MMP13 catalytic domain, mutant with improved stability

Human, recombinant.
residues 104-268, swissprot accession P45452
MW = 18500 Da.
EC #
CAT # G04MP13Cm

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G04MP13Cm none 10 µg 200.00
G04MP13Cm none 5 x 10 µg 400.00

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

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MW = 18.5 kDa. Recombinant matrix metalloproteinase-13 (MMP-13, collagenase-3, col3) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-13 (residues 104-268 swissprot accession P45452). This product is derived from MMP-13 Catalytic domain and contain also the mutation F175D to increase its stability and solubility. No residual enzyme activity has been detected using the method described in the specific activity section of this data sheet.

> 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.

Specific activity
> 40U/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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V. Knäuper et al. J. Biol. Chem. 1997, 272, 7608.
F.J.Moy et al. J Mol Biol. 2000 Sep 22; 302(3):671-89.
S. Cowell et al. Biochem. J. 1998, 331, 453.
G. Murphy and V. Knäuper Matrix Biol. 1997, 15, 51.

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