ADAM10/KUZ Antibody – Rabbit Polyclonal

Members of the ADAM family are cell surface proteins with a unique structure possessing both potential adhesion and protease domains. This gene encodes and ADAM family member that cleaves many proteins including TNF-alpha and E-cadherin. Alternate splicing results in multiple transcript variants encoding different proteins that may undergo similar processing. [provided by RefSeq, Feb 2016]

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

Chromosomal Location of Human Ortholog: 15q21.3

Cellular Component: cell surface; cytoplasm; endoplasmic reticulum lumen; focal adhesion; Golgi apparatus; Golgi-associated vesicle; membrane; nucleus; plasma membrane

Molecular Function: endopeptidase activity; metalloendopeptidase activity; metallopeptidase activity; protein binding; protein homodimerization activity; protein kinase binding

Biological Process: cellular protein metabolic process; constitutive protein ectodomain proteolysis; ephrin receptor signaling pathway; extracellular matrix disassembly; in utero embryonic development; membrane protein ectodomain proteolysis; monocyte activation; negative regulation of cell adhesion; neutrophil degranulation; Notch receptor processing; Notch signaling pathway; PMA-inducible membrane protein ectodomain proteolysis; positive regulation of cell growth; positive regulation of cell migration; positive regulation of cell proliferation; post-translational protein modification; protein amino acid phosphorylation

Disease: Alzheimer Disease 18; Reticulate Acropigmentation Of Kitamura