Mouse ADAM9 Ectodomain Biotinylated Antibody

ADAM9, also known as MDC9 or meltrin gamma, is a member of the ADAM family that contains a disintegrin and metalloprotease-like domain (1). Like other membrane‑anchored ADAMs, ADAM9 consists of a pro domain with a cysteine switch and furin cleavage sequence, a catalytic domain with the zinc-binding site and Met-turn expected for reprolysins, a disintegrin-like domain, a cysteine-rich domain, an EGF-like domain, a transmembrane domain, and the cytoplasmic domain. ADAM9 is able to cleave peptides corresponding to cleavage sites of tumor necrosis factor-alpha (TNF-alpha), the p75-TNF receptor, the beta-amyloid protein precursor, and the c-kit ligand-1, implying that it may participate in shedding of these membrane proteins (2). In fact, ADAM9 has been shown to shed membrane‑anchored heparin‑binding EGF-like growth factor (3). In addition, it also cleaves oxidized insulin B-chain and fibronectin (2, 4). Besides its catalytic activity, ADAM9 functions as an adhesion molelcule through binding of its disintegrin domain to integrins such as alpha_v beta₅ and alpha₆ beta₁ (5, 6). The cytoplasmic domain of ADAM9 interacts with Src homology 3 (SH3)‑containing proteins and protein kinase C, and may mediate different signaling pathways (3, 7). ADAM9 is widely expressed in tissues (8).