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            5T4 expression is mechanistically associated with the directional movement of cells through epithelial mesenchymal transition, facilitation of CXCL12\/CXCR4 chemotaxis, blocking of canonical Wnt\/beta-catenin while favouring non-canonical pathway signalling            \u003ca rel=\"nofollow\"\u003e             PMID:                        25066861            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Tyrosine 325 plus the leucine-rich repeat 1 surface centered on a second exposed aromatic residue, phenylalanine 97, are essential for inhibition of Wnt\/beta-catenin signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24582434            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The surface expression of 5T4 marks the use of the CXCR4 rather than the CXCR7 receptor, with distinct consequences for CXCL12 exposure.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22956548            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            5T4 is a potential new antigen for targeted therapies such as immunotherapy in MPM, as it is overexpressed on mesothelioma cells and recognised by 5T4-specific cytotoxic T-cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22498111            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Glycosylation and epitope mapping of the 5T4 glycoprotein oncofoetal antigen            \u003ca rel=\"nofollow\"\u003e             PMID:                        11903056            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results sugest that 5T4 is a transient marker of human embryonic stem cell differentiation \u0026amp; that 5T4 phenotype, colony seeding density and culture conditions influence the maintenance of pluripotent hES cells and their differentiation to neural lineages.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16616918            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            there is a repertoire of CD8 T cell recognition of 5T4 in normal human donors and some candidate HLA-A*0201 epitopes have been identified            \u003ca rel=\"nofollow\"\u003e             PMID:                        16646078            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the mRNA expression of trophoblast glycoprotein is up-regulated in cells circulating within blood from women with preeclampsia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17978129            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            5T4-based cancer vaccine: cytotoxic T lymphocyte epitopes identified in Trovax-vaccinated colorectal cancer patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        18567615            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            colorectal cancer patients who had preexisting cell proliferative responses to 5T4 were longer-term survivors            \u003ca rel=\"nofollow\"\u003e             PMID:                        18833005            \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":43915079254241,"sku":"BL-2215NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLROAItUaAAB90e-3tbc062_72367159-64bf-4e09-a005-5367325960dd.jpg?v=1685852422"},{"product_id":"recombinant-cynomolgus-nectin-4-protein-his-tag-bl-2216np","title":"Recombinant Cynomolgus Nectin-4 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 Cynomolgus Poliovirus Receptor-Related Protein  4 is produced by our Mammalian expression system and the target gene encoding Gly32-Ser349 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=\"L0N6D9\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/L0N6D9\/entry\"\u003eL0N6D9\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%;\"\u003ePVRL4; Nectin-4; Ig superfamily receptor LNIR; Poliovirus receptor-related protein 4; PRR4; LNIR\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%;\"\u003eNectin-4 (PVRL4) is a type I transmembrane glycoprotein which belongs to the nectin family of Ig superfamily proteins. It contains two Ig-like C2-type domains and one Ig-like V-type domain. PVRL4 seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with nectin-1. It does not act as receptor for alpha-herpesvirus entry into cells. It is predominantly expressed in placenta, the embryo and breast carcinoma. But it is not detected in normal breast epithelium. The soluble form is produced by proteolytic cleavage at the cell surface (shedding), probably by ADAM17. Mutations in this gene are the cause of ectodermal dysplasia-syndactyly syndrome type 1, an autosomal recessive disorder.\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%;\"\u003e34.9 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%;\"\u003e38-50 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","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915047862497,"sku":"BL-2216NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLRSAbZ1MAACO0as6Aps897_16d6a0a9-27ae-4d85-952a-ded5db51c2f6.jpg?v=1685851487"},{"product_id":"recombinant-human-axl-protein-his-tag-bl-2218np","title":"Recombinant Human AXL 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 Tyrosine-protein kinase receptor UFO is produced by our Mammalian expression system and the target gene encoding Ala26-Pro440 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%;\"\u003eAAA61243\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%;\"\u003eTyrosine-protein kinase receptor UFO; AXL oncogene; UFO\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%;\"\u003eAxl, also known as Ufo and Ark, is a widely expressed 140 kDa glycoprotein in the TAM receptor tyrosine kinase family. Axl binds the vitamin K-dependent protein Gas6 which triggers tyrosine autophosphorylation of the Axl cytoplasmic domain. Axl functions in dampening the immune response, regulating cytokine secretion, clearing apoptotic cells and debris, and maintaining cell survival. Axl is highly expressed in solid cancers and promotes in vivo tumorigenesis and tumor cell invasiveness. It also functions as a cellular entry receptor for Gas6-opsonized lentiviruses. Axl contributes to cell survival, migration, invasion, metastasis and chemosensitivity justify further investigation of Axl as novel therapeutic targets in cancer. The receptor tyrosine kinase AXL is thought to play a role in metastasis. The soluble AXL receptor as a therapeutic candidate agent for treatment of metastatic ovarian cancer. GAS6\/AXL targeting as an effective strategy for inhibition of metastatic tumor progression in vivo.\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%;\"\u003e45.6 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%;\"\u003e60-90 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 \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%;\"\u003eReceptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, AXL binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TNS2. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6\/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response.; (Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope.; (Microbial infection) Acts as a receptor for Ebolavirus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope.\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.\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, Tyr protein kinase family, AXL\/UFO 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            905           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            109135           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:558           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000301178           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30176265            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Findings suggest that METTL3 plays very important oncogenic roles in ovarian carcinoma development and\/or aggressiveness by stimulating AXL translation and EMT.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30249526            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Co-expression of CDCP1 and AXL is often observed in EGFR-mutation-positive tumors, limiting the efficacy of EGFR TKIs. Co-treatment with EGFR TKI and TPX-0005 warrants testing.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29433983            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrates that motility behavior of AXL-expressing tumor cells can be elicited by Gas6-bearing apoptotic bodies generated from tumor treatment with therapeutics that produce killing of a portion of the tumor cells present but not all, hence generating potentially problematic invasive and metastatic behavior of the surviving tumor cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        28923840            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that average methylation in AXL at birth was associated with higher risk for asthma-related phenotypes in childhood, especially wheezing. The effects of average AXL methylation on wheezing symptoms were magnified in girls compared to boys.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29177020            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we identified YAP-driven AXL overexpression as a mechanism of resistance to EGFR TKIs in lung cancer cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29136529            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The anti-angiogenic effect of luteolin may be associated with the inhibition of the Gas6\/Axl pathway and its downstream phosphatidylinositol 3-kinase (PI3K)\/protein kinase B (Akt)\/mammalian target of rapamycin (mTOR) signaling pathways.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28627676            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            AXL is influenced by p53 status and could cause the emergence of aggressive clones after exposure to chemotherapy in colon and breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        28596680            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Taken together, these findings suggest that AXL most likely serves as an attachment factor for Zika virus on the cell surface, and that productive infection requires endocytosis and delivery of the virus to acidified intracellular compartments.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29574335            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            serum Axl shows high diagnostic accuracy at early stage hepatocellular carcinoma as well as cirrhosis            \u003ca rel=\"nofollow\"\u003e             PMID:                        28526812            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            AXL is the only relevant Zika virus entry cofactor expressed on fetal endothelial cells, and that when produced in mammalian cells, only Zika virus, but not West Nile virus or dengue virus, can use AXL, because it more efficiently binds Gas6.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28167751            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate AXL receptor tyrosine kinase (AXL) as an important mediator of docetaxel resistance in prostate cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28455956            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            AXL promotes epithelial cell efferocytosis in a tyrosine kinase-dependent manner.AXL role in AKT-dependent drug resistance.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28184013            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The plasma concentrations of Gas6 and Axl are lowered in rheumatoid arthritis patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24702788            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The anti-AXL antibody 20G7-D9 represents a promising therapeutic strategy in triple-negative breast cancer with mesenchymal features by inhibiting AXL-dependent Epithelial-Mesenchymal Transition, tumor growth, and metastasis formation            \u003ca rel=\"nofollow\"\u003e             PMID:                        27923843            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Suppression of AXL by shRNA and inhibitor prolonged survival of chronic myelogenous leukemia (CML) mice and reduced the growth of leukemia stem cells ( LSCs) in mice. Gas6\/AXL ligation stabilizes beta-catenin in an AKT-dependent fashion in human CML CD34(+) cells. Our findings improve the understanding of LSC regulation and validate Gas6\/AXL as a pair of therapeutic targets to eliminate CML LSCs            \u003ca rel=\"nofollow\"\u003e             PMID:                        27852702            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our data point to a targetable Axl-PI3 kinase-PD-L1 axis that is highly associated with radiation resistance            \u003ca rel=\"nofollow\"\u003e             PMID:                        28476872            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            AXL+ and GAS6+ expression is relevant to a poor prognosis in resected lung adenocarcinoma (AD)patients at stage I. AXL\/GAS6 might serve as crucial predictive and prognostic biomarkers and targets to identify individuals at high risk of post-operative death.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28440492            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            report that Axl regulates FGFR signaling via complex formation with FGFR3            \u003ca rel=\"nofollow\"\u003e             PMID:                        26598018            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            AZD7762 inhibits the proliferative\/metastatic activity of breast cancer cells through the suppression of cellular AXL signaling events including anti-apoptosis, migration, invasion, and angiogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27829217            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BGB324 does not inhibit BCR-ABL1 and consequently inhibits chronic myeloid leukemia (CML)independent of BCR-ABL1 mutational status. Our data show that Axl inhibition has therapeutic potential in BCR-ABL TKI-sensitive as well as -resistant CML and support the need for clinical trials            \u003ca rel=\"nofollow\"\u003e             PMID:                        27856601            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show that AXL is upregulated in endometrial cancer tissues and indicate that AXL promotes invasion and migration of endometrial cancer cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27764792            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these results suggest that HOTAIR promotes renal cell carcinoma (Rcc) tumorigenesis via miR-217\/HIF-1alpha\/AXL signaling, which may provide a new target for the diagnosis and therapy of Rcc disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28492542            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The expression of MerTK and AxlTK varied according to the deposition of immunoglobulin and complements on glomeruli. Both MerTK and AxlTK expressions were increased on glomeruli and varied according to pathological classifications.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28127639            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression level of AXL is associated with lung adenocarcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26942465            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            AXL is a strong adverse prognostic factor for esophageal squamous cell carcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        27172793            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our data demonstrate that AXL is a crucial therapeutic target of carvacrol-induced inhibition of NSCLC cell proliferation and migration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29277784            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results show that TYRO3, AXL and GAS6 are expressed at higher levels in LMS and expression of its ligands correlates to a worse PFS in LMS patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29024938            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-34a reconstitution in DMPM cells significantly inhibited proliferation and tumorigenicity, induced an apoptotic response, and declined invasion ability, mainly through the down-regulation of c-MET and AXL and the interference with the activation of downstream signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28100259            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            kinase AXL drives the mesenchymal gene signature and motility of ovarian tumor cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27703029            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The AXL inhibitor R428 attenuated RTK and ERK activation and reduced cell motility in Mes cells in culture and reduced tumor growth            \u003ca rel=\"nofollow\"\u003e             PMID:                        27703030            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results highlight the dual role of Axl during Zika virus infection of glial cells: promoting viral entry and modulating innate immune responses.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28076778            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The expression of AXL was positively associated with GAS6 expression (P \u0026lt; 0.001), and tumor differentiation (P = 0.014) in advanced NSCLC with metastases. AXL expression displayed no association with gender, age, smoking history, pathology, T stage, N stage, CEA, and LDH.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28551766            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate a role for AXL receptor tyrosine kinase (AXL) in regulating the nuclear translocation of epidermal growth factor receptor (EGFR) and suggest that AXL-mediated SRC family kinases (SFKs) and neuregulin-1 (NRG1) expression promote this process.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28049763            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Combination of high serum levels of soluble AXL and BNP had greater predictive value for heart failure than BNP alone.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27718443            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results demonstrate that Gas6\/Axl axis confers aggressiveness in breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27279912            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a lower stability and greater dynamic nature of the Axl kinase domain            \u003ca rel=\"nofollow\"\u003e             PMID:                        28724631            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Silencing AXL or the inhibition of AXL kinase activity significantly inhibits tumor cell migration and invasion in colorectal cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28727830            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we identify PROS1 as a driver of Oral Squamous Cell Carcinoma tumor growth and a modulator of AXL expression            \u003ca rel=\"nofollow\"\u003e             PMID:                        28118606            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studies indicate that aberrant AXL receptor tyrosine kinase (AXL) signaling and development of an epithelial-to-mesenchymal transition (EMT) phenotype underlie resistance of anaplastic lymphoma kinase (ALK F1174L)-driven neuroblastoma (NB) cells to TAE684 and its derivatives.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26616860            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studied axl kinase as a negative regulator of an alveolar epithelial cell phenotype; results found that inhibition of Axl kinase could form epithelial adhesion structure and augment surfactant protein production via the MET of human lung multi-potent cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28553934            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            AXL is efficiently and sequentially cleaved by alpha- and gamma-secretases in various types of cancer cell lines.  The AXL intracellular domain cleavage product translocates into the nucleus via a nuclear localization sequence that harbored a basic HRRKK motif.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28034848            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a relationship between AXL and the cellular response to DNA damage whereby abrogation of AXL signaling leads to accumulation of the DNA-damage markers gammaH2AX, 53BP1, and RAD51.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27893463            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Small molecule and antibody inhibitors of AXL and MER have recently been described, and some of these have already entered clinical trials. The optimal design of treatment strategies to maximize the clinical benefit of these AXL and MER targeting agents are discussed in relation to the different cancer types and the types of resistance encountered.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28251492            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our results demonstrate that AR can promote melanoma metastasis via altering the miRNA-539-3p\/USP13\/MITF\/AXL signal and targeting this newly identified signal with AR degradation enhancer ASC-J9 may help us to better suppress the melanoma metastasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27869170            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            AXL can be an effective therapeutic target in combination with targeted therapy such as PARP inhibitors in several different malignancies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27671334            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            AXL\/TAZ\/YAP expression is associated with poor prognosis in male breast cancer patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27987320            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ablation of AXL has no effect on ZIKA virus (ZIKV) entry or ZIKV-mediated cell death in human induced pluripotent stem cell (iPSC)-derived NPCs or cerebral organoids.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27912091            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the candidate viral entry receptor AXL is highly expressed by human radial glial cells, astrocytes, endothelial cells, and microglia in developing human cortex and by progenitor cells in developing retina.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27038591            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Coexistence of vimentin-positive and Axl-high expression is a poor prognostic factor for primary breast cancer. Vimentin and Axl expression might contribute to the aggressive phenotype in breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27506606            \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":43915055628513,"sku":"BL-2218NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLRSANo8aAACEGUxfaik091_396cd9c8-9c32-4de3-aa3a-70ea5836264a.jpg?v=1685851761"},{"product_id":"recombinant-rhesus-macaque-slamf7-protein-his-tag-bl-2221np","title":"Recombinant Rhesus Macaque SLAMF7 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 Rhesus Macaque SLAM Family Member 7 is produced by our Mammalian expression system and the target gene encoding Ser23-Met226 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=\"F7HQ72\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/F7HQ72\/entry\"\u003eF7HQ72\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%;\"\u003eSLAM Family Member 7; CD2 Subset 1; CD2-Like Receptor-Activating Cytotoxic Cells; CRACC; Membrane Protein FOAP-12; Novel Ly9; Protein 19A; CD319; SLAMF7; CS1\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%;\"\u003eSLAMF7 is a single-pass type I membrane protein and contains 1 Ig-like C2-type (immunoglobulin-like) domain. SLAMF7 is expressed in NK cells, activated B-cells, NK-cell line but not in promyelocytic, B-cell lines, or T-cell lines. Although the cytoplasmic domain of CS1 contains immunoreceptor tyrosine-based switch motifs (ITSM), which enables to recruite signaling lymphocyte activation molecule (SLAM)-associated protein (SAP\/SH2D1A), it activates NK cells in the absence of a functional SAP. SLAMF7 positively regulated natural killer cell functions by a mechanism dependent on the adaptor EAT-2 but not the related adaptor SAP. However, in the absence of EAT-2, CRACC potently inhibited natural killer cell function. It was also inhibitory in T cells, which are typically devoid of EAT-2. Thus, SLAMF7 can exert activating or inhibitory influences on cells of the immune system depending on cellular context and the availability of effector 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%;\"\u003e23.3 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%;\"\u003e30-50 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":43915092361441,"sku":"BL-2221NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLRWAMR4cAACQLWDhiAc611_8da6dab9-a0d0-4b66-93ad-c9d54137a862.jpg?v=1685852934"},{"product_id":"recombinant-mouse-axl-protein-his-tag-bl-2222np","title":"Recombinant Mouse AXL 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 Mouse Tyrosine-protein kinase receptor UFO is produced by our Mammalian expression system and the target gene encoding Ala19-Pro443 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=\"Q00993\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/Q00993\/entry\"\u003eQ00993\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%;\"\u003eTyrosine-protein kinase receptor UFO; AXL oncogene; UFO\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%;\"\u003eAxl, also known as Ufo and Ark, is a widely expressed 140 kDa glycoprotein in the TAM receptor tyrosine kinase family. Axl binds the vitamin K-dependent protein Gas6 which triggers tyrosine autophosphorylation of the Axl cytoplasmic domain. Axl functions in dampening the immune response, regulating cytokine secretion, clearing apoptotic cells and debris, and maintaining cell survival. Axl is highly expressed in solid cancers and promotes in vivo tumorigenesis and tumor cell invasiveness. It also functions as a cellular entry receptor for Gas6-opsonized lentiviruses. Axl contributes to cell survival, migration, invasion, metastasis and chemosensitivity justify further investigation of Axl as novel therapeutic targets in cancer. The receptor tyrosine kinase AXL is thought to play a role in metastasis. The soluble AXL receptor as a therapeutic candidate agent for treatment of metastatic ovarian cancer. GAS6\/AXL targeting as an effective strategy for inhibition of metastatic tumor progression in vivo.\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%;\"\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 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":43915069489377,"sku":"BL-2222NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLRWAKBXFAACKWoMIgyI438_995fec40-0fb2-4fea-be88-b4e10253062a.jpg?v=1685852144"},{"product_id":"recombinant-human-baffr-protein-fc-tag-bl-2228np","title":"Recombinant Human BAFFR 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 Tumor Necrosis Factor Receptor Superfamily Member 13C is produced by our Mammalian expression system and the target gene encoding Ser7-Ala71 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%;\"\u003eQ96RJ3\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%;\"\u003eBAFF R; BAFFR; BR3; CD268; TNFRSF13C\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 13C (TNFRSF13C) also known as B-cell-activating factor receptor (BAFFR) and CD268 antigen, is a member of the tumor necrosis factor receptor superfamily. BAFF promotes the survival of B cells and is essential for B cell maturation. BAFF binds to three TNF receptor superfamily members: B-cell maturation antigen (BCMA\/TNFRSF17), transmembrane activator and calcium-modulator and cyclophilin ligand interactor (TACI\/TNFRSF13B) and BAFF receptor (BAFF R\/BR3\/TNFRSF13C). These receptors are type III transmembrane proteins that lack a signal peptide. BAFF R is highly expressed in spleen, lymph node and resting B cells. It is also expressed at lower levels in activated B cell, in resting CD4+ T cells, in thymus and peripheral blood leukocytes. BAFF knockout mice lack mature B cells. Similarly, A\/WySnJ mice that are defective in BAFF-R intracellular signaling also lack mature B cells, suggesting that BAFF R is the critical receptor for BAFF during B lymphopoiesis. It has been proposed that abnormally high levels of BAFFR\/TNFRSF13C (CD268) may contribute to the pathogenesis of autoimmune diseases by enhancing the survival of autoreactive B cells.