Mouse Anti-Human ADAM-9
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|Centrifuge vial prior to opening. Reconstitute the antibody with 500 µl sterile PBS and the final concentration is 200 µg/ml.
|Stability and Storage
|Lyophilized samples are stable for 2 years from date of receipt when stored at -70°C. Reconstituted antibody can be aliquoted and stored frozen at < -20°C for at least six months without detectable loss of activity.
|This antibody was produced from a hybridoma (mouse myeloma fused with spleen cells from a mouse )immunized with Human ADAM-9 (extracellular domain) recombinant protein.
|recombinant human ADAM-9 (extracellular domain)
|ADAM9; MCMP; MDC9; CORD9; Mltng
|ADAM9, also known as MDC9 or meltrin γ, is a member of the ADAM family that contains a disintegrin and metalloprotease-like domain. 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 Metturn expected for reprolysins, a disintegrin-like domain, a cysteinerich 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-α (TNFα), the p75 TNF receptor, the βamyloid protein precursor, and the c-kit ligand 1, implying that it may participate in shedding of these membrane proteins. In fact, ADAM9 has been shown to shed membrane-anchored heparin-binding EGF-like growth factor. In addition, it also cleaves oxidized insulin βchain and fibronectin. Besides its catalytic activity, ADAM9 functions as an adhesion molecule through binding of its disintegrin domain to integrins such as αvβ5 and α6β1. The cytoplasmic domain of ADAM9 interacts with Src homology 3 (SH3)containing proteins and protein kinase C, and may mediate different signaling pathways. ADAM9 is widely expressed in tissues.
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