MMP2 - catalytic domain fibronectin deficient[产品打印页面]

Description
MW = 17.5 kDa calculated. Matrix Metalloproteinase-2 (MMP-2, Gelatinase A, Type IV collagenase) catalytic domain without fibronectin 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 residue numbers are based on the unprocessed precursor, UniProtKB 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     447
AAHEFGHAMG LEHSQDPGAL MAPIYTYTKN FRLSQDDIKG IQELYGA

Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 14.4 and 18.4 kDa.

Supplied as
0.15 mg/mL solution in Tris 20 mM pH 7.2, CaCl2 10 mM, ZnCl2 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.5 M, glycerol 10%, Brij-35 0.05%. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280= 32430 M-1cm-1 calculated).

Specific activity
> 40U/μg. Activity described as U=100 pmol/min at 25°C using a colorimetric ***** with thiopeptide 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.