\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%;\"\u003e33.4 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%;\"\u003e38-58 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 \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%;\"\u003eB-cell receptor specific for TNFSF13B\/TALL1\/BAFF\/BLyS. Promotes the survival of mature B-cells and the B-cell response.\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%;\"\u003eMembrane; Single-pass type III membrane protein.\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            17755           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            606269           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:115650           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000291232           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        27436754            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Expression patterns of BAFF and its receptor BAFF-R differ according to lupus nephritis class.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29087261            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            up-regulated expression in intractable temporal lobe epilepsy            \u003ca rel=\"nofollow\"\u003e             PMID:                        28441631            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Inhibition of ADAM10 augments BAFF-dependent survival of primary human B cells, whereas inhibition of ADAM17 increases BAFFR expression levels.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28249164            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Relationships between serum BAFF and BBR expression [(BAFFR, calcium signal modulating cyclophilic ligand interactor (TACI) and B cell maturation antigen (BCMA)] were determined on B cell subsets, defined using immunoglobulin (Ig)D\/CD38. Twenty pre-RTX and 18 rheumatoid arthritis patients relapsing after B cell depletion were included.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28800164            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Among the BAFF receptors in a cohort of rheumatoid arthritis (RA) patients, the AA have shown, by fluorescence activated cell sorter (FACS) analysis of median fluorescence intensity (MFI), that transmembrane activator and calcium-modulating cyclophilin ligand interactor (TACI) and B cell maturation antigen (BCMA) do not change            \u003ca rel=\"nofollow\"\u003e             PMID:                        28834574            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The expression levels of serum BAFF and the three receptors (TACI, BCMA and BAFF-R) in non-Hodgkin lymphoma patients were significantly higher than in healthy controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28028945            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Variants in BAFF-R gene is associated with chronic lymphocytic leukemia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27468724            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF-R, as the principal receptor of BAFF, not only decreased the apoptosis of B cells and CD8+ T cells by upregulating the expression of Bcl-2 and BclxL, but also promoted B-cell proliferation in immune thrombocytopenia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26749059            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            genetic polymorphism contributes to the pathogenesis of primary antibody deficiency            \u003ca rel=\"nofollow\"\u003e             PMID:                        26613719            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF and BAFF-R are expressed in the thyrocytes derived from patients with either autoimmune thyroid disorders or multinodular goiter, as well in the infiltrating immune cells of Graves' disease and Hashimoto's thyroiditis            \u003ca rel=\"nofollow\"\u003e             PMID:                        26214745            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There is an increased prevalence of the BAFF-R His159Tyr mutation in patients with Sjogren's syndrome (SS), particularly in those with SS complicated by MALT lymphoma whose disease onset occurred at a younger age.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26097183            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of mutant caspase-9 correlated with a downregulation of BAFFR (B-cell-activating factor belonging to the TNF family (BAFF) receptor) in B cells and ICOS (inducible T-cell costimulator) in T cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25569260            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Variants of TNFRSF13C were associated with common variable immunodeficiency.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26122175            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Negative expression of BAFF-R, but not of BAFF, could be an independent risk factor for progression-free survival and Overall survival in patients with diffuse large B-cell lymphoma treated with standard R-CHOP.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26327569            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the common TLR4-D299G, TLR4-T399I and BAFFR-P21R polymorphisms provide the carriers with a protective advantage against ICU-acquired sepsis; this finding was more profound for medical patients compared to trauma or surgical ones            \u003ca rel=\"nofollow\"\u003e             PMID:                        25454804            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show significant differences in expression of tumour necrosis factor family (BAFF) receptors BAFF-R, BCMA and TACI in patients with and without anti-Jo-1 or anti-Ro52\/anti-Ro60 autoantibodies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25301447            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In view of the restricted expression of the BAFF-R on normal cells and the multiple anti-pre-B ALL activities stimulated by this antibody, a further examination of its use for treatment of pre-B ALL is warranted.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24825858            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Availability of BAFF determines BAFF-R and TACI expression on B cells in common variable immunodeficiency.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24809296            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our study demonstrates that BR3 is involved in the survival of cultured epithelial cells due to an autocrine effect of BAFF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24602383            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF-R, but not BAFF, may have a role in progression-free survival and overall survival in follicular lymphoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        23272079            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BLyS and its receptors are expressed by B lymphocytes in the peripheral blood and the bone marrow of patients with multiple myeloma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23276925            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            P21R\/H159Y TNFRSF13C compound heterozygous mutation and P21R heterozygous mutations were detected in Turkish patients with common variable immunodeficiency.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22699762            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF-R expression is tightly regulated during B-cell development in mouse and human and this exprssion is correlated with posirive selection.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22028296            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            It was also found that NF-kappaB was an important transcription factor involved in regulating BAFF-R expression through one NF-kappaB binding site in the BAFF-R promoter            \u003ca rel=\"nofollow\"\u003e             PMID:                        21607696            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Soluble BAFF levels inversely correlate with peripheral B cell numbers and the expression of BAFF receptors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22124120            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The activation profile of diffuse large B-cell lymphomas\/posttransplantation lymphoproliferative disorders was not associated with BAFF\/BAFF-R expression, whereas nuclear p52 activation might be linked to Epstein-Barr virus.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21871426            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The human BAFF-R gene might be regulated via a transcriptional event through one putative NF-kappaB site on the BAFF-R gene promoter.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21744373            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            reduced expression via inhibition of the NF-KappaB pathway in B cells of rheumatoid arthritis patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        21515993            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            primary leukemia B-cell precursors aberrantly express receptors of the BAFF-system, BAFF-R, BCMA, and TACI            \u003ca rel=\"nofollow\"\u003e             PMID:                        21687682            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This is the first study, presenting together the TNFSF members APRIL, BAFF, TWEAK and their receptors in different areas of normal renal tissue and renal cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21483105            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BLyS and its receptors might have a potential role in the growth and survival of malignant plasma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19731825            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results describe the mechanisms underlying aberrant BAFF-R expression in precursor B acute lymphoblastic leukemia (precursor B-ALL) and mature B chronic lymphocytic leukemia (CLL).            \u003ca rel=\"nofollow\"\u003e             PMID:                        21099364            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF-R was rather specifically related to low growth activity of germinal center B-cell-like -type diffuse large B-cell lymphoma of nodal origin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21123970            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            inverse correlation between BAFF and APRIL in Kawasaki disease is reversed by IVIG treatment            \u003ca rel=\"nofollow\"\u003e             PMID:                        20945608            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Elevated plasma BAFF and reduced BAFF receptor 3 (BR3) protein expression on peripheral B cells could act as biomarkers for active disease in systemic lupus erythematosus patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        20974656            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a novel lymphoma-associated mutation in human BAFF-R that results in NF-kappaB activation and reveals TRAF6 as a necessary component of normal BAFF-R signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21041452            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data from BAFF-R-expressing cells suggested potential regulatory sites in TNFRSF13C promoter region.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20554963            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This report is the first showing universal expression of BAFF-R by pre-B ALL cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20460528            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            IFN-gamma and the NF-kappaB pathway could be involved in regulating the transcription and mRNA expression of BAFF-R gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20230666            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the mechanism of transcriptional regulation of BAFF-R            \u003ca rel=\"nofollow\"\u003e             PMID:                        20025535            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF-R is a receptor for the TNF family member ligand, BAFF [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        12456020            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFFR-mediated NF-kappa B activation and IL-10 production in B cells is downregulated by TNFR-associated factor-3.            \u003ca rel=\"nofollow\"\u003e             PMID:                        12471121            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            crystal structure and interaction with BAFF protein            \u003ca rel=\"nofollow\"\u003e             PMID:                        12715002            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF\/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site.            \u003ca rel=\"nofollow\"\u003e             PMID:                        12755599            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of BCMA, TACI, and BAFF-R by multiple myeloma cells support cell growth and survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        14512299            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study reports the crystal structure of a 24-residue fragment of the cytoplasmic portion of BAFF-R bound in complex with TRAF3.            \u003ca rel=\"nofollow\"\u003e             PMID:                        15585864            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the PVPAT sequence of BAFFR not only functions as a key signaling motif of BAFFR but also determines its signaling specificity in the induction of the noncanonical NF-kappaB pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        15644327            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            amino acid sequence of genomic DNA from blood of common variable immunodeficiency patients;mutations may result in humoral immunodeficiency            \u003ca rel=\"nofollow\"\u003e             PMID:                        16160919            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF-R is expressed on most mature B cells and B-cell lymphoproliferative disorders.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16226112            \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":43915058675937,"sku":"BL-2228NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLRWAE2jNAACZo_RFEJ0036_359146cc-3be5-4676-b98b-b18b87fd1d96.jpg?v=1685851863"},{"product_id":"recombinant-human-carbonic-anhydrase-9-protein-his-tag-bl-2229np","title":"Recombinant Human Carbonic Anhydrase 9 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 Carbonic Anhydrase 9 is produced by our Mammalian expression system and the target gene encoding Gln38-Asp414 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%;\"\u003eQ16790\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%;\"\u003eCA9; CA-IX; Carbonic Anhydrase IX; Carbonate dehydratase IX; G250; MN; P54\/58N; RCC; RCC-associated protein G250\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%;\"\u003eCarbonic anhydrases IX (CA IX), also known as membrane antigen MN or CA9, is a member of the carbonic anhydrase (CA) family and may be involved in cell proliferation and cellular transformation. CAs are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide (H2O + CO2 = H+ + HCO3–) and thus participate in a variety of biological and physical processes. CA9 is a transmembrane enzyme expressed primarily in carcinoma cells. It is one of the best markers for hypoxia and for RCC. Appears to be a novel specific biomarker for a cervical neoplasia.\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 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%;\"\u003e45-60 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%;\"\u003eReversible hydration of carbon dioxide. Participates in pH regulation. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia.\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. Nucleus, nucleolus. Cell membrane; Single-pass type I membrane protein. Cell projection, microvillus membrane; Single-pass type I membrane protein. Note=Found on the surface microvilli and in the nucleus, particularly in nucleolus.\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%;\"\u003eAlpha-carbonic anhydrase 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            1383           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            603179           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:768           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000367608           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29952031            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Our results do not suggest a prognostic role for CA IX overexpression in stage III non-small cell lung cancer patients who received neoadjuvant treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30029935            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FZD1 and CAIX might be important biological markers for the carcinogenesis, metastasis, invasion, and prognosis of pancreatic ductal adenocarcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        28921449            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression of CA9 is associated with breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29893327            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that the conformational flexibility may have several important roles in tumour progression, facilitating interactions of carbonic anhydrase IX (hCA IX) with partner proteins assisting tumour spreading and progression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29564477            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the findings of this study establish the SOX9\/CA9-mediated oncogenic pathway in glioma, the inhibition of which enhances the sensitivity of glioma cells to Temozolomide (TMZ) treatment, and thus highlights the value of developing small molecules or antibodies against the SOX9\/CA9 pathway, for combination therapy with TMZ, in the more efficient management of glioma            \u003ca rel=\"nofollow\"\u003e             PMID:                        29749469            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA9 SNP rs1048638 and haplotype A1AA are associated with the susceptibility of cervical invasive squamous cell carcinoma for Taiwanese women            \u003ca rel=\"nofollow\"\u003e             PMID:                        29725249            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The TCGA data revealed that CAIX expression was significantly higher in bladder cancer specimens than in normal tissue.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29949785            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CAIX enzyme inhibition assay showed the IC50 values in nM range. Though all the three compounds (1-3) showed a good binding with CAIX, compound 2 showed the best inhibition of CAIX activity. These compounds were non-toxic on normal cell lines (HEK-293) and significantly inhibit the proliferation of hypoxic cancer cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        28830777            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA9 expression was observed in normal islets, while neuroendocrine microadenomas and small (\u0026lt; 1 cm) pancreatic neuroendocrine neoplasms\/tumors showed CA9 expression loss.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29666945            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study revealed that CA9 expression was a pivotal predictive factor for poor prognosis after radical surgery for HCC. Moreover, the CA9 regulation of the expression of EMT-related molecules represented a mechanism that enhanced malignant potential.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28849188            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Report weak CA9 immunoreactivity in majority of CA9 positive colorectal carcinoma cases associated with macroscopic growth pattern.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28554753            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Molecular characterization of carbonic anhydrase IX catalytic domain has been presented.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27373313            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors present evidence that enhanced autophagy does not play a role in the enhanced growth of the CA9+ cells. Our study suggests a direct in vivo functional link between hypoxic cells and CICs in primary cervix cancer xenografts.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27901496            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genetic disruption of the intracellular pH-regulating proteins Na+\/H+ exchanger 1 (SLC9A1) and carbonic anhydrase 9 reduces the proliferation of colon cancer cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28055960            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that targeting the hypoxic tumor compartment by knockdown of carbonic anhydrase IX (CAIX) using short hairpin RNA or by chemical inhibition of CAIX with acetazolamide potentiates the anti-cancer activity of mTOR inhibitors rapamycin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27153561            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors demonstrate that CAIX associates with MMP14 through potential phosphorylation residues within its intracellular domain, and that CAIX enhances MMP14-mediated collagen degradation by directly contributing hydrogen ions required for MMP14 catalytic activity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28692057            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results provide evidence that CAIX induces chemoresistance of A549 cells, a lung cancer cell line.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28028936            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggest the possibility that CA9 exosomes released from hypoxic RCC may enhance angiogenesis in microenvironment, thereby contributing to cancer progression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28851650            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA9 expression is highly associated with distant metastases, including para-aortic involvement.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27102843            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Increased miR-210 and concomitant decreased ISCU RNA levels were found in ~40% of tumors and this was significantly associated with HIF-1alpha and CAIX, but not MCT1 or MCT4, over-expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28099149            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            describe the identification of the structural determinants responsible for the CA IX\/CAND1 interaction            \u003ca rel=\"nofollow\"\u003e             PMID:                        28388044            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that CAIX (carbonic anhydrase IX) is a novel downstream mediator of asTF (alternatively spliced tissue factor) in pancreatic ductal adenocarcinoma, particularly under hypoxic conditions that model late-stage tumor microenvironment; tumor hypoxia appears to lead to up-regulation of CAIX expression (or 'activation'), which is more pronounced in tumor cells overexpressing asTF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27721473            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our findings suggest that LCN2 suppresses tumour metastasis by targeting the transcriptional and post-transcriptional regulation of CAIX in oral squamous cell carcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        27207653            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings suggest that CA9, and particularly its carbonic anhydrase activity, promotes the tumorigenicity of adult T-cell leukemia\/lymphoma-derived cells and may be involved in malignant development of lymphoma-type adult T-cell leukemia\/lymphoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28075522            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We demonstrated that the expression levels of glycolysis-related proteins glucose transporter 1, hexokinase II, carbonic anhydrase IX, and monocarbonylate transporter 4 differ between thyroid cancer subtypes and are correlated with poorer prognosis            \u003ca rel=\"nofollow\"\u003e             PMID:                        28347233            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CAIX and PTEN had prognostic importance for metastatic renal cell carcinoma patients receiving first-line VEGFR TKI. Future validation and mechanistic studies are required.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26526582            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            combined HIF1alpha and CAIX protein expression may serve as an unfavorable prognostic indicator particularly in patients treated with cyclophosphamide-based chemotherapy or radiotherapy as well as those with basal phenotype of breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        27184798            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA9 may have a role in castration-resistant prostate cancer progression            \u003ca rel=\"nofollow\"\u003e             PMID:                        27630286            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The diagnostic accuracy of CA9 expression for clear cell renal cell carcinoma was 100%.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27775441            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression of CA IX was associated with pancreatic cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26224207            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CAIX mRNA expression was significantly higher (p \u0026lt; 0.05) in hypoxia for all cell lines, which was in agreement with protein expression by ICC. CAXII expression was mixed, with a modest hypoxia-related increase in two cell lines (p \u0026lt; 0.05) and no change in others.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26276155            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We also demonstrated that the cell-surface CA IX level dropped during the death progress due to an increased ECD shedding, which required a functional ADAM17. Inhibitors of metalloproteinases reduced CA IX ECD shedding, but not apoptosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26993100            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In neuroblastoma cells, CAIX and PGK1 expression is up regulated under hypoxia and correlates with response to targeted anti-proliferative treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26510737            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Flow cytometrically sorted CA9+ population showed increased mRNA level of a Wnt signaling factor AXIN2. In conclusion, these observations indicate that CA9 expression in normal crypt base cells has association with intestinal epithelial stemness            \u003ca rel=\"nofollow\"\u003e             PMID:                        26648507            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We used cobalt chloride (CoCl2) as a hypoxia-mimetic agent and found that the expression of HIF-1a protein, CA IX mRNA and protein, is effectively upregulated, except for HIF-1a mRNA.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26648580            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We conclude that CA9\/miR34 interplay shares in the hypoxic regulation of mammospheres and therefore, may play a relevant role in the hypoxic breast cancer stem cell niche.