Product Details
| Alternative Name: | Matrix metalloproteinase 10, Stromelysin-2 |
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| MW: | 19.4 kDa |
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| 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. |
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| EC: | 3.4.24.22 |
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| UniProt ID: | P09238 |
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| Formulation: | Liquid. In 50mM TRIS, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.5% Brij-35, and 30% glycerol. |
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| Purity Detail: | Partially purified by single-step affinity chromatography and gel filtration. |
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| 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%. |
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| 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. |
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| Application Notes: | Useful tool to study of enzyme kinetics, cleave target substrates, and screen for inhibitors. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Regulatory Status: | RUO - Research Use Only |
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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;
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