MMP3cat_wt

MMP3 catalytic domain

Human, recombinant.
residues 100-272, swissprot accession P08254
MW = 19500 Da.
EC # 3.4.24.17
CAT # G04MP03C

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G04MP03C none 10 µg 200.00
G04MP03C none 5 x 10µg 400.00

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

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Description
MW = 19.5 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 100-272 swissprot accession P08254).

Sequence
                                        100        110        120
                                        M-F RTFPGIPKWR KTHLTYRIVN
       130        140        150        160        170        180
YTPDLPKDAV DSAVEKALKV WEEVTPLTFS RLYEGEADIM ISFAVREHGD FYPFDGPGNV
       190        200        210        220        230        240
LAHAYAPGPG INGDAHFDDD EQWTKDTTGT NLFLVAAHEI GHSLGLFHSA NTEALMYPLY
       250        260        270
HSLTDLTRFR LSQDDINGIQ SLYGPPPDSP ET


Purity
> 95% by SDS-PAGE. The enzyme was observed as a single band migrating molecular weight of between 29.2 and 19.5 kDa.

Specific activity
> 30U/μg. Activity described as U=100 pmol/min at 37°C using a colorimetric assay with thiopeptolide Ac-Pro-Leu-Gly-[2- mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 (Biomol) as substrate.

Suppied As
0.25mg /ml in 20mM Tris, pH 7.2, 10mM CaCl2, 0.1mM ZnCl2, 0.3M NaCl, 0.2M Acetohydroxamic Acid (AHA). The concentration is calculated from the absorbance at 280nm, (ε280 = 28420 M-1 cm-1).

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

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References
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.

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