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26553365            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Knockdown of CAIX significantly reduced proliferation of cancer cells, suggesting that rapid efflux of lactate and H(+), as enhanced by CAIX, contributes to cancer cell survival under hypoxic conditions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26337752            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that carbonic anhydrase IX (CAIX) inhibition as a relevant therapeutic goal in breast cancer, targeting the migratory, invasive, and metastatic potential of this disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26259239            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Inhibition of CA9 expression or activity resulted in radiation sensitization of RCC in a preclinical mouse model.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26252502            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Urinary CAIX has a high sensitivity and specificity for diagnosing urothelial bladder cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26138037            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The intrinsic thermodynamic parameters of compound binding to CA IX helped to draw the compound structure to thermodynamics relationship.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26794023            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our study showed that the expression of CAIX in oral squamous cell carcinoma (OSCC) samples can predict the progression of OSCC and survival of OSCC patients in Taiwan            \u003ca rel=\"nofollow\"\u003e             PMID:                        26130414            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we aimed to determine the effect of immunohistochemical staining of ezrin, carbonic anhydrase IX (CA IX), and neuropilin-2 on the prognosis of patients diagnosed with metastatic RCC who were treated with TKIs between January 2007 and June 2012.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26026587            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA IX is expressed in B-cell lymphomas and is qualitatively correlated with extracellular acidosis in xenograft tumor models.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25130478            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We have developed an efficient system for the production of the catalytic domain of CA IX in methylotrophic yeast Pichia pastoris            \u003ca rel=\"nofollow\"\u003e             PMID:                        26522624            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CAIX expression is increased in hypoxia to compensate for the decrease in its activity produced by a low extracellular pH. A major function of CAIX is to lower the extracellular pH.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26249175            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A strong positive correlation between the mRNA expression levels of HIF-2alpha, CA9, VEGF, GLUT-1 and OPN suggests a specific hypoxia-associated profile of mRNA expression in glioblastoma multiforme            \u003ca rel=\"nofollow\"\u003e             PMID:                        25963717            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            expression of the CA-IX protein is a crucial predictor of poor prognosis in resectable hepatocellular carcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        25738958            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Preventing carbonic anhydrase IX association with 45 S rDNA gene promoters.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25793203            \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":43915092492513,"sku":"BL-2229NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLRWANo1BAACOUIBFWcA067_10e29b65-89c3-4294-b457-bf5583173908.jpg?v=1685852940"},{"product_id":"recombinant-cynomolgus-nectin-4-protein-fc-tag-bl-2235np","title":"Recombinant Cynomolgus Nectin-4 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 Cynomolgus Poliovirus Receptor-Related Protein  4 is produced by our Mammalian expression system and the target gene encoding Gly32-Ser349 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=\"L0N6D9\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/L0N6D9\/entry\"\u003eL0N6D9\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%;\"\u003ePVRL4; Nectin-4; Ig superfamily receptor LNIR; Poliovirus receptor-related protein 4; PRR4; LNIR\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%;\"\u003eNectin-4 (PVRL4) is a type I transmembrane glycoprotein which belongs to the nectin family of Ig superfamily proteins. It contains two Ig-like C2-type domains and one Ig-like V-type domain. PVRL4 seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with nectin-1. It does not act as receptor for alpha-herpesvirus entry into cells. It is predominantly expressed in placenta, the embryo and breast carcinoma. But it is not detected in normal breast epithelium. The soluble form is produced by proteolytic cleavage at the cell surface (shedding), probably by ADAM17. Mutations in this gene are the cause of ectodermal dysplasia-syndactyly syndrome type 1, an autosomal recessive disorder.\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%;\"\u003e61 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%;\"\u003e80-90 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 20m 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","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915061199073,"sku":"BL-2235NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLRiAUCEFAACLuIBeF5I608_800e126c-5f70-40f0-988d-4dfcb734d395.jpg?v=1685851921"},{"product_id":"recombinant-human-vista-protein-his-tag-bl-2242np","title":"Recombinant Human VISTA 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 Platelet Receptor Gi24 is produced by our Mammalian expression system and the target gene encoding Phe33-Ala194 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=\"AAH20568.1\" target=\"_blank\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/protein\/AAH20568.1\"\u003eAAH20568.1\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%;\"\u003ePlatelet receptor Gi24; Stress-induced secreted protein-1; Sisp-1; C10orf54; SISP1\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%;\"\u003eplatelet receptor Gi24 is a single-pass type I membrane protein, and located at the cell surface. The protein can be cleaved by MMP14, and stimulate MMP14-mediated MMP2 activation. It is participated in the BMP signaling pathway. It also regulates the CD4-pasitive, alpha-beta T cell proliferation, and T cell cytokine production negatively. However, the protein can regulate stem cell differentiation positively.\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%;\"\u003e19.2 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%;\"\u003e30-50 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":43915043995873,"sku":"BL-2242NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLVSAXFGPAAC0wdJpM4Y990_3ed826ec-1f6d-4554-856e-ef7f78119b8a.jpg?v=1685851349"},{"product_id":"recombinant-human-claudin-18-2-protein-his-tag-bl-2259np","title":"Recombinant Human Claudin-18.2 Protein (N-8His)","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 CLDN18.2 is produced by our E.coli expression system and the target gene encoding Asp28-Leu76 is expressed with a 8His 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=\"P56856-2\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/P56856\/entry#P56856-2\"\u003eP56856-2\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%;\"\u003eClaudin-18; CLDN18\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%;\"\u003eClaudin-18(CLDN18) is a protein that in humans is encoded by the CLDN18 gene. It belongs to the group of claudins. CLDN18 belongs to the large claudin family of proteins, which form tight junction strands in epithelial cells. CLDN18 plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. CLDN18 has two isoform A1 and isoform A2. IMAB362 (Claudiximab) is a monoclonal antibody against isoform 2 of Claudin-18. It is under investigation for the treatment of gastrointestinal adenocarcinomas and pancreatic tumors. IMAB362 was developed by Ganymed Pharmaceuticals AG.\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%;\"\u003eSupplied as a 0.2 μm filtered solution of 25mM Tris-HCl, 25mM NaCl, 0.1% Triton X-100, 10% glycerol, 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%;\"\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":43915015323873,"sku":"BL-2259NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLaWAL8MFAACjbafgkDU179_f5938f7b-7404-47df-8414-341d517ff74d.jpg?v=1685850574"},{"product_id":"recombinant-cynomolgus-tslp-protein-his-tag-bl-2262np","title":"Recombinant Cynomolgus TSLP 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 Cynomolgus Thymic Stromal Lymphopoietin is produced by our E.coli expression system and the target gene encoding Tyr29-Gln159(Glu37Gln) 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=\"XP_005557555.1\" target=\"_blank\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/protein\/XP_005557555.1\"\u003eXP_005557555.1\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%;\"\u003eThymic stromal lymphopoietin;Thymic stroma-derived lymphopoietin;Tslp\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%;\"\u003eThymic stromal lymphopoietin (TSLP) is a protein belonging to the cytokine family, contains 140 amino acids. It is known to play an important role in the maturation of T cell populations through activation of antigen presenting cells. TSLP induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c+ dendritic cells. It can induce allergic inflammation by directly activating mast cells. TSLP is produced mainly by non-hematopoietic cells such as fibroblasts, epithelial cells and different types of stromal or stromal-like cells. These cells are located in regions where TSLP activity is required.\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%;\"\u003e16.2 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%;\"\u003e16 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, 6% Trehalose, 2% Glycine, 50mM NaCl, 0.05% Tween 80, pH7.5.\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 0.1 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":43915032035553,"sku":"BL-2262NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLaaANoDcAACe9Dn2q6Q088_aabe093a-ac51-4569-8d59-1c5a23b868d3.jpg?v=1685850980"},{"product_id":"recombinant-rhesus-macaque-icos-protein-fc-tag-bl-2275np","title":"Recombinant Rhesus Macaque ICOS 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 Rhesus Macaque Inducible T-cell Costimulator is produced by our Mammalian expression system and the target gene encoding Gly20-Lys140 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=\"H9Z062\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/H9Z062\/entry\"\u003eH9Z062\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%;\"\u003eInducible T-cell costimulator; activation-inducible lymphocyte immunomediatory molecule; CD278; AILIM; CVID1; ICOS\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%;\"\u003eInducible T-cell costimulator, also known as activation-inducible lymphocyte immunomediatory molecule, CD278, AILIM, CVID1 and ICOS, belongs to the CD28 and CTLA4 cell surface receptor family.. ICOS contains one Ig-like V-type domain and exsits as a homodimer with disulfide-linked. ICOS is highly expressed on tonsillar T-cellsand can be induced by PMA and ionomycin, ICOS plays an important role in cell-cell signaling, immune responses, and regulation of cell proliferation. Defects in ICOS are the cause of immunodeficiency common variable type 1, which is a primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antige.\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%;\"\u003e40.8 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%;\"\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 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","brand":"Beta LifeScience","offers":[{"title":"10μg","offer_id":43915091247329,"sku":"BL-2275NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLbKARGjqAADmXr128zo822_ca0b9a74-9743-4592-b89c-c6a79210093b.jpg?v=1685852878"},{"product_id":"recombinant-human-bcma-protein-fc-tag-bl-2278np","title":"Recombinant Human BCMA Protein (C-mFc)","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 Tumor Necrosis Factor Receptor Superfamily Member 17 is produced by our Mammalian expression system and the target gene encoding Met1-Ala54 is expressed with a mouse 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%;\"\u003eQ02223\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 17; B-cell maturation protein; CD269; Tnfrsf17; Bcm; Bcma\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%;\"\u003eB cell maturation antigen (BCMA) is a member of the TNF receptor superfamily. It has been designated TNFRSF17. Mouse BCMA is a 185 amino acid (aa) protein consisting of a 49 aa extracellular domain, a 23 aa transmembrane domain, and a 113 aa intracellular domain. BCMA is a type III membrane protein containing one extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs and mature B cell lines. Although some expression has been observed at the cell surface, BCMA appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells. This data suggests that BCMA may play an important role in B cell development,function and regulation.\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%;\"\u003e32.5 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%;\"\u003e35-42 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 \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%;\"\u003eReceptor for TNFSF13B\/BLyS\/BAFF and TNFSF13\/APRIL. Promotes B-cell survival and plays a role in the regulation of humoral immunity. Activates NF-kappa-B and JNK.\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 III membrane protein. Endomembrane system; Single-pass type III membrane protein. Note=Perinuclear Golgi-like structures.\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            11913           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            109545           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:608           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000053243           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29087261            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            High BCMA expression is associated with primary central nervous system lymphoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28521029            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            soluble BCMA sequesters circulating BAFF, thereby preventing it from performing its signaling to stimulate normal B-cell and plasma cell development, resulting in reduced polyclonal antibody levels in multiple myeloma patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26960399            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Studied expression of B-cell maturation antigen (BCMA) in osteoblasts and the toxic effect of chromium on its expression; found BCMA is involved in osteogenesis of osteoblasts; chromium downregulates expression of BCMA in osteoblasts.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26011700            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BCMA has other contributors for ligands binding except DxL motif. The affinity of BCMA for APRIL higher than for BAFF may be caused by the segment outside of the conservative DxL motif. Moreover, the exposition of new binding modes of BCMA2 interacting with APRIL may establish the foundation of designing novel drugs in the future            \u003ca rel=\"nofollow\"\u003e             PMID:                        28260502            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            New molecular mechanisms of in vivo Multiple Myeloma (MM) growth and immunosuppression critically dependent on BCMA and APRIL in the Bone marrow microenvironment, further supporting targeting this prominent pathway in MM.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27127303            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We have identified a specific serum protein, BCMA, as a novel independent marker for both monitoring and predicting outcomes for MM patients. We have shown that sBCMA is elevated in MM patients, and can be used to follow their disease status, PFS and OS.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28034989            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The expression levels of serum BAFF and the three receptors (TACI, BCMA and BAFF-R) in non-Hodgkin lymphoma patients were significantly higher than in healthy controls.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28028945            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Decreased BCMA expression on peripheral B cells according to severe disease activity suggests that BCMA plays an important regulating role in B-cell hyperactivity and immune tolerance homeostasis in systemic lupus erythematosus patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        26424128            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            results suggest that Akt and JNK pathways are involved in the regulation of B-cell maturation antigen (BCMA)            \u003ca rel=\"nofollow\"\u003e             PMID:                        26914861            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            shedding of BCMA by gamma-secretase controls plasma cells in the bone marrow and yields a potential biomarker for B-cell involvement in human autoimmune diseases            \u003ca rel=\"nofollow\"\u003e             PMID:                        26065893            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            elevated serum levels in patients with Behcet's disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        25759827            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show significant differences in expression of tumour necrosis factor family (BAFF) receptors BAFF-R, BCMA and TACI in patients with and without anti-Jo-1 or anti-Ro52\/anti-Ro60 autoantibodies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25301447            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High BCMA expression is associated with breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25750171            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BAFF and APRIL as well as their cognate receptors (BCMA, TACI) correlate with glioma grade. (Meta-analysis)            \u003ca rel=\"nofollow\"\u003e             PMID:                        24376672            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The B cell maturation antigen (BCMA) is a tumor necrosis family receptor member that is predominantly expressed on terminally differentiated B cells and, upon binding to its ligands B cell activator of the TNF family and a proliferation inducing ligand.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23237506            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Activation of B cells through BCMA regulates spinal cord injury-induced autoimmunity via a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF).            \u003ca rel=\"nofollow\"\u003e             PMID:                        23088438            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that MAGE3, Survivin and B-cell maturation antigen (BCMA) mRNA-pulsed dendritic cells (DCs) are capable of stimulating tumor-associated antigens (TAA)-specific T-cell responses in multiple myeloma (MM) patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23728352            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that B-cell maturation antigen (BCMA) is a suitable target for chimeric antigen receptor (CAR)-expressing T cells, and adoptive transfer of anti-BCMA-CAR-expressing T cells is a promising new strategy for treating multiple myeloma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23344265            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23776238            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the effect of APRIL is mediated via BCMA, which does not activate the classical NF-kappaB pathway, whereas it induces a novel signaling pathway, which involves JNK2 phosphorylation, FOXO3A activation, and GADD45 transcription            \u003ca rel=\"nofollow\"\u003e             PMID:                        23071284            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum BCMA levels were higher among patients with progressive disease than those with responsive disease. Overall survival was shorter among patients whose serum BCMA levels were above the median.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22804669            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TNFRSF17 may be a candidate gene associated with the pathogenesis of colon cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22108903            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data advance BCMA as an inflammation-related TNF superfamily member in keratinocytes, of potential importance in the management of inflammatory skin conditions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22166983            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            primary leukemia B-cell precursors aberrantly express receptors of the BAFF-system, BAFF-R, BCMA, and TACI            \u003ca rel=\"nofollow\"\u003e             PMID:                        21687682            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This is the first study, presenting together the TNFSF members APRIL, BAFF, TWEAK and their receptors in different areas of normal renal tissue and renal cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21483105            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Signaling through BCMA enhances B cell activation following exposure to TLR9 agonists, and increased expression in SLE may contribute to the production of IgG autoantibodies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21250838            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            genetic polymorphisms are associated with gastrointestinal disorders            \u003ca rel=\"nofollow\"\u003e             PMID:                        20016944            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of BCMA, TACI, and BAFF-R by multiple myeloma cells support cell growth and survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        14512299            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            APRIL.TACI_d2 and APRIL.BCMA complexes together reveal the mechanism by which TACI engages high affinity ligand binding through a single cysteine-rich domain            \u003ca rel=\"nofollow\"\u003e             PMID:                        15542592            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BCMA is a target of donor B-cell immunity in patients with myeloma who respond to Donor lymphocyte infusions            \u003ca rel=\"nofollow\"\u003e             PMID:                        15692072            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Review. APRIL interactions with BCMA likely govern memory B cell populations.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16919470            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Review. Direct BAFF\/APRIL signalling in T cells and\/or T cell modulation in response to a BAFF-modified B cell compartment may play an important role in inflammation and immunomodulation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16931039            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The BCMA inhibited HRS cell accumulation in vitro and might attenuate HL expansion in vivo.            \u003ca rel=\"nofollow\"\u003e             PMID:                        16960154            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            BCMA TVs were observed only in some CD19+ cell samples.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17825416            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            rheumatoid arthritis fibroblast like synoviocytes are stimulated by APRIL and express the APRIL receptor BCMA            \u003ca rel=\"nofollow\"\u003e             PMID:                        17968879            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of B cell maturation Ag (BCMA) is also highly regulated and we demonstrate that BCMA expression is only acquired in MB cells and in a manner accompanied by loss of BAFF-R expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        18025170            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we observed APRIL expression, together with TACI and BCMA in gut-associated lymphoid tissue, lamina propria, and in the epithelium of stomach, small and large intestine, and rectum.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19741596            \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":43915041079521,"sku":"BL-2278NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLbOAEcTYAADMbntmRDw530_946b8b4c-872b-480e-b449-aefa98d51a69.jpg?v=1685851259"},{"product_id":"recombinant-human-ca125-protein-his-tag-bl-2302np","title":"Recombinant Human CA125 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 Mucin-16 is produced by our Mammalian expression system and the target gene encoding Gly12660-Met12923 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%;\"\u003eQ8WXI7\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%;\"\u003eCA125 ovarian cancer antigen; CA125; CA-125; CA125MUC-16; FLJ14303; MUC16; mucin 16, cell surface associated; mucin-16\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%;\"\u003eMUC16, also known as the CA125 antigen, is a mucin protein that may be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy. MUC16 is over-expressed by tumor cells including ovarian and mesothelial cancers. The transmembrane form can adhere to mesothelin in the peritoneum, facilitating metastasis of ovarian cancer to the peritoneal cavity. MUC16 also binds galectin-1 on immune cells and enhances its expression on tumor cells. MUC16-expressing tumors adhere to NK cells, down-regulate CD16 and suppress NK response, which may promote immune evasion. MUC16 is also cyclically expressed in the endometrium and may contribute to immune privilege during pregnancy. In the eye, MUC16 and other mucins protect the cornea and keep it hydrated. It is altered on the conjunctival epithelium of patients with non-Sjogren dry eye syndrome.\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%;\"\u003e29.2 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%;\"\u003e40-70 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 50 mM Tris-HCl, 100 mM Glycine, 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 0.1 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%;\"\u003eThought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces.\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. Secreted, extracellular space. Note=May be liberated into the extracellular space following the phosphorylation of the intracellular C-terminus which induces the proteolytic cleavage and liberation of the extracellular domain.\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            15582           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            606154           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:94025           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000381008           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29797475            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            The expression profile of studied Mucins MUC16 and MUC1 and truncated O-glycans was not associated with the site of origin of ovarian cancer (OVCA) cell lines            \u003ca rel=\"nofollow\"\u003e             PMID:                        30011875            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum HE4 with its high specificity is useful in ruling out ovarian malignancy especially among the premenopausal women and Risk of Ovarian Malignancy Algorithm (ROMA)which is the combination of both serum CA 125 and HE4, appears to be an all-rounder with overall good sensitivity and specificity especially among the postmenopausal women.