MMP3 catalytic domain, inactive mutant

Human, recombinant.
residues 105-265, swissprot accession P08254
MW = 18000 Da.
EC #
CAT # G04MP03Ci

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G04MP03Ci none 10 µg 200.00
G04MP03Ci none 5 x 10 µg 400.00

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

(▲ Top)

MW = 18 kDa. Recombinant matrix metalloproteinase-3 (MMP-3, stromelysin-1, transin) cloned from human cDNA, expressed in E.coli. The enzyme consists of the catalytic domain of human MMP-3, residues 105-265 (Swissprot accession P08254). The enzyme has been inactivated by mutagenesis (E219A). This product is derived from MMP-3 Catalytic domain, and contain also the mutation F171D 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 enzyme was observed as a single band migrating at a molecular weight of < 20 kDa.

Supplied as
0.2mg/ml in Tris 20mM pH 7.2, CaCl2 10mM, ZnCl2 0.1mM, NaCl 0.3M, Acetohydroxamic Acid (AHA) 0.2M. The concentration is calculated from the absorbance at 280nm (ε280 = 28420 M-1 cm-1).

Specific activity
Not detected. Activity described as U=100 pmol/min at 25°C using a colorimetric assay with thiopeptolide 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.

(▲ Top)

L.L. Johnson et al. J. Biol. Chem. 2000, 275, 11026.
L.Chen et al. J. Mol. Biol. (1999) 293, 545-557.
H. Weingarten and J. Feder Anal. Biochem. 1985, 147, 437.
H. Weingarten et al. Biochemistry. 1985, 24, 6730.

(▲ Top)