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- goat polyclonal IgG, 200 µg/ml
- epitope mapping near the C-terminus of ADAM9 of human origin
- recommended for detection of precursor and mature ADAM9 of mouse, rat and human origin by WB, IP, IF and ELISA; also reactive with additional species, including equine, canine and porcine
- blocking peptide, sc-23290 P
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ADAM9 Background Information The human ADAM9 gene maps to chromosome 8p11 and encodes an 819 amino acid glycoprotein that is present in brain, liver, heart, kidney, lung, and trachea (1–3). ADAM (a disintegrin and metalloprotease) glycoproteins are a family of over 30 membrane-anchored, Zn2+-dependent proteases that influence fertilization, muscle fusion, cytokine secretion, modulation of Notch-related neurogenic pathways, monocyte fusion, and many other cell adhesion-dependent events (4–6). ADAM proteins contain a signal domain, a pro domain, a metalloprotease domain, a disintegrin domain (Integrin ligand), a cysteine-rich region, an epidermal growth factor-like domain, a transmembrane (TM) domain (alternative splicing before the TM domain in ADAM11, 12, 17, and 28 can yield soluble forms), and a cytoplasmic tail (4–8). Removal of the amino-terminal signal peptide initiates secretion from the cell, or anchoring on the cell surface (3,4–6). Furin or furin-like proprotein convertase-dependent cleavage of the pro domain initiates catalytic activity of the metalloprotease (3,4–6). |
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ADAM9 (C-15)
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ADAM9 (C-15): sc-23290. Western blot analysis of ADAM9 expression in Caki-1 (A) and HeLa (B) whole cell lysates.
ADAM9 (C-15): sc-23290. Western blot analysis of ADAM9 expression in non-transfected: sc-117752 (A) and mouse ADAM9 transfected: sc-118238 (B) 293T whole cell lysates.
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