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30063463            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA125 appears the most reliable biomarker for OC monitoring, whereas HE4 contributes additional information only in a minority of cases            \u003ca rel=\"nofollow\"\u003e             PMID:                        30125544            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The level of HE4 in ovarian cancer ascites may reflect the therapeutic effect of ovarian cancer patients, and a high level of HE4 might predict chemoresistance and the possibility of ascites formation. The determination of the expression of HE4 alone or combined with CA125 levels in both serum and ascites in ovarian cancer patients with ascites may have important significance for guiding and improving the treatment            \u003ca rel=\"nofollow\"\u003e             PMID:                        29903044            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Lower CA125 serum levels, negative vascular invasion, and wild-type BRAF status were significantly associated with improved 2-year DFS rates among patient with stage III disease who received adjuvant chemotherapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29562502            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We can infer from this study that increased maternal serum CA 125 levels are associated with the preeclampsia and its severity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29718786            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum CA125 concentrations are correlated with coronary artery calcification score in the population without known coronary artery disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29731508            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High serum CA125 level is associated with epithelial ovarian cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28444641            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum CA-125 was significantly different between infertile women with and without pelvic endometriosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29944231            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Use of HE4 instead of CA125 did not significantly improve diagnostic performance of risk of malignancy indices 1-4 in patients with an adnexal mass            \u003ca rel=\"nofollow\"\u003e             PMID:                        29238719            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            TP53 autoantibody levels provide a biomarker with clinically significant lead time over elevation of CA125 or an elevated ROCA value. Quantitative assessment of autoantibodies in combination with CA125 holds promise for earlier detection of invasive epithelial ovarian cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        28637689            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA-125 levels may be the most useful marker for predicting advanced-stage disease            \u003ca rel=\"nofollow\"\u003e             PMID:                        25761476            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            For screened women at familial\/genetic ovarian cancer risk, risk of ovarian cancer algorithm had better early-stage sensitivity at high specificity, and low yet possibly acceptable positive predictive value compared with CA125 , warranting further larger cohort evaluation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28143870            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum SCC-Ag, hs-CRP, and CA-125 were higher in recurrence cervical patients which could be potential biomarkers for predicting cervical cancer recurrence risk.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28901315            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The determination of CA125 before surgery may be helpful in the evaluation of the regional lymph nodes, and is a poor prognostic factor for overall survival and disease-free survival in endometrial cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28624692            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High CA125 expression is associated with adnexal malignancy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27116243            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The ratio between menstrual and midcycle phases had the worst performance. CA-125 may be useful for the diagnosis of deep endometriosis, especially when both are collected during menstruation and in midcycle.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28660213            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Architect CA 125 II and HE4 values in Chinese women presenting with a pelvic mass            \u003ca rel=\"nofollow\"\u003e             PMID:                        28549533            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            highly predictive of endometriosis in women with symptoms of pain and\/or subfertility            \u003ca rel=\"nofollow\"\u003e             PMID:                        27987404            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HE4 seems to be superior to CA125 in the detection of recurrent disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29463191            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High CA125 expression is associated with breast, endometrial and ovarian cancers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26918940            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            knockdown of MUC16 significantly weakened the capabilities of cells for proliferation and migration            \u003ca rel=\"nofollow\"\u003e             PMID:                        27167110            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this platinum-resistant population, PD was typically detected earlier by imaging than by CA-125, irrespective of bevacizumab treatment. Disease status by CA-125 at the time of PD was not prognostic for overall survival. Regular radiologic assessment as well as symptom benefit assessment should be considered during PROC follow-up.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27407100            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data characterized CA-125 kinetics and identified modeled kinetic parameters.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29187468            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these studies demonstrate that PPARgamma is an important modulator of MUC16 expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27292441            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data point to a novel opportunity to enrich Abs at mucosal sites by targeting Abs to MUC16 through changes in Fc glycosylation, potentially blocking viral movement and sequestering the virus far from the epithelial border.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26960182            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Within this review, we highlight both the processes involved in the expression of aberrant glycan structures on mucins, as well as the potential downstream impacts on cellular signaling.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27483328            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In a cohort of patients with acute decompensated heart failure, cancer antigen 125 is independently associated with prolonged length of stay.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28265209            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The current study uncovers the contribution of oncogenic KRAS to serum marker CA125 production through a mechanism that involves the ERK\/c-Myc axis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28108627            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mesothelin\/mucin 16 signaling in activated portal fibroblasts regulates cholestatic liver fibrosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28287406            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the loss of MUC16 and E-cadherin expression resulted in the formation of more compact spheroids.  In addition, our data describe an unusual link between E-cadherin expression and less compact spheroids. Our data also emphasize the role of MUC16 and b1 integrin in Epithelial ovarian cancer (EOC) spheroid formation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27612856            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Preoperative CA-125 can predict neither the progression-free nor overall survival for primary serous ovarian cancer patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28551658            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In pseudomyxoma peritonei CA125 was infrequently expressed by tumor cells, but in most of the cases adjacent nonneoplastic mesothelial cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27038681            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Differences in the apparent expression levels of CEA, CA153 and CA125 in patients with nipple discharge and healthy persons were validated.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27327081            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The endometrial expression of PR and Ki67 along with serum CA125 predicted the development of lymph node metastasis in endometrial cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27163153            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            a distinct role for N-glycans in promoting MUC16's binding affinity toward galectin-3 and in causing retention of the lectin on the epithelial cell surface.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28487369            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HE4 is elevated less frequently than CA125 in benign adnexal tumors, regardless of age or menopausal status            \u003ca rel=\"nofollow\"\u003e             PMID:                        27752776            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            rebamipide induces the differential upregulation of MUC16 in stratified cultures of human corneal epithelial cells, which may have implications to the proper restoration of barrier function in ocular surface disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27725198            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In postmenopausal women, CA-125 levels were significantly higher in those with epithelial ovarian cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27855043            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            When the value of CA125 is higher than 10 U\/ml and continuously increased, need to be vigilant and should be combined with imaging examination (PET-CT), early detection of recurrent lesions and early retreatment, especially maybe have the opportunity for surgery, this result may improve the prognosis for recurrent patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28284216            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Pap test abnormalities are frequent in ECCC. Although it is less accurate in the diagnosis of ECCC than in the detection of malignancy, endometrial sampling is still the main procedure for the diagnosis of ECCC. Higher preoperative CA-125 concentrations imply the presence of advanced stage ECCC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27173475            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            levels before treatment and decreased speed of decline of serum CA125 after treatment were independent factors. There is a negative correlation between pre-treatment CA125 level and prognosis, the sooner decrease of CA125 levels post-treatment the better prognosis are.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27629537            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We found the high specificity of HE4 and CA125 while differentiating ovarian benign diseases from epithelial ovarian cancer in postmenopausal women and the high sensitivity of CA125 in detecting epithelial ovarian cancer in premenopausal patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        27436085            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results collectively indicate unique links between dual-specificity phosphatase 28 (DUSP28) and mucins MUC5B\/MUC16 and their roles in pancreatic cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27230679            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            that, in adenocarcinomas and borderline ovarian tumors, the major carriers of SLe(a) and SLe(x) are MUC16 and\/or MUC1 (100 and 92 % for SLe(a)            \u003ca rel=\"nofollow\"\u003e             PMID:                        27003157            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A statistically significant difference was observed between HE4 values at primary diagnosis and at recurrence, respectively, comparing recurrent and non-recurrent patients while CA125 values resulted not statistically significant at each time point.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26531723            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We assessed the diagnostic accuracy of a newly developed laboratory score-based on CA125, platelet count (PLT), C-reactive protein (CRP), and fibrinogen levels-in the preoperative diagnosis of adnexal mass            \u003ca rel=\"nofollow\"\u003e             PMID:                        26499778            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High CA125 expression is associated with Ovarian Tumors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27268637            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We evaluated the clinical performance of LOCItrade mark-based tumor marker assays CEA, CA19-9, CA15-3, CA125 and AFP in patients with gastrointestinal cancer and demonstrated their high diagnostic power            \u003ca rel=\"nofollow\"\u003e             PMID:                        28011514            \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":43915021091041,"sku":"BL-2302NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLbaAS3E7AACyA_vYDg0409_f1a7f916-9ea0-48c1-b958-faa1090ba859.jpg?v=1685850719"},{"product_id":"recombinant-human-gpc3-protein-fc-tag-bl-2309np","title":"Recombinant Human GPC3 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 Glypican-3 is produced by our Mammalian expression system and the target gene encoding Gln25-His559 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%;\"\u003eP51654\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%;\"\u003eGlypican-3; GTR2-2; Intestinal protein OCI-5; MXR7; GPC3; OCI5\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%;\"\u003eGlypican-3\/GPC3 is a member of the glypican family. It belongs to the glypican family and is highly expressed in lung, liver, and kidney. It is a heparan sulfate proteoglycan, which is overexpressed in various neoplasms such as hepatocellular carcinoma, malignant melanoma, and testicular yolk sac tumor, and plays an important role in cell growth and differentiation. GPC3 function is tissue dependent. In some tissues, GPC3 acts as a tumor suppressor gene, whereas in others, it acts as an oncofetal protein. GPC3 is a reliable marker for hepatocellular carcinoma. The sensitivity and specificity exceeds both alpha-fetoprotein and hepatocyte-paraffin1. GPC3 immunohistochemistry can aid in the differentiation of testicular germ cell tumors, being expressed in all yolk sac tumors but not in seminomas. GPC3 expression has also been identified in some squamous cell carcinomas of the lung and clear cell carcinomas of the ovary. Glypican-3 is currently regarded as a tumor marker and potential target for immunotherapy.\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%;\"\u003e87.7 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%;\"\u003e100-120\u0026amp;65\u0026amp;40 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 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%;\"\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%;\"\u003eCell surface proteoglycan that bears heparan sulfate. Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins. Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation. Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligands. Positively regulates the non-canonical Wnt signaling pathway. Binds to CD81 which decreases the availability of free CD81 for binding to the transcriptional repressor HHEX, resulting in nuclear translocation of HHEX and transcriptional repression. Inhibits the dipeptidyl peptidase activity of DPP4. Plays a role in limb patterning and skeletal development by controlling the cellular response to BMP4. Modulates the effects of growth factors BMP2, BMP7 and FGF7 on renal branching morphogenesis. Required for coronary vascular development. Plays a role in regulating cell movements during gastrulation.\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; Lipid-anchor, GPI-anchor; Extracellular side.\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%;\"\u003eGlypican 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            4451           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            300037           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:2719           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000377836           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28378832            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            GPC3 is operating through an intricate molecular signaling network. From the balance of these interactions, the inhibition of breast metastatic spread induced by GPC3 emerges.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30267212            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Its surface is modified with anti-GPC3 antibody.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29916268            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data suggest that transcriptionally targeted delivery of transgene in HCC cells can be achieved using the GPC3 promoter and this targeting strategy produces limited toxicity to normal liver cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        29563582            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High GPC3 expression is associated with Hepatocellular Carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28429175            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study demonstrated that GPC3 expression is inversely associated with glucose metabolism, suggesting that GPC3 may play a role in regulating glucose metabolism in hepatocellular carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29398870            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the intravenous injection of SF-PL\/siGPC3 into nude mice bearing subcutaneous human HepG2 xenografts effectively inhibited tumor growth and also increased the survival rates of animals. These results revealed the great potential of the PEI-modified liposomal nanomedicine carrying SF and siGPC3 to improve Hepatocellular carcinomatreatment            \u003ca rel=\"nofollow\"\u003e             PMID:                        29106433            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Invasive hepatocellular carcinoma (HCC) samples and HCC cell lines with high metastatic potential exhibited higher MXR7 expression. Overexpression of MXR7 promoted epithelial-mesenchymal transition (EMT) progress, and MXR7 depletion repressed the EMT phenotype. Human MXR7 protein is a mediator of EMT and metastasis in HCC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28812296            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Overexpression of GPC3 was significantly associated with poor prognosis in patients with hepatocellular carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29901640            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data show that glycanation and convertase maturation are not required for soluble mutant GPC3 to inhibit hepatocellular carcinoma cell proliferation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29345911            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that several microRNAs targeting the oncogenic functions of glypican-3 (GPC3).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28476031            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            presence distinguishes aggressive from non-aggressive odontogenic tumors            \u003ca rel=\"nofollow\"\u003e             PMID:                        27647326            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPC3 as a potential metastasis suppressor gene and suggest its value as a prognostic marker in gastric cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27259271            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this study we systematically evaluated a series of CAR constructs targeting glypican-3 (GPC3), which is selectively expressed on several solid tumors. We compared GPC3-specific CARs that encoded CD3zeta (Gz) alone or with costimulatory domains derived from CD28 (G28z), 4-1BB (GBBz), or CD28 and 4-1BB (G28BBz).            \u003ca rel=\"nofollow\"\u003e             PMID:                        27530312            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that glypican-3 (GPC3) is an important regulator of epithelial-mesenchymal transition (EMT) in breast cancer, and a potential target for procedures against breast cancer metastasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27507057            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Glypican-3 overexpression in Wilms tumor correlates with poor overall survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28432433            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            glypican-3 has a role in HBV-related hepatocellular carcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        27286460            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MOSPD1 is a possible candidate gene for DORV, probably in combination with GPC3. Further studies of the combined functions of MOSPD1 and GPC3 are needed, and identification of additional patients with MOSPD1 and GPC3 duplication should be pursued            \u003ca rel=\"nofollow\"\u003e             PMID:                        28636109            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Glypican-3 is correlated with the clinical malignant behavior of hepatocellular carcinoma and its phenotype changes from positive to negative during tumor cells differentia- tion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28087980            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The diagnostic sensitivity for hepatocellular carcinoma increased to 72.8% (206 of the 283) when glypican 3 was combined with alpha-fetoprotein.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26370140            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The lncRNA glypican 3 antisense transcript 1 (GPC3-AS1) has been reported to be a potential biomarker for hepatocellular carcinoma (HCC) screening. We observed a significant upregulation of GPC3-AS1 in HCC. Increased expression of GPC3-AS1 was associated with alpha-fetoprotein, tumor size, microvascular invasion, encapsulation, Barcelona Clinic Liver Cancer stage, and worse prognosis of HCC patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27573079            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study provides the first evidence that GPC3 can modulate the PCSK9 extracellular activity as a competitive binding partner to the LDLR in HepG2 cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27758865            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            By subsequent Sanger sequencing of genomic DNA we could map the chromosomal break points to define a deletion size of 43,617 bp including exons 5 and 6 of the GPC3 gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28371070            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This is the first study in which the optimal HLA-A*0201 GPC3 epitopes were screened from a large number of candidates predicted by three software. The optimized HLA-A*0201 GPC3 peptides will provide new epitope candidates for hepatocellular carcinoma (HCC) immunotherapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27102087            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPC3 and KRT19 overexpression are associated with carcinogenesis, progression, and poor prognosis in patients with PDAC and a valuable biomarker for diagnosis of PDAC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27689616            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The clinical implication of GPC3 detection and targeting in the management of patients with hepatocellular carcinoma. Review.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26755876            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Glypican 3 expression showed a significant difference between endometrioid endometrial carcinoma and serous endometrial carcinoma, and it was significantly correlated with tumor grade, stage and myometrial invasion            \u003ca rel=\"nofollow\"\u003e             PMID:                        26722522            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that notum and glypican-1 and glypican-3 gene expression during colorectal cancer (CRC) development and present evidence to suggest them as potential new biomarkers of CRC pathogenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26517809            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPC3 expression was measured in hepatocellular carcinoma at different stages and correlated with prognosis. CK19+\/GPC3+ HCC has the highest risk of intrahepatic metastasis, microvascular invasion, regional lymph node involvement, and distant metastasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26977595            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Review: Glypican-3 is a highly specific biomarker for the diagnosis of hepatocellular carcinoma and a promising therapeutic target.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26256079            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In South Korean hepatocellular carcinoma patients, GPC3 expression was more frequent in hepatocellular carcinoma with aggressive features, but it was not an independent prognostic biomarker.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26764243            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In this meta-analysis, GPC3 was found to be acceptable as a serum marker for the diagnosis of hepatocellular carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26502856            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPC3 may be a candidate marker for detecting lung squamous cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26345955            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            study suggests that GPC3 is involved in HCC cell migration and motility through HS chain-mediated cooperation with the HGF\/Met pathway, showing how HS targeting has potential therapeutic implications for liver cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        26332121            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            potential role of GPC3 in urothelial carcinogenesis warrants further investigation, especially the potential use of Glypican-3 for therapeutic and diagnostic purposes            \u003ca rel=\"nofollow\"\u003e             PMID:                        25896897            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Downregulation of glypican-3 expression increases migration, invasion, and tumorigenicity of ovarian cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25967456            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPC3 expression is an independent prognostic factor for postoperative hepatocellular carcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        25432695            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Identify a GPC3-specific T-cell receptor. Expression of this receptor by T cells allows them to recognize and kill GPC3-positive hepatoma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26052074            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression of glypican-3 is associated hepatoblastoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25735325            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPC3 and E-cadherin expressions are not independent prognostic factors in CRC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25619476            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In HCC patients, sGPC3N levels were significantly increased (mean\/median, 405.16\/236.19 pg mL(-1) ) compared to healthy controls (p \u0026lt; 0.0001), and 60% of HCC cases (69\/115) showed sGPC3N levels that were higher than the upper normal limit.