Recombinant Human Disintegrin And Metalloproteinase Domain-Containing Protein 15 (ADAM15) Protein (GST)

Name: Recombinant Human Disintegrin And Metalloproteinase Domain-Containing Protein 15 (ADAM15) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08497P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, Explore high-quality enzymes for research and supplementation, Featured enzyme molecules, High-quality recombinant proteins, Protease

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Disintegrin And Metalloproteinase Domain-Containing Protein 15 (ADAM15) Protein (GST) is produced by our E.coli expression system. This is a extracellular protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q13444
Target Symbol	ADAM15
Synonyms	A disintegrin and metalloproteinase domain 15 (metargidin); A disintegrin and metalloproteinase domain 15; ADA15_HUMAN; ADAM 15; ADAM metallopeptidase domain 15; Adam15; and cysteine-rich protein 15; Disintegrin and metalloproteinase domain-containing protein 15; disintegrin-like; EC 3.4.24.; MDC 15; MDC-15; MDC15; Metalloprotease RGD disintegrin protein; Metalloproteinase like disintegrin like and cysteine rich protein 15; Metalloproteinase-like; Metargidin
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	DVVTETKTVELVIVADHSEAQKYRDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAHLLPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPGPAPAKTCIMEASTDFLPGLNFSNCSRRALEKALLDGMGSCLFERLPSLPPMAAFCGNMFVEPGEQCDCGFLDDCVDPCCDSLT
Expression Range	207-452aa
Protein Length	Extracellular Domain
Mol. Weight	53.6kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain.
Subcellular Location	Endomembrane system; Single-pass type I membrane protein. Cell junction, adherens junction. Cell projection, cilium, flagellum. Cytoplasmic vesicle, secretory vesicle, acrosome.
Database References	HGNC: 193 OMIM: 605548 KEGG: hsa:8751 STRING: 9606.ENSP00000349436 UniGene: PMID: 28282546 Data show that ADAM9 silencing affected MMP2 and ADAM15 expression. PMID: 27554339 ADAM15 promotes lung cancer cell invasion through directly targeting MMP9 activation. PMID: 26323669 the results revealed an undescribed role of ADAM15 in the invasion of human bladder cancer and suggested that the ADAM15 catalytic domain may represent a viable therapeutic target in patients with advanced disease. PMID: 26930657 present a tumor suppressive mechanism for ADAM15 exosomes and provide insight into the functional significance of exosomes that generate tumor-inhibitory factors PMID: 25208722 these data suggest the potential role of miR147b in regulating endothelial barrier function by targeting ADAM15 expression. PMID: 25333931 findings indicated that silencing ADAM15 had antiinflammatory effects in FLSs and efficiently inhibited the development of CIA. PMID: 25650586 The severity of intrauterine adhesions positively correlates to the protein and transcript expression levels of ADAM-15 and ADAM-17 in uterine tissue. PMID: 23910172 ADAM15 contributes to apoptosis resistance in rheumatoid arthritis synovial fibroblasts by activating the Src/FAK pathway upon FasL exposure. PMID: 23918525 In conclusion, our data identified rhddADAM15 as a potent inhibitor of tumor growth and metastasis, making it a promising tool for use in anticancer treatment. PMID: 23688428 ADAM15 acts as a negative regulator of TRIF-mediated NF-kappaB and IFN-beta reporter gene activity via TLR3 and TLR4 signaling. PMID: 23365087 dispensable for cutaneous wound healing and B16F1 melanoma growth, but significantly contributes to metastasis formation PMID: 22621184 Exosomes rich in ADAM15 display enhanced binding affinity for integrin alphavbeta3 in an RGD-dependent manner and suppress vitronectin- and fibronectin-induced cell adhesion, growth, and migration, as well as in vivo tumor growth. PMID: 22505472 ADAM15 tail can transduce a percepted extracellular signal to enhance FAK and Src phosphorylation. PMID: 22544741 Promoter methylation of ADAM15 was examined as well as the microsatellite instability status. Thirty-six percent of colorectal carcinomas displayed a reduced expression of ADAM15. PMID: 21190186 gene expressions for ADAM8 and ADAM15 were notably lower in ascending aorta as compared with aortic dissection PMID: 21728902 demonstrate the intrinsic promoter activity of ADAM15 in quiescent mesangial cells and show the involvement of Sp1 in its regulation PMID: 21196774 the downregulation of ADAM15 plays an important role in melanoma progression and ADAM15 act as a tumorsuppressor in melanoma. PMID: 20851104 The effects of ADAM15 on endothelial hyperpermeability and neutrophil transmigration are mediated by intracellular signalling involving Src and ERK1/2 