Anti-ADAM10

0.5mg/ml if reconstituted with 0.2ml sterile DI water. ADAM10, A Disintegrin and Metalloproteinase Domain 10, is also known 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 ADAM10 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 (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed:26686862, PubMed:11786905). Contributes to the normal cleavage of the cellular prion protein (PubMed:11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed:12475894). 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 (PubMed:17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed:19114711, PubMed:21288900). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146). [The UniProt Consortium]