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25784484            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPC3 contributes to hepatocellular carcinoma progression and metastasis through impacting epithelial-mesenchymal transition of cancer cells, and the effects of GPC3 are associated with ERK activation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25572615            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Most cases of hepatoblastoma and yolk sac tumor, and some cases of other tumors were found to express GPC3. On the other hand, GPC3 was physiologically expressed during the fetal and neoinfantile period under 1 year of age.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25344940            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            OPN, SPINK1, GPC3 and KNPA2 were significantly over-expressed in HCC tissues. These genes may be useful in developing future biomarkers and therapeutic strategies for HCC            \u003ca rel=\"nofollow\"\u003e             PMID:                        25862856            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that zinc-fingers and homeoboxes 2 (ZHX2) suppresses glypican 3 (GPC3) transcription by binding with its core promoter.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25195714            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            propose that the structural changes generated by the lack of cleavage determine a change in the sulfation of the HS chains and that these hypersulfated chains mediate the interaction of the mutant GPC3 with Ptc            \u003ca rel=\"nofollow\"\u003e             PMID:                        25653284            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            GPC3 is associated with the HCC cell biological behavior.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25270552            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that the triple stain of reticulin, glypican-3, and glutamine synthetae is useful in the differentiation of hepatocellular carcinoma, hepatic adenoma, and focal nodular hyperplasia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25822763            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data shows that GPC3 gene expression is downregulated in primary clear cell renal cell carcinoma; its overexpression arrest cells in G1 phase suggesting its role as tumor suppressor in clear cell renal cell carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25168166            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrated that highly expression of GPC3 could enrich hepatocellular carcinoma -related genes' mRNA expression and positive associate with dysplasia in cirrhotic livers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25542894            \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":43915021517025,"sku":"BL-2309NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLbaAJLnYAACN6pbfjjE749_cb5368da-7142-4249-bf77-a83c36251804.jpg?v=1685850734"},{"product_id":"recombinant-human-tslp-rprotein-his-tag-bl-2316np","title":"Recombinant Human TSLP RProtein (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 Cytokine Receptor-Like Factor 2 is produced by our Mammalian expression system and the target gene encoding Gly25­Lys231 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=\"Q9HC73\" target=\"_blank\" href=\"https:\/\/www.uniprot.org\/uniprotkb\/Q9HC73\/entry\"\u003eQ9HC73\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%;\"\u003eCRL2; CRL2cytokine receptor CRL2 precusor; CRLF2; CRLF2Y; CRLM-2; Cytokine receptor-like 2; cytokine receptor-like factor 2; ILXR; IL-XR; P2RY8\/CRLF2 fusion; PCOR1; TSLP R; TSLP receptor; TSLPR\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%;\"\u003eReceptor for thymic stromal lymphopoietin (TSLP). Forms a functional complex with TSLP and IL7R which is capable of stimulating cell proliferation through activation of STAT3 and STAT5. Also activates JAK2 (By similarity). Implicated in the development of the hematopoietic system. TSLP R expression is ubiquitous in the immune and hematopoietic cells, but is up-regulated in Th2-skewed cells. Cells expressing TSLP R alone bind TSLP with low affinity. Co-expression of TSLP R and IL-7 R alpha is required for high-affinity TSLP binding and signal transduction . The TSLP R and IL-7 R alpha are coexpressed primarily on monocytes and dendritic cells and at lower levels in lymphoid cells. TSLP has been shown to induce the release of T cell-attracting chemokines from monocytes and enhance the maturation of CD11c+ dendritic cells.\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%;\"\u003e24.8 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%;\"\u003e35-50 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":43915039178977,"sku":"BL-2316NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLbeAMAzIAACcRYnEZzw890_0db1b526-c12b-49f1-9ea9-3f9243a323e9.jpg?v=1685851198"},{"product_id":"recombinant-human-nectin-4-protein-fc-tag-bl-2326np","title":"Recombinant Human Nectin-4 Protein (C-mFc)","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 Poliovirus Receptor-Related Protein  4 is produced by our Mammalian expression system and the target gene encoding Gly32-Val351 is expressed with a mouse 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%;\"\u003eQ96NY8\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%;\"\u003ePVRL4; Nectin-4; Ig superfamily receptor LNIR; Poliovirus receptor-related protein 4; PRR4; LNIR\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%;\"\u003eNectin-4 (PVRL4) is a type I transmembrane glycoprotein which belongs to the nectin family of Ig superfamily proteins. It contains two Ig-like C2-type domains and one Ig-like V-type domain. PVRL4 seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with nectin-1. It does not act as receptor for alpha-herpesvirus entry into cells. It is predominantly expressed in placenta, the embryo and breast carcinoma. But it is not detected in normal breast epithelium. The soluble form is produced by proteolytic cleavage at the cell surface (shedding), probably by ADAM17. Mutations in this gene are the cause of ectodermal dysplasia-syndactyly syndrome type 1, an autosomal recessive disorder.\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%;\"\u003e60.7 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%;\"\u003e80-90 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%;\"\u003eSeems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. Does not act as receptor for alpha-herpesvirus entry into cells.; (Microbial infection) Acts as a receptor for measles virus.\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. Cell junction, adherens junction. Note=Colocalizes with AFDN at cadherin-based adherens junctions (PubMed:11544254).; [Processed poliovirus receptor-related protein 4]: Secreted. Note=The secreted form is found in breast tumor patients (PubMed:15784625).\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%;\"\u003eNectin 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            19688           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            609607           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:81607           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000356991           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        28778498            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Nectin-4 promotes cell-cell adhesion\/aggregation, migration, and proliferation of ovarian tumor cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28038455            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Nectin-4 is not only a BCSC marker but also a breast cancer metastasis marker            \u003ca rel=\"nofollow\"\u003e             PMID:                        28600142            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study suggests that PVRL4 is post-transcriptionally regulated by miR-128 and miR-31.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27507538            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High Nectin-4 expression is associated with neoplasms.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27013195            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We show that Measles virus gains entry into MCF7, DLD-1, and HTB-20 cancer cells through a PVRL4-mediated macropinocytosis pathway and identified the typical cellular GTPase and kinase involved.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28250131            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            nectin-4 serves as a stimulatory co-receptor for the prolactin receptor by regulating the feedback inhibition of SOCS1 in the JAK2-STAT5a signaling pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        28258213            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Nectin-4 is both a new promising prognostic biomarker and specific therapeutic target for Triple-negative breast cancers            \u003ca rel=\"nofollow\"\u003e             PMID:                        27998973            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ADAM17 and ADAM10 cleave Nectin-4 and release soluble Nectin-4 (sN4).            \u003ca rel=\"nofollow\"\u003e             PMID:                        28232483            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The data presented in this study suggested that nectin-4 may be a therapeutic target for systemic lupus erythematous through affecting the cell apoptosis            \u003ca rel=\"nofollow\"\u003e             PMID:                        26617807            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Nectin-4 is critical for gallbladder cancer cell progression via PI3K\/AKT pathway activation of Rac1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26949052            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Nectin-4 expression, when compared with control group, was higher in endometriotic lesions of patients having ovarian endometriosis and peritoneal endometriosis. This difference was significant in the endometrium of patients having endometriosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27328518            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Transformation of breast cancer cells is dependent on PVRL4.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23682311            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Nectin-4 is a significant prognostic predictor, and may play a critical role in pancreatic cancer. Nectin-4 may be novel therapeutic target for pancreatic cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25888293            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In airway epithelial cells, measles virus spread requires the nectin-4\/afadin complex and is based on cytoplasm transfer between columnar cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25926640            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present study described clinical investigation of the EDSS1 identified in a large consanguineous family; DNA sequence analysis revealed a novel homozygous nonsense mutation (181C\u0026gt;T, p.Asp61*) in the PVRL4 gene.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25529316            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ovarian tissue expression and serum nectin 4 appear to be potential markers in ovarian cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25019423            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors show that the same key residues in the BC and FG loops of nectin-4 govern binding to the measles virus attachment protein hemagglutinin (H) and cell entry, nectin-4 homodimerization, and heterodimerization with nectin-1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25275122            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            data outline a synergistic action of nectin-1 and -4 in the early steps of AJ formation and implicate this interaction in modulating the Rac1 signaling pathway            \u003ca rel=\"nofollow\"\u003e             PMID:                        24577405            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ablation of nectin4 binding compromises CD46 usage by a hybrid vesicular stomatitis virus\/measles virus.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24335299            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Thus, while nectin-4 and CD46 interact functionally with the measles virus H protein beta4-beta5 hydrophobic groove, SLAM merely covers it.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23760251            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that expression of nectin-4 is up-regulated in eutopic endometrium of patients with endometriosis compared with control subjects.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22926846            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We show that human nectin4 is fully functional as a canince distemper virus receptor.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23174504            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            structure of the membrane-distal domain of nectin-4 in complex with measles virus hemagglutinin (MV-H; structure shows nectin-4 binds the MV-H beta4-beta5 groove exclusively via its N-terminal IgV domain; the contact interface is dominated by hydrophobic interactions            \u003ca rel=\"nofollow\"\u003e             PMID:                        23202587            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            crystals of nectin-4 diffracted to 1.8 A resolution and belonged to space group P2(1), with unit-cell parameters a = 33.1, b = 51.7, c = 56.9 A, beta = 94.7 degrees            \u003ca rel=\"nofollow\"\u003e             PMID:                        22869128            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            measles virus targets nectin-4 to emerge in the airways            \u003ca rel=\"nofollow\"\u003e             PMID:                        22048310            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Measles virus infection reduced PVRL4 surface expression in MCF7 cells, a property that is characteristic of receptor-associated viral infections.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21901103            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings of study suggest that increased expression of Nectin-4 may indicate a worse prognosis in breast cancer patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21526486            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Sequence analysis revealed a homozygous missense mutation (c.635C\u0026gt;G; p.Pro212Arg) in the recently reported PVRL4 gene causing EDSS1            \u003ca rel=\"nofollow\"\u003e             PMID:                        21346770            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ectoderma dysplasia-syndactyly syndrome. Second example of \"nectinopathy\".            \u003ca rel=\"nofollow\"\u003e             PMID:                        21333831            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            nectin 4 may serve as a potential biomarker that helps discriminate benign gynecologic diseases from ovarian cancer in a panel with CA125.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20959669            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ectodermal dysplasia-syndactyly syndrome is the second known \"nectinopathy\" caused by mutations in a nectin adhesion molecule.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20691405            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the active form of TACE is overexpressed in breast tumors and may indicate that TACE is responsible for Nectin-4 shedding not only in vitro but also in vivo            \u003ca rel=\"nofollow\"\u003e             PMID:                        15784625            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Nectin-4 was not detected in normal breast epithelium; by contrast Nectin-4 was expressed in ductal breast carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17474988            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Nectin-4 might play a significant role in lung carcinogenesis, and it should be a new candidate serum and tissue biomarker, as well as a therapeutic target.            \u003ca rel=\"nofollow\"\u003e             PMID:                        19679554            \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":43915092590817,"sku":"BL-2326NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLRqAFZ3qAACFwy6BG8A013_c7831ca9-51e0-44b5-bbb1-6d58a864a278.jpg?v=1685852944"},{"product_id":"recombinant-human-acvr2b-protein-his-fc-tag-bl-2364np","title":"Recombinant Human ACVR2B Protein (C-Fc-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 Activin Receptor Type 2B is produced by our Mammalian expression system and the target gene encoding Ser19-Thr134 is expressed with a human IgG1 Fc, 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%;\"\u003eQ13705\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%;\"\u003eActivin Receptor Type-2B; Activin Receptor Type IIB; ACTR-IIB; ACVR2B\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%;\"\u003eActivin proteins that belong to the transforming growth factor-beta (TGF-β) superfamily, exert their biological actions by binding to heteromeric receptor complexes of type I and type II serine\/threonine kinase receptors. On ligand binding, type I and II receptors form a stable complex, resulting in phosphorylation of type I receptors by type II receptors with constitutive kinase activity, and subsequently initiates the activation of downstream molecules including the endogenous Smads. ActRIIB, also known as ActRIIB, is a type II receptor containing an extracellular domain (ECD), a transmembrane segment, and a cytoplasmic region that includes the kinase domain. ActRIIB is a receptor for activin A, activin B and inhibin A. Multiple ActRIIB isoforms can also be generated, which bind activin isoforms with different affinities.\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%;\"\u003e41.3 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 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%;\"\u003eTransmembrane serine\/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine\/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A\/INHBA, activin-B\/INHBB as well as inhibin-A\/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor.\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.\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            174           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            602730           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:93           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000340361           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        26848890            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            ActR-IIB is expressed in male germ cells and Sertoli cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26289399            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We found that the AAAAA, AGGAG, and AGGGA haplotypes in ACVR2B were associated with susceptibility to Premature Ovarian Failure when they also had at least one CATAG haplotype in ADAMTS19.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25051287            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-21 interacts directly with the 3'-untranslated region of ACVR2B mRNA. Mechanical stretch suppressed ACVR2B protein levels in periodontal ligament stem cells. Gain- and loss of function of ACVR2B mediated the osteogenic differentiation of PDLSCs.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25203845            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Activin type IIB receptors are clearly demonstrable throughout the adult human hypothalamus and basal forebrain.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22296042            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            After eccentric exercise, postmenopausal women not using hormone therapy (HT) expressed lower levels of ActRIIb while postmenopausal women using HT showed a heightened response.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22395277            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The interaction between all five miRNAs and ACVR2B was verified by an in vitro assay.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22431721            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mutations in Activin A Receptor Type IIB were identified in 4 of the 47 patients (8.5%) with heterotaxy syndrome.  Our results expand the mutation spectrum of monogenic heterotaxy syndrome with associated cardiac anomalies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21864452            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            discussion of crystal structure of kinase domain of ActRIIB; structural analysis may be of help in developing selective inhibitors [REVIEW]            \u003ca rel=\"nofollow\"\u003e             PMID:                        21353874            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Inhibition of negative regulators of skeletal muscle by a soluble form of activin type IIB receptor (ACE-031) increases muscle mass independent of fiber-type expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        20466801            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            analysis of expression and cellular compartmentalization of the activin receptors ActRIIA, ActRIIB and ActRIB, the inhibin co-receptor (betaglycan), and activin signaling proteins Smads 2, 3 and 4, and growth regulatory role during lactation            \u003ca rel=\"nofollow\"\u003e             PMID:                        12782414            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            activin signaling via type II receptors requires a specific sequence for ALK4 binding            \u003ca rel=\"nofollow\"\u003e             PMID:                        15123686            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results indicate that haplotype structure at the ACVR2B and follistatin loci may contribute to interindividual variation in skeletal muscle mass and strength, although these data indicate sex-specific relationships.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17347381            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The high-resolution structure of human ActRIIB kinase domain in complex with adenine establishes the conserved bilobal architecture consistent with all other catalytic kinase domains.            \u003ca rel=\"nofollow\"\u003e             PMID:                        17893364            \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":43915082039521,"sku":"BL-2364NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLbyADAGQAADQdFR3FzY938_0f23ae4b-422d-41c3-a53a-e76044a34387.jpg?v=1685852502"},{"product_id":"recombinant-human-her2-protein-fc-tag-bl-2371np","title":"Recombinant Human HER2 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 Tyrosine-protein Kinase ErbB-2 is produced by our Mammalian expression system and the target gene encoding Thr23-Thr652 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%;\"\u003eP04626\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%;\"\u003eReceptor tyrosine-protein kinase erbB-2; Metastatic lymph node gene 19 protein; Proto-oncogene Neu; Tyrosine kinase-type cell surface receptor HER2; ERBB2; MLN19; NGL; TKR1\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 epidermal growth factor receptor 2 (HER2) is a type of membrane glycoprotein, and belongs to the epidermal growth factor (EGF) receptor family. HER2 plays a key role in development, cell proliferation and differentiation. HER2 has been reported to associate with malignancy and a poor prognosis in numerous carcinomas, including breast, prostate, ovarian, lung cancers and so on. HER2 is activated by dimerization and not activated by EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity.It is heterodimer with EGFR, ERBB3 and ERBB4. HER2 associates with the 5'-TCAAATTC-3' sequence in the PTGS2\/COX-2 promoter and activates its transcription. It implicated in transcriptional activation of CDKN1A and the function of the protein involves STAT3 and SRC. And also it involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth.\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%;\"\u003e96.5 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%;\"\u003e120-145 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%;\"\u003eProtein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization.; In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2\/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell 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%;\"\u003e[Isoform 1]: Cell membrane; Single-pass type I membrane protein. Early endosome. Cytoplasm, perinuclear region. Nucleus.; [Isoform 2]: Cytoplasm. Nucleus.; [Isoform 3]: Cytoplasm. 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%;\"\u003eProtein kinase superfamily, Tyr protein kinase family, EGF 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            3430           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            137800           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:2064           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000269571           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30340409            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Authors showed that mRNA and protein levels of COX2 and HER2 were upregulated in CRC compared with the adjacent tissues. COX2 protein levels and nuclear COX2 expression were correlated with a poor prognosis of CRC patients. COX2 expression was positively associated with HER2 expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29873317            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In patients with HER2-positive advanced breast cancer who have been heavily pretreated with anti-HER2 agents and cytotoxic chemotherapy, trastuzumab emtansine (T-DM1) is well tolerated and provided a meaningful progression-free survival of 6 months and an overall survival that has not been reached.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29326401            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The expression of C-Met and HER2 protein in lung adenocarcinoma is highly correlated, and whether it is synergistic in the targeted therapy of lung adenocarcinoma deserves further study.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29400000            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Although ST6GalI overexpression increased HER2 sialylation, corresponding to decreased HER2 phosphorylation, high alpha2,6sialylation enhanced Akt and ERK phosphorylation levels compared to those in the vector cell line; ST6GalI knockdown had the opposite effects. Collectively, these results implicated a functional role of ST6GalI in promoting tumor cell progression and trastuzumab resistance.