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MMP-10 (catalytic domain) (human), (recombinant)

BML-SE329-0010 10 µg 506.00 USD
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Product Details

Alternative Name:Matrix metalloproteinase 10, Stromelysin-2
MW:19.4 kDa
Source:Produced in E. coli. Active Matrix Metalloproteinase-10 (MMP-10, stromelysin-2, transin-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-10 (Phe99-Glu271, NM_2425) with a C-terminal purification tag. This comprises an active form of MMP-10 which lacks the C-terminal hemopexin domain. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected.
UniProt ID:P09238
Formulation:Liquid. In 50mM TRIS, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.5% Brij-35, and 30% glycerol.
Purity Detail:Partially purified by single-step affinity chromatography and gel filtration.
Activity:Preincubation of MMP-10 catalytic domain at 22nM with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 100nM for 1 hour inhibits enzymatic activity by 95%.
Specific Activity:≥200 pmol/min/µg at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100 µM; Prod. No. BML-P125) as substrate.
Application Notes:Useful tool to study of enzyme kinetics, cleave target substrates, and screen for inhibitors.
Shipping:Dry Ice
Long Term Storage:-80°C
Regulatory Status:RUO - Research Use Only

Product Literature References

Paxillin-mediated recruitment of calcineurin to the contractile ring is required for the correct progression of cytokinesis in fission yeast: R. Martin-Garcia, et al.; Cell Rep. 25, 772 (2018), Abstract;
Matrix metalloproteinase-10 is a critical effector of protein kinase Ciota-Par6alpha-mediated lung cancer: L.A. Frederick, et al.; Oncogene 27, 4841 (2008), Abstract; Full Text

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