Human ADAM9 Ectodomain Biotinylated Antibody Summary
Ala206-Asp697
Accession # Q13443
Applications
Human ADAM9 Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 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.
Background: ADAM9
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 beta -chain and fibronectin (2,4). Besides its catalytic activity, ADAM9 functions as an adhesion molecule 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, et al. (2001) DDT 6:417.
- Roghan, et al. (1999) J. Biol. Chem. 274:3531.
- Izumi, et al. (1998) EMBO J. 17:7260.
- Schwettmann and Tschesche (2001) Prot. Expre. & Purif. 21:65.
- Nath, et al. (2000) J. Cell Sci. 113:2319.
- Zhou, et al. (2001) Biochem. Biophys. Res. Comm. 280:574.
- Howard, et al. (1999) J. Biol. Chem. 274:31693.
- Weskamp, et al. (1996) J. Cell. Biol. 132:717.
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