>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
<1.0 EU per 1 μg of the protein by the LAL method.
55 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
Dilute rhADAM9 to 40 µg/mL in Assay Buffer.
Dilute substrate to 20 µM in Assay Buffer.
Combine equal volumes of 40 µg/mL rhADAM9 and 20 µM substrate. Include a control containing Assay Buffer and 20 µM substrate without any rhADAM9.
Incubate reactions at 37 °C for 30 minutes.
Load 100 μL of reactions and control per well in a black plate.
Read with excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively, in endpoint mode.
Calculate specific activity:
Specific Activity (pmol/min/µg) =
Adjusted Fluorescence* (RFU) x Conversion Factor** (pmol/RFU)
Incubation time (min) x amount of enzyme (µg)
*Adjusted for Control **Derived using calibration standard MCA-Pro-Leu-OH (Bachem, Catalog # M-1975).
rhADAM9: 2.0 µg
Substrate: 10 µM
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human ADAM9 Protein, CF
a disintegrin and metalloproteinase domain 9 (meltrin gamma)
ADAM metallopeptidase domain 9 (meltrin gamma)
ADAM metallopeptidase domain 9
Cellular disintegrin-related protein
cone rod dystrophy 9
disintegrin and metalloproteinase domain-containing protein 9
Metalloprotease/disintegrin/cysteine-rich protein 9
Myeloma cell metalloproteinase
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.
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