Anti-ADAM10

0.5mg/ml if reconstituted with 0.2ml sterile DI water. A Disintegrin and Metalloproteinase Domain 10 is also know as AD10. ADAM10 is a member of the ADAM family and members of this family are cell surface proteins with a unique structure possessing both potential adhesion and protease function. The gene is mapped to chromosome 15q21.3-q23. ADAM proteins contain an N-terminal signal sequence, followed by a prodomain, a metalloprotease-like domain, a disintegrin-like domain, a cysteine-rich region, an EGF -like repeat, a transmembrane domain, and a C-terminal cytoplasmic tail. Conversion of the membrane-bound precursor to a secreted mature protein is mediated by a protease termed TNFA convertase. ADAM10 possesses TNFA convertase activity. Protein function: 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. [The UniProt Consortium]