activation. PMID: 20189953 cytoplasmic tail of ADAM15 confers a modulatory effect on the autophosphorylation site Y397 of the focal adhesion kinase (FAK) during chondrocyte-collagen interaction PMID: 18774960 ADAM15 conveys antiapoptotic properties to osteoarthritis chondrocytes that might sustain their potential to better resist the influence of death-inducing stimuli under pathophysiologic conditions PMID: 20213810 Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins SNX33 and nephrocystin PMID: 19718658 These data demonstrate selective, phosphorylation-dependent interactions of ADAM15 with Src family PTKs and Grb2, which highlight the potential for integration of ADAM functions and cellular signaling PMID: 11741929 Atrial fibrillation is associated with an increase in the expression of ADAM15 in the heart atrium PMID: 11839628 structure determined by X ray chrystallography PMID: 11840679 functional classification based on a conserved motif for bining intergrinalpha9beta1 PMID: 11882657 ADAM 15 IS involved in the restructuring of the mesangial matrix and in the migration of MC in disease. PMID: 12091380 Data suggest that ADAM15, whose expression may be driven by VE-cadherin, may be a component of adherens junctions and play a role in endothelial functions mediated by these cell contacts. PMID: 12243749 ADAM8, ADAM15, and MDC-L, but not ADAM17, catalyzed ectodomain shedding of CD23, the low affinity IgE receptor. PMID: 12777399 ADAM15 has a role in pathological neovascularization in mice PMID: 12897135 ADAM 15 was detected in perinatal cortical pyramidal cells; during aging there was also an increase in intracellular staining and the number of stained cells per volume (cell density). In AD brains ADAM 15 was seen in a few diffuse plaques PMID: 14707550 In humans, the cytoplasmic domain of ADAM15v2 strongly interacts with Lck and Hck and regulates leukocyte function. PMID: 15263807 The expression and the role of ADAMs in intestinal epithelial cells, including its role in wound healing in human cell lines and cultured colonic cells. PMID: 15358598 Altered regulation of alternative exon usage in ADAM15 gene may provide a useful target for cancer diagnostics development PMID: 15384173 ADAM15 decreases integrin alphavbeta3/vitronectin-mediated ovarian neoplasm cell adhesion and movement in an RGD-dependent fashion. PMID: 15618016 Lung carcinoma cell lines and tissues were frequently ADAM15 positive. PMID: 15756594 ADAM15 is generally overexpressed in adenocarcinoma and is highly associated with metastatic progression of prostate and breast cancers PMID: 16756724 ADAM15 is upregulated in epithelial cells during inflammatory bowel disease compared with the normal colon epithelial cells. PMID: 16894352 the ADAM-15 disintegrin-like domain and a number of mutants in which the RGD-containing loop was substituted by cognate regions from ADAM-2, -12 and -19 were tested in terms of integrin-binding activity PMID: 17080222 ADAM-15-mediated cell-cell interactions are involved in mechanisms of epithelial restitution and production of pro-inflammatory mediators PMID: 17416588 disintegrin domain of ADAM-15 inhibits ASMC adhesion and migration through the beta(1)-integrin, without modulating signaling pathways involved in ASMC migratory responses PMID: 17575078 the alternative exon use is a physiological post-transcriptional mechanism regulating ADAM15 expression in human tissues. PMID: 17937806 Loss of ADAM15 significantly attenuated the metastatic spread of PC-3 cells to bone. Data strongly support a functional role for ADAM15 in prostate tumor cell interaction with vascular endothelium and the metastatic progression of human prostate cancer. PMID: 18281484 Four ADAM-15 variants are differentially expressed in human mammary carcinoma tissues compared with normal breast. PMID: 18296648 This presents a novel mechanism by which ADAM15 regulates cell-matrix adhesion and migration. PMID: 18387333 ADAM15 catalyzes the cleavage of E-cadherin to generate a soluble fragment that in turn binds to and stimulates ErbB receptor signaling PMID: 18434311 Recombinant ADAM15 disintegrin domain inhibits melanoma cell proliferation partly through p38 kinase activation. PMID: 18695922 results define key catalytic properties of ADAM15 in cells and its response to stimulators and inhibitors of ectodomain shedding. PMID: 19207106 involved in advanced atherosclerosis, in catalytically active form, most notably associated with cells of monocytic origin PMID: 19253070 Insights into the mechanism of how a splice variant linked to clinical agressiveness in breast cancer causes increased activity of ADAM15B. PMID: 19487280

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.