Anti-ADAM15 Antibody Picoband® Fluoro488 Conjugated

Disintegrin and metalloproteinase domain-containing protein 15 is an enzyme that in humans is encoded by the ADAM15 gene. This gene is mapped to 1q21.3. The protein encoded by this gene is a member of the ADAM (a disintegrin and metalloproteinase) protein family. ADAM family members are type I transmembrane glycoproteins known to be involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules. This protein contains multiple functional domains including a zinc-binding metalloprotease domain, a disintegrin-like domain, as well as a EGF-like domain. Through its disintegrin-like domain, this protein specifically interacts with the integrin beta chain, beta 3. It also interacts with Src family protein-tyrosine kinases in a phosphorylation-dependent manner, suggesting that this protein may function in cell-cell adhesion as well as in cellular signaling. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed.

Disintegrin and metalloproteinase domain-containing protein 15; ADAM 15; Metalloprotease RGD disintegrin protein; Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15; MDC-15; Metargidin; ADAM15; MDC15

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 muscle. Expressed in chondrocytes. Expressed in airway smooth muscle and glomerular mesangial cells.

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.

1. Herren, B., Raines, E. W., Ross, R. Expression of a disintegrin-like protein in cultured human vascular cells and in vivo. FASEB J. 11: 173-180, 1997. 2. Horiuchi, K., Weskamp, G., Lum, L., Hammes, H.-P., Cai, H., Brodie, T. A., Ludwig, T., Chiusaroli, R., Baron, R., Preissner, K. T., Manova, K., Blobel, C. P. Potential role for ADAM15 in pathological neovascularization in mice. Molec. Cell. Biol. 23: 5614-5624, 2003. 3. Karkkainen, I., Karhu, R., Huovila, A.-P. J. Assignment of the ADAM15 gene to human chromosome band 1q21.3 by in situ hybridization. Cytogenet. Cell Genet. 88: 206-207, 2000.