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30226606            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study demonstrate that the miR-495 exerts promotive effects on GC chemosensitivity via inactivation of the mTOR signaling pathway by suppressing ERBB2. The study provides reliable evidence supporting the use of miR-495 as a novel potential target in the chemotherapy of GC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30147110            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In early breast cancer, PIK3CA mutations seem to identify HER2+ patients who are less likely to reach pCR. The clinical implications of PIK3CA mutations tend to vary between exon 9 and exon 20. This mechanism should be explored in further studies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29575819            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HER2 and HER3 expression was detected in 22.2% and 86.1% of samples, respectively. The frequency of EGFR mutation was 45.7% and was not significantly different between stage 0 and IA1 (40.0% and 48.0%, respectively), suggesting that EGFR mutation does not correlate with cancer progression from stage 0 to IA1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29473311            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            It has been demonstrated that the heterogeneity of HER2 expression accelerated the development of metastases which caused the poor survival of mice with heterogeneous HER2 expression (HER2-60).            \u003ca rel=\"nofollow\"\u003e             PMID:                        30042341            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Her-2\/neu amplification increases with increasing grade of breast cancer. A high proportion of Her-2\/neu gene amplified cases indicates aggressive disease in that area and need for FISH testing on large scale, which is the gold standard for equivocal cases on immunohistochemistry.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30060783            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that the major mechanism is the ability of p140Cap to interfere with ERBB2-dependent activation of Rac GTPase-controlled circuitries.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28300085            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study showed the expression levels of Gli1 and HER2 were significantly higher in gastric cancer, and they are positively related. HER2 may regulate Gli1 by Akt-mTOR-p70S6K pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29321573            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The combination of immunohistochemical expression of BRCA1, ER, PR, and HER-2\/neu and clinicopathological details may be helpful in predicting the individuals more likely to carry BRCA1 mutations and thus selecting the candidate and family members for genetic screening for BRCA1 mutations.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29567881            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In the current settings, HER2\/neu is not found to be a prognostic marker in head-and-neck cancers.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30004046            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results may be commented as HE4 expression rises in patients with HER2\/neu amplification.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30004048            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HER2 gene amplification in circulating tumor DNA predicts HER2-positive breast neoplasms resistance to trastuzumab emtansine.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29700710            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Statistical analysis performed in this study did not reveal the significant relationship between HER2 overexpression on the tumor cells and microvessel density in the tumor stroma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30334990            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data showed a high rate of discordance in matched pairs of primary tumors and metastases, suggesting that the accurate evaluation of proto-oncogene protein HER-2 (HER2) status is essential before any therapeutic decision.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30203148            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HER2 gene amplification occurred during the early stages of gastric cancer and showed heterogeneity in several cases. HER2 gene amplification may be involved in tumor progression in early gastric cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30120594            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Activating HER2 mutation is present in about 3% of bone metastases from breast cancers, with significantly higher rates in the pleomorphic subtype of lobular cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30094493            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggested a possible link between tRNALeu overexpression and RSK1\/MSK2 activation and ErbB2\/ErbB3 signaling, especially in breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28816616            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High HER2 expression is associated with metastasis in breast Cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29187405            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study confirmed that biosimilar trastuzumab improves the overall response rate when combined with chemotherapy for HER2+ breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        30082554            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The Authors reveal a gender difference in the prognostic value of concomitant AIB1 and HER2 copy number gain (CNG) in glioma patients which were barely noticed before. These observations indicated that genetic alterations synergistic with essential respects of sex determination influence glioma biology and patients outcomes.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30153912            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The survival rates in this study are equal to the documented global rates; nodal disease burden emerged as the most important prognostic factor. In addition, in EBCs, a lack of hormone receptor expression and in LABC, Her2neu overexpression appear to worsen the outcome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30147088            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results showed that HER2 and FGFR2 are regulated by DDX6 at the post-transcriptional step in gastric cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29987267            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HER2 overexpression is associated with Gastric Cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29938472            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ERBB2 oncogene at 17q12 is susceptible to palindromic gene amplification in HER2-positive breast tumors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28211519            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results show mutation in ERBB2-exon17 was associated with worse survival results in patients with pancreatic neoplasm. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        30227250            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High HER2 expression and Gene Amplification is associated with Upper Tract Urothelial Carcinomas.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28755093            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High HER2 expression is associated with invasion and lymph node metastasis in gastric cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29970682            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Basal HER2 phenotype showed poor DFS, but equivalent pCR rate after concurrent neo-adjuvant chemotherapy with trastuzumab. A different treatment approach to basal-HER2 type is needed even for cases that achieved adequate clinical response after neo-adjuvant chemotherapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29971625            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In the largest series reported to date, patients with HER2-amplified m17 cancers treated with trastuzumab have outcomes comparable to patients from the large phase III adjuvant trastuzumab trials who were HER2-positive, supporting the critical role of HER2-directed therapy in this patient population.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28986743            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The interplay of dual MET\/HER2 overexpression in the AKT and ERK pathways for esophageal cancer is described. Therefore, combination therapy could be a novel strategy for EAC with amplification of both MET and HER2.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29223420            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study provides evidence that the hostile environment developed in spheroids has a key role in the acquisition of resistance to Trastuzumab and is associated with an increase in the number of breast cancer stem cells as well as a modulation in HER2 expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28722778            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A major finding of our study is that one out of five (20%) patients with breast cancer BM had a receptor discrepancy between the primary tumor and the subsequent BM, with loss of hormone receptors (ER and\/or PR) expression, and gain of HER2 overexpression as the most commonly observed changes            \u003ca rel=\"nofollow\"\u003e             PMID:                        28975433            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High HER2 expression is associated with Gastric Adenocarcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29802704            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Absence of HER2 Expression of Circulating Tumor Cells is associated with Non-Metastatic Esophageal Cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30275185            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HER2 positivity was found in a minority of rectal cancer patients and was not significantly associated with clinicopathologic and molecular characteristics.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30056472            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study discovered a novel enhancer HER2 gene body enhancer (HGE) in the 3' gene body of HER2. The HGE activates promoters 1 and 2 in trans., and hence the TFAP2C-mediated transcriptional induction of HER2 expression in breast cancer samples.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29035388            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ctDNA gene mutation profiles differed among HR\/HER2 subtypes of metastatic breast cancer (MBC) patients. By identifying mutations associated with treatment resistance, we hope to improve therapy selection for MBC patients who received multiline treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29807833            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            It was concluded that miR494 inhibited the cancer initiating cells phenotype and reversed resistance to lapatinib by inhibiting FGFR2 in HER2positive gastric cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29786108            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HER2 overexpression was evident in nearly 25% of the Malaysian patients with locally advanced or metastatic gastric cancer. The overexpression correlated significantly with male gender and diffuse-type tumors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28124769            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There was a statistically significant association between positive p95-HER2 expression and negative hormonal receptors expression (p=0.004), high Ki-67 expression (p\u0026lt;0.001) and development of visceral metastasis            \u003ca rel=\"nofollow\"\u003e             PMID:                        29779938            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The authors herein prove, for the first time, that the transcriptional repressor Blimp1 is a novel mediator of p130Cas\/ErbB2-mediated invasiveness. Indeed, high Blimp1 expression levels are detected in invasive p130Cas\/ErbB2 cells and correlate with metastatic status in human breast cancer patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28442738            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ERBB2 amplification is driving resistance to erlotinib in lung adenocarcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28870636            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results showed that combining the results of IHC and FISH according to the HER2 testing algorithm is a useful method for accurately evaluating HER2-positive EMPD.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29744813            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Because the concordance rates of HER2 IHC score 2\/3+ cases were lower than that of HER2 IHC score 0\/1+ cases, further studies for detailed analysis criteria for HER2 IHC score 2+ or 3+ are required.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28478639            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            HER2 interacts with Beclin 1 in breast cancer cells and inhibits autophagy. Mice with increased basal autophagy due to a genetically engineered mutation in Becn1 are protected from human HER2-driven mammary tumorigenesis. HER2-mediated inhibition of Beclin 1 and autophagy likely contributes to HER2-mediated tumorigenesis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29610308            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings suggest that early-stage morphological alterations of HER2-positive BC cells during cancer progression can occur in a physical and signalling-independent manner.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27599456            \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":43915026235617,"sku":"BL-2371NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLb2AfmwhAAClH4PcNAU178_ac048eaa-00be-4e32-86fb-18ba2780aafa.jpg?v=1685850838"},{"product_id":"biotinylated-human-egfr-viii-protein-his-avi-tag-bl-2394np","title":"Biotinylated Human EGFR vIII Protein (C-6His-Avi)","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 Epidermal Growth Factor Receptor\/Receptor Tyrosine Protein Kinase ErbB1 is produced by our Mammalian expression system and the target gene encoding Leu25-Ser378 is expressed with a 6His, Avi 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=\"NP_001333870\" target=\"_blank\" href=\"https:\/\/www.ncbi.nlm.nih.gov\/protein\/NP_001333870\"\u003eNP_001333870\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%;\"\u003eEpidermal growth factor receptor; EGFR; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1; EGFR\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 EGFR subfamily of receptor tyrosine kinases is composed of EGFR, ErbB2, ErbB3 and ErbB4. The EGFR shares 43% - 44% aa sequence identity with the ECD of human EGFR subfamily. All these family members are type I transmembrane glycoproteins with an extracellular ligand binding domain. The extracellular ligand binding domain is containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain. Ligand binding could induce EGFR homodimerization and heterodimerization with ErbB2, resulting in cell signaling, heterodimerization tyrosine phosphorylation and kinase activation. It can bind EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, HB-EGF, epigen, and so on. Its signaling regulates multiple biological functions including cell proliferation, differentiation, motility, and apoptosis. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR is overexpressed in different tumors. Several anti-cancer drugs use EGFR as target.\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%;\"\u003e41.5 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%;\"\u003e60-90 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":"20μg","offer_id":43915209081057,"sku":"BL-2394NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLb-ACoImAADIOJew8ss021.jpg?v=1685852083"},{"product_id":"biotinylated-human-epcam-protein-his-avi-tag-bl-2395np","title":"Biotinylated Human EpCAM Protein (C-6His-Avi)","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 Epithelial Cell Adhesion Molecule is produced by our Mammalian expression system and the target gene encoding Gln24-Lys265 is expressed with a 6His, Avi 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%;\"\u003eAAH14785.1\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%;\"\u003eEpithelial Cell Adhesion Molecule; Ep-CAM; Adenocarcinoma-Associated Antigen; Cell Surface Glycoprotein Trop-1; Epithelial Cell Surface Antigen; Epithelial Glycoprotein; EGP; Epithelial Glycoprotein 314; EGP314; hEGP314; KSA; Tumor-Associated Calcium Signal Transducer 1; CD326; EPCAM\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%;\"\u003eEpithelial Cell Adhesion Molecule (EpCAM) is a signal type I transmembrane glycoprotein that belongs to the EPCAM family. EpCAM is composed of an extracellular domain with one thyroglobulin type-1 domain, a transmembrane domain and a cytoplasmic domain. EpCAM is found on the surface of adenocarcinoma, but not on mesodermal or neural cell membranes. The EpCAM molecule has been shown to function as a homophilic Ca2+ independent adhesion molecule. It may act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium as an immunological barrier providing the first line of defense against infection. Defects in EPCAM are a cause of hereditary non-polyposis colorectal cancer type 8 (HNPCC8) and diarrhea type 5 (DIAR5). EpCAM plays a role in embryonic stem cells proliferation and differentiation; it up-regulates the expression of FABP5, MYC and Cyclin A and Cyclin E. It is highly and selectively expressed by undifferentiated embryonic stem cells.\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%;\"\u003e30.2 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%;\"\u003e35-50 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 \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 act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E.\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%;\"\u003eLateral cell membrane; Single-pass type I membrane protein. Cell junction, tight junction.\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%;\"\u003eEPCAM 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            11529           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            185535           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4072           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000263735           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29352248            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Functions of EpCAM in physiological processes and diseases (Review).            \u003ca rel=\"nofollow\"\u003e             PMID:                        30015855            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our results suggest that GA733-2-Fc conjugated to ER-retention motif KDEL is a more efficient antigen to prevent tumor growth induced by colorectal carcinoma and minimize an allergic response.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30249898            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            extracellular vesicles tend to localize in the intestinal tract associated with epithelial cell adhesion molecule            \u003ca rel=\"nofollow\"\u003e             PMID:                        27721471            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Overexpression of EpCAM and melan-A is associated with malignant melanoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29076925            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Quercetin suppressed breast cancer stem cell proliferation, self-renewal, and invasiveness. It also lowered the expression levels of proteins related to tumorigenesis and cancer progression, such as aldehyde dehydrogenase 1A1, C-X-C chemokine receptor type 4, mucin 1, and epithelial cell adhesion molecules.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29353288            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Adenocarcinomas showed significantly higher staining scores of both VEGF and alphaSMA than squamous cell carcinomas did. In 42 cases of high CD31 score, five-year survival rate (87%) of patients with lung cancer showing mature tumor vessels was significantly better than that (69%) of patients with immature tumor vessels            \u003ca rel=\"nofollow\"\u003e             PMID:                        29970536            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            New EPCAM founder deletion causing Lynch Syndrome has been described in Polish population.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28369810            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The novel and updated insights in the EpCAM field by simplifying the understanding of the biological role of this fascinating molecule, and by showing the promising therapeutic tools that have been developed by various approaches which use antibodies and vaccines for different cancer types for the clear purpose of improving patient outcome. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        29759567            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This is the first demonstration that the low sensitivity of CellSearch(R) to detect circulating tumor cells in colorectal cancer patients is not due to the lack of EpCAM            \u003ca rel=\"nofollow\"\u003e             PMID:                        28604994            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings indicate that epithelial cell adhesion molecule (EpCAM) can be used as an additional distinction-marker for cystic lesions of the sellar region.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27431859            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that epithelial cell adhesion molecule (EpCAM) show high tumor distinctiveness.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28820475            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Low expressions of Oct4-EpCAM in IHC and CD133 in qPCR may reveal roles in gastric cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        27557490            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EpCAM expression contributes to tumor resistance to chemotherapy in patients with ovarian cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28574829            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present findings suggest that Ep-CAM expression may be associated with CRC carcinogenesis, while the loss of Ep-CAM expression is correlated with the progression, metastasis, and poor prognosis of CRC. Ep-CAM expression may be a useful biomarker for the clinical diagnosis of CRC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28558958            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the present study identified a positive correlation between EpCAM and COX-2 expression in breast cancer cell lines and tissue specimens. EpCAM and COX-2 were associated with the prognosis of breast cancer patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28393249            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CD133+ cells were genetically heterogeneous among patients without any defined profile compared to CD133-\/EpCAM+ cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28347289            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Combining the targets E-cadherin, epithelial membrane antigen (EMA), human epidermal growth receptor type 2 (Her2\/neu), carcinoembryonic antigen (CEA) resulted in nearly 100% detection of ductal ovarian metastases, whereas the combination of EMA, Her2\/neu and epithelial cell adhesion molecule (EpCAM) was most suitable to detect lobular ovarian metastases.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28327103            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Whole-genome sequencing identified the homozygous intronic variant EPCAM c.556-14A\u0026gt;G, considered explanatory for the patient's intractable diarrhea and providing a diagnosis of congenital tufting enteropathy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28701297            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Low EPCAM expression is associated with colorectal carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26528695            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our study provided clinical evidence for EpCAM intracellular domain as a predictor of cancer development in patients with oral dysplasia and recurrence in oral squamous cell carcinoma patients            \u003ca rel=\"nofollow\"\u003e             PMID:                        27421772            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Elevated epithelial cell adhesion molecule EpCAM (mRNA+) CTC and Treg\/CD4(+) levels were associated with early recurrence of hepatocellular carcinoma (HCC), indicative of poor clinical outcome.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27439521            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Observations provide important insights into the regulation of EpCAM expression during EMT, demonstrate an unexpected role for EpCAM in the regulation of ERK and define a novel double-negative feedback loop between EpCAM and ERK that contributes to the regulation of EMT.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28192403            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study shows the potential of an EpCAM specific NIR-fluorescent agent in combination with a clinically validated intraoperative imaging system to visualize various tumours during surgery.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27842504            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The studies identified the characteristics and function of EpCAM glycosylation sites on breast cancer cell adhesion.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28315854            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results identify EpCAM as a substrate of matriptase and link HAI-2, matriptase, EpCAM, and claudin-7 in a functionally important pathway that causes disease when it is dysregulated.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28094766            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The EpCAM aptamer conjugated NCS showed specificity to EpCAM-positive cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28668853            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Pseudomyxoma peritonei ubiquitously express CEA and EpCAM.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27038681            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            relationship between EpCAM-regulated transcription and altered biophysical properties of cells that promoteepithelial-mesenchymal transition (EMT) in advanced endometrial cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27569206            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            used a next generation sequencing (NGS) approach. NY-SAR-35 expression induced growth, proliferation, metastasis, and stemness genes, as indicated by the up-regulations of CXCR4, EpCAM, CD133, and CD44, at the mRNA and protein levels            \u003ca rel=\"nofollow\"\u003e             PMID:                        28126340            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These results indicate that adipocyte-secreted factors might regulate cancer stem cell behavior through several signaling molecules including c-Met, STAT3 and ERK1\/2 and inhibition of these signaling pathways offer novel strategies in targeting the effect of adipose-derived cytokines in cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27131739            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The meta-analysis demonstrated that the expression of EpCAM in the gastric cancer group was greater than that in the control group. Moreover, EpCAM overexpression was associated with larger tumour size, lymphnode metastasis and worse prognosis in gastric cancer. [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        28403178            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            expression of EpCAM(MT) is associated with a more aggressive phenotype and predicts poor survival in patients with colorectal cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26996277            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Higher levels of epithelial cell adhesion molecule (EpCAM) in breast cancer may be associated with poor response to Neoadjuvant chemotherapy (NAC) via a potential chemoresistant effect.