MMP3 - catalytic domain

210,00680,00

Human, recombinant
Residues 100-272, UniProtKB accession P08254
MW = 19.5 kDa
EC # 3.4.24.17
CAT # G04MP03C

SKU: G04MP03C Categories: , Tags: , , , , ,
Catalog n.QtyPrice
210,00
420,00
680,00
VAT not included

For any special request or bulk quantities Click Here

Additional information

Qty

10 μg, 5 x 10 μg, 100 μg

Shipping in Dry Ice

yes

Description

Description
MW = 19.5 kDa calculated. 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, UniProtKB 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

Available mutants
F171D – mutant with improved stability – CAT # G04MP03Cm
F171D, E219A – inactive mutant with improved stability – CAT # G04MP03Ci

Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 18.4 and 25.0 kDa.

Suppied As
0.2 mg/mL solution in Tris 20 mM, pH 7.2, CaCl2 10 mM, ZnCl2 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.2 M. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 28420 M-1cm-1 calculated).

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.

Storage
-80°C. After initial defrost, aliquot the product into individual tubes and refreeze at -80°C.
Avoid repeated freeze/thaw cycles.

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

 RELEATED RESEARCH FIELDS

 

References
Johnson, L.L. et al. J. Biol. Chem. 275 (15), 11026-11033 (2000).
Chen, L. et al. J. Mol. Biol. 293 (3), 545-557 (1999).
Weingarten, H. & Feder, J. Anal. Biochem. 147 (2), 437-440 (1985).
Weingarten, H., Martin, R. & Feder, J. Biochemistry 24 (23), 6730-6734 (1985).
Social media & sharing icons powered by UltimatelySocial

By continuing to use the site, you agree to the use of cookies. more information

The cookie settings on this website are set to "allow cookies" to give you the best browsing experience possible. If you continue to use this website without changing your cookie settings or you click "Accept" below then you are consenting to this.

Close