Immobilized RecombinantHuman ADAM15 (Catalog # 9234-AD)supports theadhesion of Jurkat human acute T cell leukemia cells. The ED50 for this effectis 0.5-3 μg/mL.
A disintegrin and metalloproteinase 15 (ADAM15), also known as MDC15 and Metargin, is an approximately 110 kDa transmembrane member of the M12B family of peptidases (1). Human ADAM15 is synthesized with a 189 amino acid (aa) propeptide that contains a cysteine switch motif. The 75 kDa activated form of human ADAM15 (after removal of the propeptide) consists of a 490 aa extracellular domain (ECD) with a peptidase, disintegrin, cysteine-rich, and EGF-like domain followed by a 21 aa transmembrane segment and a 146 aa cytoplasmic domain (2). Within the ECD, human ADAM15 shares 85% aa sequence identity with mouse and rat ADAM15. Alternative splicing generates multiple additional isoforms with various deletions or substitutions in the cytoplasmic domain, deletion in the propeptide and peptidase domains, or truncation at the beginning of the EGF-like domain (3, 4). ADAM15 is widely expressed, including on colonic epithelial cells, smooth muscle cells, vascular endothelial cells, and it is upregulated during chronic inflammation and tumor progression (5-8). It is also expressed on spermatocytes where both propeptide and the protease domain are cleaved during spermatocyte maturation (9, 10). ADAM15 promotes endothelial permeability, T cell adhesion, MMP-9 production and activation, and tumor cell metastasis (6, 8, 11, 12). It binds to Integrin alpha V beta 3 (13) and mediates the proteolytic shedding of cell surface N-Cadherin, E-Cadherin, MICB, CD23/Fc epsilon RII, and FGF R2 (IIb) (6, 7, 14-16).
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A Disintegrin and Metalloprotease-like Domain 15
Entrez Gene IDs:
8751 (Human); 11490 (Mouse)
ADAM 15; ADAM metallopeptidase domain 15; disintegrin-like, and cysteine-rich protein 15; EC 3.4.24; MDC15; MDC-15; Metargidin
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