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27041736            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            By monitoring the change of fluorescence signal, the target EpCAM protein could be detected sensitively and selectively with a linear detection range from 3nM to 54nM and limit of detection (LOD) around 450pM. In addition, this nanobiosensor has been successfully used for EpCAM-expressed breast cancer MCF-7 cell detection            \u003ca rel=\"nofollow\"\u003e             PMID:                        27614683            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EpCAM, CD44 and CD133 expression could be candidate markers for Barrett esophagus disease progression            \u003ca rel=\"nofollow\"\u003e             PMID:                        28216140            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These findings are important for a better understanding of epithelial cell adhesion molecule apoptosis regulation and suggest epithelial cell adhesion molecule as a potential target for the treatment of breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28349835            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            that epithelial cell adhesion molecule showed different expression pattern among salivary gland neoplasms and in different grades of mucoepidermoid carcinomas            \u003ca rel=\"nofollow\"\u003e             PMID:                        27649957            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we concluded that the peptide could be a better supplement to the EpCAM antibody for capturing Circulating tumor cells (CTCs) in microfluidic system with broader spectrum            \u003ca rel=\"nofollow\"\u003e             PMID:                        27818051            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study presented a molecular characterization of congenital tufting enteropathy Italian patients, and identified three mutations in the EpCAM gene            \u003ca rel=\"nofollow\"\u003e             PMID:                        26684320            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EpCAM serves as a potential biomarker of prognostic significance that could be used to identify oral squamous cell carcinoma patients at high risk and to predict patient survival            \u003ca rel=\"nofollow\"\u003e             PMID:                        26401964            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Findings show that the EGF-like domain of EpCAM is cleaved off in cancer cells which have undergone epithelial-mesenchymal transition.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26775583            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Based on these results, it can be concluded that EpCAM is suitable for use as an EC biomarker, therapeutic target, and effective parameter for tumor transfer and prognosis evaluation by aptamer SYL3C staining            \u003ca rel=\"nofollow\"\u003e             PMID:                        26687301            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CHD4 was abundantly expressed in EpCAM(+) hepatocellular carcinoma with expression of hepatic stem cell markers and poor prognosis in two independent cohorts.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26095183            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Flow cytometry assay showed doxorubicin exposure decreased EpCAM positive cell quantities in three HCC cell lines. EpCAM siRNA knock-down attenuated cell mortality after doxorubicin exposure            \u003ca rel=\"nofollow\"\u003e             PMID:                        26984381            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            EpCAM based capture detects and recovers circulating tumor cells from all subtypes of breast cancer except those low claudin expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26556851            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Increased Expression of EPCAM mRNA is associated with Recurrence After Curative Resection of Hepatocellular Carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25791790            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We revealed a new molecular mechanism of MTA1-mediated invasion and metastasis in lung cancer through downstream target EpCAM, and interfering with EpCAM function may be a novel therapeutic strategy for treatment of MTA1-overexpressing lung carcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        26698569            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            knockdown of EpCAM can inhibition breast cancer cell growth and metastasis via inhibition of the Ras\/Raf\/ERK signaling pathway and MMP-9            \u003ca rel=\"nofollow\"\u003e             PMID:                        26356670            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate that the anti-epithelial cell adhesion molecule (EpCAM) monoclonal antibodie can potentially be used for cancer-targeted therapy.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26317650            \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":43915193549025,"sku":"BL-2395NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLb-ARzzBAADMiltCLlE478.jpg?v=1685851520"},{"product_id":"biotinylated-human-mesothelin-protein-his-avi-tag-bl-2396np","title":"Biotinylated Human Mesothelin Protein (C-6His-Avi)","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 Mesothelin  is produced by our Mammalian expression system and the target gene encoding Glu296-Ser598 is expressed with a 6His, Avi 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%;\"\u003eAAH09272.1\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%;\"\u003eMegakaryocyte potentiating factor; mesothelin; Pre-pro-megakaryocyte-potentiating factor; soluble MPF mesothelin related protein; CAK1; MPF; MSLN; SMR; CAK1; CAK1 antigen\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%;\"\u003eMesothelin is a cell surface glycoprotein whose expression is limited to mesothelial cells of the serosa (pleura, pericardium, and peritoneum) and epithelial cells of the trachea, tonsils, fallopian tube, and kidneys. Mesothelin plays an important role in cell survival, proliferation, migration, invasion, tumor progression, and resistance to chemotherapy. The overexpression of mesothelin can activate NF-κB and signal transducer and activator of transcription 3 (Stat3), inhibit apoptotic signaling and TNF-α-induced apoptosis, and accelerate the G1–S transition. Mesothelin is also found overexpressed in various cancers, including malignant mesothelioma, pancreatic or ovarian carcinoma, sarcomas and in some gastrointestinal or pulmonary carcinomas. As a result of its limited expression in normal tissues, mesothelin has been reported as an ideal tumor-associated marker for the development of targeted therapy.\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%;\"\u003e36.7 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%;\"\u003e38-60 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%;\"\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%;\"\u003eMembrane-anchored forms may play a role in cellular adhesion.; Megakaryocyte-potentiating factor (MPF) potentiates megakaryocyte colony formation in vitro.\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; Lipid-anchor, GPI-anchor. Golgi apparatus.; [Megakaryocyte-potentiating factor]: Secreted.; [Isoform 3]: 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%;\"\u003eMesothelin 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            7371           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            601051           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:10232           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000372313           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        30319054            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            We have demonstrated that a rising serum mesothelin is a sensitive marker of progression in the follow up of patients with MPM.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29454314            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we engineered variants of the fibronectin type III domain (Fn3) non-antibody protein scaffold to bind to mesothelin with high affinity, using directed evolution and yeast surface display            \u003ca rel=\"nofollow\"\u003e             PMID:                        29738555            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our goal was to stimulate antitumor immunity by combining SS1P or LMB-100 with anti-CTLA-4. We constructed a BALB\/c breast cancer cell line expressing human mesothelin (66C14-M), which was implanted in one or two locations. SS1P or LMB-100 was injected directly into established tumors and anti-CTLA-4 administered i.p. In mice with two tumors, one tumor was injected with immunotoxin and the other was not.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28674083            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mesothelin-targeted immunotoxin RG7787 increases pancreatic cancer cell sensitivity to taxane-mediated killing by increasing taxane-mediated microtubule stability and priming cells for apoptosis by decreasing levels of the pro-survival factor Mcl-1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27999204            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            RG7787 plus nab-paclitaxel is very active against primary human mesothelioma cells in vitro as well as in vivo, with serum mesothelin levels correlating with tumor response. These results indicate that this combination could be useful for treating patients with mesothelioma            \u003ca rel=\"nofollow\"\u003e             PMID:                        27635089            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Efficient growth suppression in pancreatic cancer PDX model by fully human anti-mesothelin CAR-T cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28929447            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mesothelin\/mucin 16 signaling in activated portal fibroblasts regulates cholestatic liver fibrosis.(            \u003ca rel=\"nofollow\"\u003e             PMID:                        28287406            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MiR-21-5p is suggested as novel regulator of MSLN with a possible functional role in cellular growth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28125734            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we report herein that high tumor mesothelin expression predicts a shorter PFS and OS in EOC patients and demonstrates that serum mesothelin predicts local tumor mesothelin expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28160193            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We provide new evidence for the role of MSLN in EMT regulation, tumorigenesis and metastasis. Knockdown of MSLN led to mesenchymal to epithelial transition and less aggressive behavior of lung carcinoma and mesothelioma cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28288645            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MSLN expression increases cell migration and invasion in vitro.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27422997            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SMRP but not FBLN3 has a role in pleural effusions in in malignant pleural mesothelioma            \u003ca rel=\"nofollow\"\u003e             PMID:                        28314308            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High mesothelin expression is associated with malignant pleural mesothelioma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27646775            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Calretinin, D2-40 and mesothelin are aberrantly expressed in a proportion of CRC cases.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27062033            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our results showed that IMP3 immunostaining has a higher sensitivity and specificity than mesothelin for the diagnosis of pancreatic ductal adenocarcinoma. IMP3 and mesothelin may be useful markers in distinguishing neoplastic from reactive lesions of the pancreas in instances where this is impossible by morphology alone in surgical pathology practice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26874572            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results indicate a specific mesothelin-driven tumor uptake of targeted 89zirconium-labeled antibody which visualizes mesothelin expressing pancreatic cancer in real time.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26536664            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that triple-negative breast cancer (TNBC) showed the highest amplification rate (42%) in the basal-like 1 subtype.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26172299            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            There was a trend toward elevation of SMRP values in healthy individuals exposed to asbestos compared to those without exposure. Within asbestosis cases, those with higher profusion scores had higher SMRP values than those with lower profusion scores.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26188910            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High mesothelin expression was strongly associated with mutant KRAS\/wild-type EGFR and poor prognosis in advanced lung cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26028668            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            findings replicate association between rs1057147 and soluble mesothelin related peptide(SMRP)levels; SMRP performance as diagnostic biomarker for malignant pleural mesothelioma improved by considering genotype rs1057147; this polymorphism most likely affects a binding site for miR-611            \u003ca rel=\"nofollow\"\u003e             PMID:                        25436799            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Expression of mesothelin was observed in 42.3% of patients with triple negative breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25776500            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Patients with mesothelin-positive triple negative breast carcinomas (TNBC) were older than patients with mesothelin-negative TNBC, developed more distant metastases with a shorter interval, and had significantly lower overall and disease-free survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25506917            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Delivery of mesothelin-targeted CAR T cells eradicates tumors in mice with pleural malignancies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25378643            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Pleural fluid mesothelin may serve as a marker for pleural malignant mesothelioma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25505814            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Patients with colon cancer had significantly higher mesothelin serum levels than the control groups.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25477701            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mesothelin expression is associated with poor outcomes in breast cancer.Mesothelin is a prognostic breast tumor marker whose expression is highly enriched in triple negative breast cancer tumors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25193277            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A serum mesothelin level is a prognostic indicator for patients with malignant mesothelioma in routine clinical practice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25227779            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Both the serum CA125(meso) level and the ratio of the serum CA125(mesothelin) to CA125 levels (CA125(mesothelin) \/CA125) were significantly higher in patients with EOC.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25197000            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Serum IGFBP2 and MSLN are weak diagnostic classifiers individually, but may be useful in a diagnostic biomarker panel for pancreatic cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24308545            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MSLN-silencing caused decreased proliferation rate and reduced invasive capacity and sphere formation in MSLN-overexpressing Mero-14 cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24465798            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Being negative\/focally positive for mesothelin expression was associated with longer postoperative survival than positive expression in patients with cholangiocellular carcinoma. Mesothelin positivity was a predictor of short postoperative survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23701154            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our findings suggest that MLSN can be used as a marker of neoplastic transformation of epithelial cells in pancreatic mucinous cysts.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25125620            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MSLN expression in patients with early-stage lung adenocarcinoma is associated with increased risk of recurrence and reduced overall survival.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24334761            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data provides evidence for the use of mesothelin as an immunogen for tumour-specific T cell response.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24520352            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mesothelin provokes lymphatic invasion of colorectal adenocarcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23512344            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In the gastric cancer tissues, C-ERC\/mesothelin expression was associated with lymphatic invasion. N-ERC\/mesothelin was secreted into the supernatants of gastric cancer cell lines, but does not appear to be a useful serum marker of gastric cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24146039            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Use of S100P and mesothelin in cytologically borderline cases can increase the diagnostic accuracy for pancreatic adenocarcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21538952            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that biochemical markers significantly associated with mesothelioma were hyaluronan, N-ERC\/mesothelin and syndecan-1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23991032            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            PE-SMRP adds some clinical information in the work-up of patients with a PE of unknown origin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23873013            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mesothelin expression was identified in 34% of patients with triple receptor negative breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23810431            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            addition of YKL-40 may improve the specificity of mesothelin measurements alone for detecting patients with multiple myeloma            \u003ca rel=\"nofollow\"\u003e             PMID:                        24324091            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            These data suggest that in difficult diagnostic cases both PAX2 and mesothelin immunohistochemical study may be useful in discriminating between PMRCC and primary pancreatic carcinoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24344503            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SMRP could improve CYFRA 21-1 antigen and carcinoembryonic antigen (CEA) accuracy in the differential diagnosis of malignant pleural mesothelioma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23532816            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mesothelin binding to CA125\/MUC16 promotes pancreatic cancer cell motility and invasion via MMP-7 activation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23694968            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Mesothelin, megakaryocyte potentiating factor and osteopontin are expressed in malignant mesothelioma [review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        22835614            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            MSLN overexpression promoted the invasive potential of MCF-7 cells through ERK1\/2-dependent upregulation of MMP-9; this association may have contributed to metastasis of MCF-7 cells in vivo.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23321167            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that binding of mesothelin to CA125 does not alter the measurement of mesothelin for the detection of malignant mesothelioma (MM).            \u003ca rel=\"nofollow\"\u003e             PMID:                        23357461            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The mesothelin expression promotes resistance to certain chemotherapy drugs such as TNF-alpha, paclitaxel, and a combination of platinum and cyclophosphamide.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22721387            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            SMRP was lower in healthy subjects than in subjects with malignant tumors, asbestos-related pleural lesions, and other benign diseases            \u003ca rel=\"nofollow\"\u003e             PMID:                        23277285            \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":43915177591009,"sku":"BL-2396NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLb-Ac5HuAAC90fHGuLw070.jpg?v=1685851010"},{"product_id":"biotinylated-human-ror1-protein-his-avi-tag-bl-2397np","title":"Biotinylated Human ROR1 Protein (C-6His-Avi)","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 Inactive Tyrosine-protein Kinase Transmembrane Receptor ROR1 is produced by our Mammalian expression system and the target gene encoding Gln30-Glu403 is expressed with a 6His, Avi 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%;\"\u003eQ01973\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%;\"\u003eInactive tyrosine-protein kinase transmembrane receptor ROR1; Neurotrophic tyrosine kinase, receptor-related 1; ROR1; NTRKR1\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%;\"\u003eReceptor tyrosine kinase-like orphan receptor 1 (ROR1), also known as neurotrophic tyrosine kinase, it is a member of the ROR family within receptor tyrosine kinases (RTK) superfamily. Human ROR1 is a type I transmembrane protein with 937 amino acids (aa) in length. It contains a 29 aa signal sequence, a 377 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 510 aa cytoplasmic region. ROR1 expressed strongly in human heart, lung and kidney, but weakly in the CNS. At developmental stage, it expressed at high levels during early embryonic development. ROR1 has been shown to have very low kinase activity in vitro and is unlikely to function as a tyrosine kinase in vivo. It may act as a receptor for wnt ligand WNT5A which may result in the inhibition of WNT3A-mediated 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%;\"\u003e44.6 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%;\"\u003e55-80 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%;\"\u003eHas very low kinase activity in vitro and is unlikely to function as a tyrosine kinase in vivo. Receptor for ligand WNT5A which activate downstream NFkB signaling pathway and may result in the inhibition of WNT3A-mediated signaling. In inner ear, crucial for spiral ganglion neurons to innervate auditory hair 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%;\"\u003eMembrane; Single-pass type I membrane protein. Cell projection, axon.\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, Tyr protein kinase family, ROR 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            10256           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            602336           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:4919           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000360120           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29850623            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Results find ROR1 as the direct target of miR30a, and show that ROR1 contributes to mir30amediated suppression of TNBC (triple negative breast cancer) cell invasion and migration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29693179            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ROR1 and ROR2 play distinct roles in endometrial cancer. ROR1 may promote tumor progression, while ROR2 may act as a tumor suppressor in endometrioid endometrial cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29395309            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ROR1 is a promising immunotherapeutic target in many epithelial tumors; however, high cell surface ROR1 expression in multiple normal tissues raises concerns for on-target off-tumor toxicities. Clinical translation of ROR1-targeted therapies warrants careful monitoring of toxicities to normal organs and may require strategies to ensure patient safety            \u003ca rel=\"nofollow\"\u003e             PMID:                        27852699            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Report shows that ROR1 is highly expressed in colorectal cancer (CRC) tissues when compared with their adjacent normal tissues. The Kaplan-Meier curve indicated that the CRC patients with higher ROR1 expression had significantly shorter overall survival (OS), and those with lower ROR1 expression had longer OS.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28427197            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            this study reveals that 14-3-3zeta plays a critical role in Wnt5a\/ROR1 signaling, leading to enhanced CLL migration and proliferation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28465528            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these studies indicate HS1 plays an important role in ROR1-dependent Wnt5a-enhanced chemokine-directed leukemia-cell migration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28465529            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study demonstrates expression of ROR1 and its putative ligand Wnt5a in Ewing sarcomas, and of an active ROR1 protein variant in cell lines. ROR1 silencing impaired cell migration in vitro.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26739507            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            expression of ROR1 may promote leukemia-cell activation and survival and enhance disease progression in patients with chronic lymphocytic leukemia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27815263            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the mechanistic regulation and linkage of the ROR1-HER3 and Hippo-YAP pathway in a cancer-specific context            \u003ca rel=\"nofollow\"\u003e             PMID:                        28114269            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that ROR1 contributes to melanoma progression by promoting cell growth and migration.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26509654            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High ROR1-DNAJC6 expression is associated with neoplasms.