|Detection of ADAM10 in Mouse Splenocytes by Flow Cytometry. Mouse splenocytes were stained with Rat Anti-Mouse ADAM10 Alexa Fluor® 700‑conjugated Monoclonal Antibody (Catalog # FAB946N, filled histogram) or isotype control antibody (Catalog # IC006N, open histogram). View our protocol for Staining Membrane-associated Proteins.|
ADAM10 (also known as Kuzbanian, mammalian disintegrin metalloprotease, myelin-associated metalloproteinase) is a member of the ADAM family that contains a disintegrin and metalloprotease-like domain (1, 2). Like other membrane-anchored ADAMs, ADAM10 consists of the following domains, pro with a cysteine switch and furin cleavage sequence, catalytic with the zinc-binding site and Met-turn expected for reprolysins, disintegrin-like, cysteine-rich, EGF-like, transmembrane, and cytoplasmic. ADAM10 is highly conserved, with 97% amino acid identity between mouse, rat, bovine and human and 45% identity between mouse and Drosophila. The active enzyme processes notch, notch ligand delta, and amyloid protein precursor at the alpha site, playing an important role in neurogenesis (3, 4). It also processes the 26 kDa membrane-anchored pro-tumor necrosis factor-alpha (TNF-alpha ) to the 17 kDa mature TNF-alpha (5). It cleaves myelin basic protein and type IV collagen (6, 7). ADAM10 is widely expressed in tissues and resides both on the cell surface and in the cell (8, 9).
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