MMP2cat

MMP-2 CatalYtic Domain, Fibronectin Deficient

Human, recombinant.
residues 115-214 and 393-447 (residues numbers are based on the unprocessed precursor), swissprot accession P08253
MW = 17900 Da.
EC # 3.4.24.24
CAT # G04MP02C

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G04MP02C none 10 µg 200.00
G04MP02C none 5 x 10µg 400.00

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

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Description
MW = 17.9 kDa calculated. Matrix Metalloproteinase-2 (MMP-2, Gelatinase A, Type IV collagenase) catalytic domain without fibronectins domains cloned from human cDNA, expressed in E.coli. The enzyme consists of the catalytic domain of human MMP-2 fibronectin deficient (residues 115-214 and 393-447 where the residues numbers are based on the unprocessed precursor). Swiss prot accession: P08253.

Sequence
                  120        130        140        150
             M-RKPKWD KNQITYRIIG YTPDLDPETV DDAFARAFQV 
       160        170        180        190        200
WSDVTPLRFS RIHDGEADIM INFGRWEHGD GYPFDGKDGL LAHAFAPGTG 
       210     
VGGDSHFDDD ELWT                                    400
                                              QGYSLFLV 
       410        420        430        440        450
AAHEFGHAMG LEHSQDPGAL MAPIYTYTKN FRLSQDDIKG IQELYGASPD

Purity
> 95% by SDS-PAGE. The protein was observed as a single band migrating at a molecular weight 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.

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

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References
Cheng D. et al. Protein Expr Purif. 2003 Jan;27(1):63-74
Steffensen B. at al. J Biol Chem. 1995 May 12;270(19):11555-66
Banyai L. et al. FEBS Lett. 1991 Apr 22;282(1):23-5.

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