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

 
BML-SE109-0010 10 µg 384.00 USD
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Product Specification

Alternative Name:Matrix metalloproteinase 3, Stromelysin-1, Transin-1
 
MW:19.5kDa
 
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.
 
EC:3.4.24.17
 
UniProt ID:P08254
 
Formulation:Liquid. In 50mM TRIS, pH 7.5, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.05% Brij-35.
 
Purity:≥95% (SDS-PAGE)
 
Purity Detail:Purified by multi-step chromatography.
 
Specific Activity:≥10 U/µg. One U=100 pmol/min at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100µM; Prod. No. BML-P125) as substrate.
 
Application Notes:Study enzyme kinetics, cleave target substrates, and screen for inhibitors.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 

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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