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MMP-10 (catalytic domain) (human), (recombinant)

 
BML-SE329-0010 10 µg 384.00 USD
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Product Specification

Alternative Name:Matrix metalloproteinase 10, Stromelysin-2
 
MW:19.4 kDa
 
Source:Produced in E. coli. Active Matrix Metalloproteinase-10 (MMP-10, stromelysin-2, transin-2) catalytic domain from human cDNA. The enzyme consists of the catalytic domain of human MMP-10 (Phe99-Glu271, NM_2425) with a C-terminal purification tag. This comprises an active form of MMP-10 which lacks the C-terminal hemopexin domain. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected.
 
EC:3.4.24.22
 
UniProt ID:P09238
 
Formulation:Liquid. In 50mM TRIS, 5mM CaCl2, 300mM NaCl, 20µM ZnCl2, 0.5% Brij-35, and 30% glycerol.
 
Purity Detail:Partially purified by single-step affinity chromatography and gel filtration.
 
Activity:Preincubation of MMP-10 catalytic domain at 22nM with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 100nM for 1 hour inhibits enzymatic activity by 95%.
 
Specific Activity:≥18 U/µg. One U=100 pmol/min at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100 µM; Prod No. BML-P125) as substrate.
 
Application Notes:Useful tool to study of enzyme kinetics, cleave target substrates, and screen for inhibitors.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 

Product Literature References

Matrix metalloproteinase-10 is a critical effector of protein kinase Ciota-Par6alpha-mediated lung cancer: L.A. Frederick, et al.; Oncogene 27, 4841 (2008), Abstract; Full Text

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