Product Details
| Alternative Name: | Matrix metalloproteinase 3, Stromelysin-1, Transin-1 |
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| MW: | 19.5kDa |
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| Source: | Produced in E. coli. Active Matrix Metalloproteinase-3 (MMP-3, stromelysin-1, transin) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-3 (Phe100-Thr272, NM_002422) with a C-terminal purification tag. |
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| EC: | 3.4.24.17 |
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| UniProt ID: | P08254 |
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| Formulation: | Liquid. In 50mM TRIS, pH 7.5, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.05% Brij-35. |
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| Purity: | ≥95% (SDS-PAGE) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Specific Activity: | ≥350 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: | Study 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
Development and validation of novel enzyme activity methods to assess inhibition of matrix metalloproteinases (MMPs) in human serum by antibodies against enzyme therapeutics: T.J. Edkins, et al.; J. Pharm. Biomed. Anal.
70, 408 (2012),
Abstract;
The effect of a hydroxamic acid-containing polymer on active matrix metalloproteinases: G.A. Skarja, et al.; Biomaterials
30, 1890 (2009),
Abstract;
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