Highly purified recombinant enzyme containing the 22kDa catalytic domain of MMP-3.
Product Details
| Alternative Name: | Matrix metalloproteinase 3, Stromelysin-1, Transin-1 |
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| MW: | ~22kDa. |
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| Source: | Produced in E. coli. |
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| EC: | 3.4.24.17 |
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| UniProt ID: | P08254 |
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| Concentration: | 0.1mg/ml |
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| Formulation: | Liquid. In 50mM Tris-HCl, pH 7.5, containing 10mM CaCl2, 1µM ZnCl2 and 0.05% sodium azide. |
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| Purity Detail: | No other MMP contaminants are detectable. |
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| Specific Activity: | ≥900mU/mg protein (H. Nagase, et al; J. Biol. Chem. 269, 20952 (1994)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(DNP)-NH2 per min. at 37°C, pH 7.0. |
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| Shipping: | Dry Ice |
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| Short Term Storage: | -20°C |
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| Long Term Storage: | -80°C |
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| Use/Stability: | Stable for several weeks when stored at at -20°C and for at least 1 week when stored at at +4°C. |
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| Handling: | Avoid freeze/thaw cycles. |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Functional Roles of N-Linked Glycosylation of Human Matrix Metalloproteinase 9: T. Duellman, et al.; Traffic
16, 1108 (2015),
Abstract;
Full Text
Controlled biodegradation of self-assembling β-hairpin peptide hydrogels by proteolysis with matrix metalloproteinase-13: M.C. Giano, et al.; Biomaterials
32, 6471 (2011),
Abstract;
Full Text
Design and characterization of a fluorogenic substrate selectively hydrolyzed by stromelysin 1 (matrix metalloproteinase-3): H. Nagase, et al.; J. Biol. Chem.
269, 20952 (1994),
Abstract;
Full Text
A trypsin sensitive stromelysin isolated from rheumatoid synovial fluid is an activator for matrix metalloproteinases: H. Kolkenbrock, et al.; Eur. J. Clin. Chem. Clin. Biochem.
31, 625 (1993),
Abstract;
Matrix metalloproteinase-3 (stromelysin-1). Identification as the cartilage acid metalloprotease and effect of pH on catalytic properties and calcium affinity: S.M. Wilhelm, et al.; J. Biol. Chem.
268, 21906 (1993),
Abstract;
Full Text
Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9: Y. Ogata, et al.; J. Biol. Chem.
267, 3581 (1992),
Abstract;
Full Text
Evidence that human rheumatoid synovial matrix metalloproteinase 3 is an endogenous activator of procollagenase: A. Ito & H. Nagase; Arch. Biochem. Biophys.
267, 211 (1988),
Abstract;
Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes: G. Murphy, et al.; Biochem. J.
248, 265 (1987),
Abstract;
