MMP14 catalytic domain, mutant with improved stability

Human, recombinant.
residues 114-290, swissprot accession P50281
MW = 20000 Da.
EC #
CAT # G04MP14Cm

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G04MP14Cm none 10 µg 200.00
G04MP14Cm none 5 x 10 µg 400.00

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

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MW = 20 kDa. Recombinant matrix metalloproteinase-14 (MMP-14, Membrane-Type Matrix Metalloproteinase1, MT1- MMP) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-14 (residues 114-290 swissprot accession P50281) with a C-term purification tag. The protein has been mutated to increase the stability. The catalytic activity rates are not affected by the mutation. The C-terminal tag is cleaved during purification.

> 95% by SDS-PAGE. The protein was observed as a single band migrating at a molecular weight of between 29.2 and 14.4 kDa.

Specific activity
> 150U/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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M. Gioia et al. J Mol Biol. 2007 May 11;368(4):1101-13.
K. Lehti et al. J. Biol. Chem. 2000, 275:15006-13.
G. Murphy and V. Knäuper Matrix Biol. 1997, 15, 511.
W. Bode et al. Cell Mol Life Sci 1999, 55:639-52.

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