ADAM10 Antibody – Rabbit Polyclonal

ADAM10: Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth- like factor, ephrin-A2 and for constitutive and regulated alpha- secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. May regulate the EFNA5-EPHA3 signaling.

Protein type: Vesicle; Motility/polarity/chemotaxis; Cell adhesion; Membrane protein, integral; Cell surface; EC 3.4.24.81; Protease

Chromosomal Location of Human Ortholog: 15q22

Cellular Component: Golgi apparatus; focal adhesion; cell surface; intracellular membrane-bound organelle; membrane; cytoplasm; postsynaptic density; plasma membrane; integral to membrane; Golgi-associated vesicle; nucleus

Molecular Function: integrin binding; protein binding; protein homodimerization activity; metallopeptidase activity; zinc ion binding; metalloendopeptidase activity; endopeptidase activity; SH3 domain binding; protein kinase binding; receptor binding

Biological Process: epidermal growth factor receptor signaling pathway; integrin-mediated signaling pathway; axon guidance; Notch signaling pathway; extracellular matrix organization and biogenesis; in utero embryonic development; constitutive protein ectodomain proteolysis; membrane protein ectodomain proteolysis; Notch receptor processing; negative regulation of cell adhesion; protein amino acid phosphorylation; positive regulation of cell growth; collagen catabolic process; extracellular matrix disassembly; PMA-inducible membrane protein ectodomain proteolysis; cell-cell signaling; monocyte activation; positive regulation of cell proliferation; ephrin receptor signaling pathway; positive regulation of cell migration

Disease: Reticulate Acropigmentation Of Kitamura; Alzheimer Disease 18