MMP7 catalytic domain

Human, recombinant.
residues 95-267, swissprot accession P09237
MW = 19200 Da.
EC #
CAT # G04MP07C

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G04MP07C none 10 µg 200.00
G04MP07C none 5 x 10 µg 400.00

Special prices for bulk quantities, or labelled samples, available upon request.

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MW = 19.2 kDa. Recombinant matrix metalloproteinase-7 (MMP-7, matrilysin, uterine metalloproteinase) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-7 (residues 95-267 Swissprot accession P09237).

> 95% by SDS-PAGE. The protein was observed as a single band migrating at a molecular weight of between 19.5 and 14.4 kDa.

Supplied As
0.2mg/ml inTris 20mM pH 7.2, CaCl2 10mM, ZnCl2 0.1mM, NaCl 0.3M, Acetohydroxamic Acid (AHA) 0.5M. The concentration is calculated from the absorbance at 280nm, (ε280 = 33920 M-1 cm-1).

Specific activity
> 8U/μg. Activity described as U=100 pmol/min at 25°C using a colorimetric assay with thiopeptide Ac-Pro-Leu-Gly-[2- mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 (Biomol) as substrate.

Enzyme kinetic studies, cleavage of target substrates and screening of inhibitors.

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L. Ou et al. J Biomol NMR. 2004 Aug; 29(4):537-8.
M.F. Browner, W.W. Smith, A.L. Castelhano. Biochemistry. 1995 May 23; 34(20):6602-10.
L.J. McCawley and L.M. Matrisian. Curr. Opin. Cell Biol. 2001, 13, 534.
W.G. Stetler-Stevenson and A.E. Yu. Semin. Cancer Biol. 2001, 11, 143.

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