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

 
ALX-201-042-C005 5 µg 283.00 USD
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Highly purified recombinant enzyme containing the 22kDa catalytic domain of MMP-3.

Product Specification

Alternative Name:Matrix metalloproteinase 3, Stromelysin-1, Transin-1
 
MW:~22kDa.
 
Source:Produced in E. coli.
 
EC:3.4.24.17
 
UniProt ID:P08254
 
Concentration:0.1mg/ml 
 
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:Shipped on 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.
 

Product Literature References

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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