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MMP-3 (catalytic domain) (human), (recombinant)

ALX-201-042-C005 5 µg 372.00 USD
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Highly purified recombinant enzyme containing the 22kDa catalytic domain of MMP-3.

Product Details

Alternative Name:Matrix metalloproteinase 3, Stromelysin-1, Transin-1
Source:Produced in E. coli.
UniProt ID:P08254
Formulation:Liquid. In 50mM Tris-HCl, pH 7.5, containing 10mM CaCl2, 1µM ZnCl2 and 0.05% sodium azide.
Purity Detail:No other MMP contaminants are detectable.
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.
Shipping:Dry Ice
Short Term Storage:-20°C
Long Term Storage:-80°C
Use/Stability:Stable for several weeks when stored at  at -20°C and for at least 1 week when stored at at +4°C.
Handling:Avoid freeze/thaw cycles.
Regulatory Status:RUO - Research Use Only

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;

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