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27153396            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we aim to present an overview of the efforts and scientific achievements in targeting ROR family, particularly ROR-1, for the diagnosis and treatment of chronic lymphocytic leukemia --{REVIEW}            \u003ca rel=\"nofollow\"\u003e             PMID:                        28160756            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            that strong ROR1 expression might be an independent adverse prognostic factor in triple negative breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        26874851            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ror1 is crucial for spiral ganglion neurons to innervate auditory hair cells. Impairment of ROR1 function largely affects development of the inner ear and hearing in humans and mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27162350            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            targeting ROR1 can induce differentiation of cancer stem cells and inhibit metastasis in glioblastoma; in addition, ROR1 may be used as a potential marker for glioblastoma stem cells as well as a potential target for glioblastoma stem cell therapy            \u003ca rel=\"nofollow\"\u003e             PMID:                        26923195            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            expression of ROR1 was significantly higher in colorectal carcinoma tissues than in tumor-adjacent tissues            \u003ca rel=\"nofollow\"\u003e             PMID:                        27126945            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            these findings revealed that miR382 inhibits migration and invision by targeting ROR1 through regulating EMT in ovarian cancer, and might serve as a tumor suppressor in ovarian cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26575700            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that silencing receptor tyrosine kinases (RTKs) ROR2 and ROR1 has a strong inhibitory effect on the ability of ovarian cancer cells to proliferate, migrate and invade.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26515598            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the b-catenin-independent WNT score correlated with reduced overall survival only in the metastasized situation . This is in line with the in vitro results of the alternative WNT receptors ROR1 and ROR2, which foster invasion            \u003ca rel=\"nofollow\"\u003e             PMID:                        26862065            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The present findings thus support our notion that ROR1 sustains lung adenocarcinoma survival, at least in part, through direct physical interaction with ASK1            \u003ca rel=\"nofollow\"\u003e             PMID:                        26661061            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression of ROR1 (63%), pAkt (36%), and pCREB (20%) was observed in gastric adenocarcinomas, and expression of these proteins was well intercorrelated.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26245996            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study identifies an interaction between ROR1 and ROR2 that is required for Wnt5a signaling that promotes leukemia chemotaxis and proliferation.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26690702            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            miR-27b-3p suppresses cell proliferation through targeting receptor tyrosine kinase like orphan receptor 1 in gastric cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        26576539            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that the majority of chronic lymphocytic leukemia (CLL) patients had antibodies against receptor tyrosine kinase ROR1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26562161            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            This study reports an unanticipated function of ROR1 as a scaffold of cavin-1 and caveolin-1, two essential structural components of caveolae.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26725982            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Both IGF1R and ROR1 can be effectively targeted by SB modified CAR T cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26173023            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Significantly down-regulates the activity of the PI3K\/AKT\/mTOR signaling pathway.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25978653            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Human ROR1 and ROR2 are receptor tyrosine kinase-like pseudokinases.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25029443            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The newly developed OSU-2S delivery using ROR1-directed immunonanoparticles provide selective targeting of OSU-2S to MCL and other ROR1(+) malignancies, sparing normal B cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25937048            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ROR1 expression is correlated with malignant attributes of ovarian cancer and it may serve as a novel prognostic marker in ovarian cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25056203            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that shRNA silencing of type I receptor tyrosine kinase-like orphan receptor (ROR1) cells, or treatment with anti-ROR1 mAb UC-961 impaired the capacity of ovarian cancer cells to form spheroids or tumor xenografts.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25411317            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ROR1 is only detectable in embryonic tissue and generally absent in adult tissue, making the protein an ideal drug target for cancer therapy. [Review]            \u003ca rel=\"nofollow\"\u003e             PMID:                        24752542            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CLL cells expressed different isoforms of ROR1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24205204            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data shows that ROR1 and ROR2 are inversely expressed in melanomas and negatively regulate each other. Also, hypoxia initiates a shift of ROR1-positive melanomas to a more invasive, ROR2-positive phenotype.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24104062            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ROR1 can interact with TCL1 and enhance leukemogenesis in Emu-TCL1 transgenic mice.            \u003ca rel=\"nofollow\"\u003e             PMID:                        24379361            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our results show that customizing spacer design and increasing affinity of ROR1-CARs enhances T-cell effector function and recognition of ROR1(+) tumors.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23620405            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ROR1 may play a role in the survival of melanoma cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        23593420            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that type I receptor tyrosine kinase-like orphan receptor ROR1 may regulate EMT and metastasis and that antibodies targeting ROR1 can inhibit cancer progression and metastasis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23771907            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            that the receptor tyrosine kinase ROR1 was overexpressed in most patients with various hematological malignancies of both lymphoid and myeloid origins.            \u003ca rel=\"nofollow\"\u003e             PMID:                        22988987            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            cell surface expression in pediatric B-ALL along with its virtual absence from normal tissues and circulating cells makes ROR1 a promising target for mAb-based therapies.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23285131            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Many different human cancers express ROR1 and ROR1 may play a functional role in promoting tumor cell growth.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23041612            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            t(1;19) Acute Lymphoblastic Leukemia cells universally exhibit expression of and dependence on the cell surface receptor ROR1.            \u003ca rel=\"nofollow\"\u003e             PMID:                        23153538            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ROR1 was overexpressed in acute lymphoblastic leukemia            \u003ca rel=\"nofollow\"\u003e             PMID:                        22369092            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ROR1 is expressed in human breast cancers and has biological and clinical significance            \u003ca rel=\"nofollow\"\u003e             PMID:                        22403610            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            nuclear-localized ROR1 may play an important role in cell migration and cytoskeleton remodeling            \u003ca rel=\"nofollow\"\u003e             PMID:                        22199287            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Ror1 undergoes complex post-translational modifications by glycosylation and mono-ubiquitination. These modifications regulate Ror1 localization and signalling, and are highly variable among individual chronic lymphocytic leukemia patients.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21481194            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ROR1 is uniformly and highly expressed in all in chronic lymphocytic leukemia (CLL) cases at initial diagnosis and can serve as a diagnostic tool.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21531460            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            ROR1 is expressed on hematogones (non-neoplastic human B-lymphocyte precursors) and a minority of precursor-B acute lymphoblastic leukemia.            \u003ca rel=\"nofollow\"\u003e             PMID:                        21813176            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A panel of mAbs demonstrated high affinity and specificity for a diverse set of epitopes that involve all three extracellular domains of ROR1, are accessible on the cell surface, and mediate internalization            \u003ca rel=\"nofollow\"\u003e             PMID:                        21698301            \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":43915231789281,"sku":"BL-2397NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLb-AGt4eAAC5vSW9Rg0029.jpg?v=1685852917"},{"product_id":"biotinylated-human-carbonic-anhydrase-9-protein-his-avi-tag-bl-2399np","title":"Biotinylated Human Carbonic Anhydrase 9 Protein (C-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 Carbonic Anhydrase 9 is produced by our Mammalian expression system and the target gene encoding Gln38-Asp414 is expressed with a 6His, Avi 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%;\"\u003eQ16790\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%;\"\u003eCA9; CA-IX; Carbonic Anhydrase IX; Carbonate dehydratase IX; G250; MN; P54\/58N; RCC; RCC-associated protein G250\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%;\"\u003eCarbonic anhydrases IX (CA IX), also known as membrane antigen MN or CA9, is a member of the carbonic anhydrase (CA) family and may be involved in cell proliferation and cellular transformation. CAs are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide (H2O + CO2 = H+ + HCO3–) and thus participate in a variety of biological and physical processes. CA9 is a transmembrane enzyme expressed primarily in carcinoma cells. It is one of the best markers for hypoxia and for RCC. Appears to be a novel specific biomarker for a cervical neoplasia.\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%;\"\u003e43.6 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%;\"\u003e60 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%;\"\u003eReversible hydration of carbon dioxide. Participates in pH regulation. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia.\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. Nucleus, nucleolus. Cell membrane; Single-pass type I membrane protein. Cell projection, microvillus membrane; Single-pass type I membrane protein. Note=Found on the surface microvilli and in the nucleus, particularly in nucleolus.\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%;\"\u003eAlpha-carbonic anhydrase 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            1383           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           OMIM:           \u003ca rel=\"nofollow\"\u003e            603179           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           KEGG:           \u003ca rel=\"nofollow\"\u003e            hsa:768           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           STRING:           \u003ca rel=\"nofollow\"\u003e            9606.ENSP00000367608           \u003c\/a\u003e \u003c\/p\u003e \u003cp\u003e           UniGene:           \u003ca rel=\"nofollow\"\u003e             PMID:                        29952031            \u003c\/a\u003e  \u003c\/p\u003e\n\u003cli\u003e            Our results do not suggest a prognostic role for CA IX overexpression in stage III non-small cell lung cancer patients who received neoadjuvant treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        30029935            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            FZD1 and CAIX might be important biological markers for the carcinogenesis, metastasis, invasion, and prognosis of pancreatic ductal adenocarcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        28921449            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression of CA9 is associated with breast cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29893327            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that the conformational flexibility may have several important roles in tumour progression, facilitating interactions of carbonic anhydrase IX (hCA IX) with partner proteins assisting tumour spreading and progression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29564477            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            the findings of this study establish the SOX9\/CA9-mediated oncogenic pathway in glioma, the inhibition of which enhances the sensitivity of glioma cells to Temozolomide (TMZ) treatment, and thus highlights the value of developing small molecules or antibodies against the SOX9\/CA9 pathway, for combination therapy with TMZ, in the more efficient management of glioma            \u003ca rel=\"nofollow\"\u003e             PMID:                        29749469            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA9 SNP rs1048638 and haplotype A1AA are associated with the susceptibility of cervical invasive squamous cell carcinoma for Taiwanese women            \u003ca rel=\"nofollow\"\u003e             PMID:                        29725249            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The TCGA data revealed that CAIX expression was significantly higher in bladder cancer specimens than in normal tissue.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29949785            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CAIX enzyme inhibition assay showed the IC50 values in nM range. Though all the three compounds (1-3) showed a good binding with CAIX, compound 2 showed the best inhibition of CAIX activity. These compounds were non-toxic on normal cell lines (HEK-293) and significantly inhibit the proliferation of hypoxic cancer cells            \u003ca rel=\"nofollow\"\u003e             PMID:                        28830777            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA9 expression was observed in normal islets, while neuroendocrine microadenomas and small (\u0026lt; 1 cm) pancreatic neuroendocrine neoplasms\/tumors showed CA9 expression loss.            \u003ca rel=\"nofollow\"\u003e             PMID:                        29666945            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Study revealed that CA9 expression was a pivotal predictive factor for poor prognosis after radical surgery for HCC. Moreover, the CA9 regulation of the expression of EMT-related molecules represented a mechanism that enhanced malignant potential.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28849188            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Report weak CA9 immunoreactivity in majority of CA9 positive colorectal carcinoma cases associated with macroscopic growth pattern.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28554753            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Molecular characterization of carbonic anhydrase IX catalytic domain has been presented.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27373313            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors present evidence that enhanced autophagy does not play a role in the enhanced growth of the CA9+ cells. Our study suggests a direct in vivo functional link between hypoxic cells and CICs in primary cervix cancer xenografts.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27901496            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Genetic disruption of the intracellular pH-regulating proteins Na+\/H+ exchanger 1 (SLC9A1) and carbonic anhydrase 9 reduces the proliferation of colon cancer cells.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28055960            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data show that targeting the hypoxic tumor compartment by knockdown of carbonic anhydrase IX (CAIX) using short hairpin RNA or by chemical inhibition of CAIX with acetazolamide potentiates the anti-cancer activity of mTOR inhibitors rapamycin.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27153561            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Authors demonstrate that CAIX associates with MMP14 through potential phosphorylation residues within its intracellular domain, and that CAIX enhances MMP14-mediated collagen degradation by directly contributing hydrogen ions required for MMP14 catalytic activity.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28692057            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Results provide evidence that CAIX induces chemoresistance of A549 cells, a lung cancer cell line.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28028936            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The results suggest the possibility that CA9 exosomes released from hypoxic RCC may enhance angiogenesis in microenvironment, thereby contributing to cancer progression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28851650            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA9 expression is highly associated with distant metastases, including para-aortic involvement.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27102843            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Increased miR-210 and concomitant decreased ISCU RNA levels were found in ~40% of tumors and this was significantly associated with HIF-1alpha and CAIX, but not MCT1 or MCT4, over-expression.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28099149            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            describe the identification of the structural determinants responsible for the CA IX\/CAND1 interaction            \u003ca rel=\"nofollow\"\u003e             PMID:                        28388044            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data suggest that CAIX (carbonic anhydrase IX) is a novel downstream mediator of asTF (alternatively spliced tissue factor) in pancreatic ductal adenocarcinoma, particularly under hypoxic conditions that model late-stage tumor microenvironment; tumor hypoxia appears to lead to up-regulation of CAIX expression (or 'activation'), which is more pronounced in tumor cells overexpressing asTF.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27721473            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Our findings suggest that LCN2 suppresses tumour metastasis by targeting the transcriptional and post-transcriptional regulation of CAIX in oral squamous cell carcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        27207653            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The findings suggest that CA9, and particularly its carbonic anhydrase activity, promotes the tumorigenicity of adult T-cell leukemia\/lymphoma-derived cells and may be involved in malignant development of lymphoma-type adult T-cell leukemia\/lymphoma.            \u003ca rel=\"nofollow\"\u003e             PMID:                        28075522            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We demonstrated that the expression levels of glycolysis-related proteins glucose transporter 1, hexokinase II, carbonic anhydrase IX, and monocarbonylate transporter 4 differ between thyroid cancer subtypes and are correlated with poorer prognosis            \u003ca rel=\"nofollow\"\u003e             PMID:                        28347233            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CAIX and PTEN had prognostic importance for metastatic renal cell carcinoma patients receiving first-line VEGFR TKI. Future validation and mechanistic studies are required.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26526582            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            combined HIF1alpha and CAIX protein expression may serve as an unfavorable prognostic indicator particularly in patients treated with cyclophosphamide-based chemotherapy or radiotherapy as well as those with basal phenotype of breast cancer            \u003ca rel=\"nofollow\"\u003e             PMID:                        27184798            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA9 may have a role in castration-resistant prostate cancer progression            \u003ca rel=\"nofollow\"\u003e             PMID:                        27630286            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The diagnostic accuracy of CA9 expression for clear cell renal cell carcinoma was 100%.            \u003ca rel=\"nofollow\"\u003e             PMID:                        27775441            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            High expression of CA IX was associated with pancreatic cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26224207            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CAIX mRNA expression was significantly higher (p \u0026lt; 0.05) in hypoxia for all cell lines, which was in agreement with protein expression by ICC. CAXII expression was mixed, with a modest hypoxia-related increase in two cell lines (p \u0026lt; 0.05) and no change in others.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26276155            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We also demonstrated that the cell-surface CA IX level dropped during the death progress due to an increased ECD shedding, which required a functional ADAM17. Inhibitors of metalloproteinases reduced CA IX ECD shedding, but not apoptosis.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26993100            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            In neuroblastoma cells, CAIX and PGK1 expression is up regulated under hypoxia and correlates with response to targeted anti-proliferative treatment.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26510737            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Flow cytometrically sorted CA9+ population showed increased mRNA level of a Wnt signaling factor AXIN2. In conclusion, these observations indicate that CA9 expression in normal crypt base cells has association with intestinal epithelial stemness            \u003ca rel=\"nofollow\"\u003e             PMID:                        26648507            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We used cobalt chloride (CoCl2) as a hypoxia-mimetic agent and found that the expression of HIF-1a protein, CA IX mRNA and protein, is effectively upregulated, except for HIF-1a mRNA.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26648580            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We conclude that CA9\/miR34 interplay shares in the hypoxic regulation of mammospheres and therefore, may play a relevant role in the hypoxic breast cancer stem cell niche.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26553365            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Knockdown of CAIX significantly reduced proliferation of cancer cells, suggesting that rapid efflux of lactate and H(+), as enhanced by CAIX, contributes to cancer cell survival under hypoxic conditions.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26337752            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Data indicate that carbonic anhydrase IX (CAIX) inhibition as a relevant therapeutic goal in breast cancer, targeting the migratory, invasive, and metastatic potential of this disease.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26259239            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Inhibition of CA9 expression or activity resulted in radiation sensitization of RCC in a preclinical mouse model.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26252502            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Urinary CAIX has a high sensitivity and specificity for diagnosing urothelial bladder cancer.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26138037            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            The intrinsic thermodynamic parameters of compound binding to CA IX helped to draw the compound structure to thermodynamics relationship.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26794023            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            our study showed that the expression of CAIX in oral squamous cell carcinoma (OSCC) samples can predict the progression of OSCC and survival of OSCC patients in Taiwan            \u003ca rel=\"nofollow\"\u003e             PMID:                        26130414            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            we aimed to determine the effect of immunohistochemical staining of ezrin, carbonic anhydrase IX (CA IX), and neuropilin-2 on the prognosis of patients diagnosed with metastatic RCC who were treated with TKIs between January 2007 and June 2012.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26026587            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CA IX is expressed in B-cell lymphomas and is qualitatively correlated with extracellular acidosis in xenograft tumor models.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25130478            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            We have developed an efficient system for the production of the catalytic domain of CA IX in methylotrophic yeast Pichia pastoris            \u003ca rel=\"nofollow\"\u003e             PMID:                        26522624            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            CAIX expression is increased in hypoxia to compensate for the decrease in its activity produced by a low extracellular pH. A major function of CAIX is to lower the extracellular pH.            \u003ca rel=\"nofollow\"\u003e             PMID:                        26249175            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            A strong positive correlation between the mRNA expression levels of HIF-2alpha, CA9, VEGF, GLUT-1 and OPN suggests a specific hypoxia-associated profile of mRNA expression in glioblastoma multiforme            \u003ca rel=\"nofollow\"\u003e             PMID:                        25963717            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            expression of the CA-IX protein is a crucial predictor of poor prognosis in resectable hepatocellular carcinoma            \u003ca rel=\"nofollow\"\u003e             PMID:                        25738958            \u003c\/a\u003e \u003c\/li\u003e \u003cli\u003e            Preventing carbonic anhydrase IX association with 45 S rDNA gene promoters.            \u003ca rel=\"nofollow\"\u003e             PMID:                        25793203            \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":43915204296929,"sku":"BL-2399NP","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0624\/2169\/6737\/products\/CgAKNmLkLb-AIxo9AACj1vEXyW4344.jpg?v=1685851962"}],"url":"https:\/\/www.betalifesci.com\/collections\/antibody-cell-therapy-targets.oembed?page=29","provider":"Beta LifeScience","version":"1.0","type":"link"}