Recombinant Human ADAM15 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0083

Recombinant Human ADAM15 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0083
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Product Overview

Tag His
Host Species Human
Accession Q13444
Synonym MDC15
Background ADAM15, also known as Metargidin, is a type I transmembrane glycoprotein belonging to the ADAM (A Disintegrin and Metalloprotease Domain) family of proteins and is widely expressed in different tissues and cell types. Members of this family contain an amino-terminal metalloprotease domain followed by a disintegrin domain, a cysteine-rich region and a membrane proximal EGF-like domain. The disintegrin domain of ADAM15/metargidin contains an RGD tripeptide sequence, suggesting that it may potentially interact with the integrin family of proteins. ADAM15 is a transmembrane multi-domain proteins implicated in proteolysis, cell-cell and cell-matrix interactions in various disease conditions. There is also evidence supporting a role for ADAM15 in angiogenesis and angioinvasion of tumor cells, which are critical for unrestrained tumor growth and metastatic spread. Given its diverse functions, ADAM15 may represent a pivotal regulatory component of tumor progression, an important target for therapeutic intervention, or emerge as a biomarker of disease progression.
Description A DNA sequence encoding the human ADAM15 (Q13444-1) (Met 1-Thr 696) precursor was expressed, with a C-terminal His tag.
Source CHO Stable Cells
Predicted N Terminal Asp 207 (mature form)
AA Sequence Met 1-Thr 696
Molecular Weight The secreted recombinant human ADAM15 (mature form) comprises 501 a.a. after proteolytic of the signal peptide and pro peptide and has a predicted molecular mass of 54 kDa. As a result of glycosylation, rhADAM15 migrates as an approximately 65-70 kDa band in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store 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.

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
Tissue Specificity Expressed in colon and small intestine. Expressed in airway smooth muscle and glomerular mesangial cells (at protein level). Ubiquitously expressed. Overexpressed in atherosclerotic lesions. Constitutively expressed in cultured endothelium and smooth musc

Gene Functions References

  1. The results of our study demonstrate that ADAM15 is strongly up regulated in a small but highly aggressive fraction of prostate cancers. PMID: 28282546
  2. Data show that ADAM9 silencing affected MMP2 and ADAM15 expression. PMID: 27554339
  3. ADAM15 promotes lung cancer cell invasion through directly targeting MMP9 activation. PMID: 26323669
  4. 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
  5. present a tumor suppressive mechanism for ADAM15 exosomes and provide insight into the functional significance of exosomes that generate tumor-inhibitory factors PMID: 25208722
  6. these data suggest the potential role of miR147b in regulating endothelial barrier function by targeting ADAM15 expression. PMID: 25333931
  7. findings indicated that silencing ADAM15 had antiinflammatory effects in FLSs and efficiently inhibited the development of CIA. PMID: 25650586
  8. 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
  9. ADAM15 contributes to apoptosis resistance in rheumatoid arthritis synovial fibroblasts by activating the Src/FAK pathway upon FasL exposure. PMID: 23918525
  10. 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
  11. ADAM15 acts as a negative regulator of TRIF-mediated NF-kappaB and IFN-beta reporter gene activity via TLR3 and TLR4 signaling. PMID: 23365087
  12. dispensable for cutaneous wound healing and B16F1 melanoma growth, but significantly contributes to metastasis formation PMID: 22621184
  13. 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
  14. ADAM15 tail can transduce a percepted extracellular signal to enhance FAK and Src phosphorylation. PMID: 22544741
  15. 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
  16. gene expressions for ADAM8 and ADAM15 were notably lower in ascending aorta as compared with aortic dissection PMID: 21728902
  17. demonstrate the intrinsic promoter activity of ADAM15 in quiescent mesangial cells and show the involvement of Sp1 in its regulation PMID: 21196774
  18. the downregulation of ADAM15 plays an important role in melanoma progression and ADAM15 act as a tumorsuppressor in melanoma. PMID: 20851104
  19. The effects of ADAM15 on endothelial hyperpermeability and neutrophil transmigration are mediated by intracellular signalling involving Src and ERK1/2 activation. PMID: 20189953
  20. 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
  21. 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
  22. Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins SNX33 and nephrocystin PMID: 19718658
  23. 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
  24. Atrial fibrillation is associated with an increase in the expression of ADAM15 in the heart atrium PMID: 11839628
  25. structure determined by X ray chrystallography PMID: 11840679
  26. functional classification based on a conserved motif for bining intergrinalpha9beta1 PMID: 11882657
  27. ADAM 15 IS involved in the restructuring of the mesangial matrix and in the migration of MC in disease. PMID: 12091380
  28. 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
  29. ADAM8, ADAM15, and MDC-L, but not ADAM17, catalyzed ectodomain shedding of CD23, the low affinity IgE receptor. PMID: 12777399
  30. ADAM15 has a role in pathological neovascularization in mice PMID: 12897135
  31. 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
  32. In humans, the cytoplasmic domain of ADAM15v2 strongly interacts with Lck and Hck and regulates leukocyte function. PMID: 15263807
  33. 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
  34. Altered regulation of alternative exon usage in ADAM15 gene may provide a useful target for cancer diagnostics development PMID: 15384173
  35. ADAM15 decreases integrin alphavbeta3/vitronectin-mediated ovarian neoplasm cell adhesion and movement in an RGD-dependent fashion. PMID: 15618016
  36. Lung carcinoma cell lines and tissues were frequently ADAM15 positive. PMID: 15756594
  37. ADAM15 is generally overexpressed in adenocarcinoma and is highly associated with metastatic progression of prostate and breast cancers PMID: 16756724
  38. ADAM15 is upregulated in epithelial cells during inflammatory bowel disease compared with the normal colon epithelial cells. PMID: 16894352
  39. 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
  40. ADAM-15-mediated cell-cell interactions are involved in mechanisms of epithelial restitution and production of pro-inflammatory mediators PMID: 17416588
  41. 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
  42. the alternative exon use is a physiological post-transcriptional mechanism regulating ADAM15 expression in human tissues. PMID: 17937806
  43. 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
  44. Four ADAM-15 variants are differentially expressed in human mammary carcinoma tissues compared with normal breast. PMID: 18296648
  45. This presents a novel mechanism by which ADAM15 regulates cell-matrix adhesion and migration. PMID: 18387333
  46. ADAM15 catalyzes the cleavage of E-cadherin to generate a soluble fragment that in turn binds to and stimulates ErbB receptor signaling PMID: 18434311
  47. Recombinant ADAM15 disintegrin domain inhibits melanoma cell proliferation partly through p38 kinase activation. PMID: 18695922
  48. results define key catalytic properties of ADAM15 in cells and its response to stimulators and inhibitors of ectodomain shedding. PMID: 19207106
  49. involved in advanced atherosclerosis, in catalytically active form, most notably associated with cells of monocytic origin PMID: 19253070
  50. Insights into the mechanism of how a splice variant linked to clinical agressiveness in breast cancer causes increased activity of ADAM15B. PMID: 19487280


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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.

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