Detection of Human and Mouse ADAM9 by Western Blot. Western blot shows lysates of C2C12 mouse myoblast cell line and WI‑38 human lung fibroblast cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse ADAM9 Ectodomain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF949) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). Specific bands were detected for ADAM9 at approximately 110 and 80 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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 beta 5 and alpha 6 beta 1 (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).
Moss, M.L. et al. (2001) Drug Discov. Today 6:417.
Roghani, M. et al. (1999) J. Biol. Chem. 274:3531.
Izumi, Y. et al. (1998) EMBO J. 17:7260.
Schwettmann, L. and H. Tschesche (2001) Protein. Expr. Purif. 21:65.
Nath, D. et al. (2000) J. Cell Sci. 113:2319.
Zhou, M. et al. (2001) Biochem. Biophys. Res. Comm. 280:574.
Howard, L. et al. (1999) J. Biol. Chem. 274:31693.
Weskamp, G. et al. (1996) J. Cell Biol. 132:717.
A Disintegrin and Metalloprotease-like Domain 9
Entrez Gene IDs:
8754 (Human); 11502 (Mouse)
a disintegrin and metalloproteinase domain 9 (meltrin gamma); ADAM 9; ADAM metallopeptidase domain 9 (meltrin gamma); ADAM metallopeptidase domain 9; Cellular disintegrin-related protein; cone rod dystrophy 9; CORD9; disintegrin and metalloproteinase domain-containing protein 9; EC 3.4.24; EC 3.4.24.-; MCMP; MCMPMDC9KIAA0021Mltng; MDC9; Meltrin gamma; Meltrin-gamma; Metalloprotease/disintegrin/cysteine-rich protein 9; MLTNG; Myeloma cell metalloproteinase
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