DESCRIPTIONS
Carboxypeptidase B catalyzes hydrolysis of the basicamino acids lysine, arginine and histidine from the Cterminal of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0. Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is inhibited by metal chelating agents, e.g., EDTA. Recombinant Carboxypeptidase B (EC 3.4.17.2) is expressed in E.Coli and purified by high pressure liquid chromatography. There is no foreign enzyme activity such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF contain in preparation.
SALIENT ADVANTAGES
Animal origin free
Recombinant carboxypeptidase B eliminates the risk of viruses, or other potential adventitious agents found in animal derived carboxypepitdase B. Which belong to the AOF level 3 products.
Stable
A sterile recombinant carboxypeptidase B lyophilized powder eliminates the contamination opportunity and decreases the chance of activity loss in the process of transport and storage. Convenient for transport and store.
High purity
1)Recombinant carboxypeptidase B provides increased specificity and eliminates contaminating activities found in lower purity enzymes
2)No other proteases contaminated such as chymotrypsin, carboxypeptidase A, and the content of recombinant trypsin less than 10ppm.
SALIENT FEATURES
White or white-like lyophilized powder
Tris salts, NaCl salts and carbohydrates.
No chymotrypsin, carboxypeptidase A, and other protease contaminant.
The content of recombinant trypsin is less than 10ppm.
3)One single main band at 35kD by SDS-PAGE.
PRODUCTS INFORMATION
UNIT DEFINITION：One Unit of carboxypeptid
ase B activity hydrolyzes one micromole of
hippuryl-L-arginine per minute at 25℃, pH 7.65.
RELATIVE PRODUCTION: Recombinant Porcine Trypsin