Recombinant Carboxypeptidase B in E.coli Carboxypeptidase B for Mass
Carboxypeptidase B catalyzes hydrolysis of the basic amino acids
lysine, arginine and histidine from the C-terminal end of
polypeptides. The molecular weight is 33.8kD, the pH optimum is
8.0, and pI is 6.0. Carboxypeptidase B is competitively inhibited
by arginine and lysine. The enzyme is also inhibited by metal
chelating agents, e.g., EDTA. Recombinant Carboxypeptidase B is
expressed in E.Coli and purified by high pressure liquid
chromatography. There is no trace of other enzyme (such as
carboxypeptidase A and chymotrypsin) activity. No protease
inhibitors such as PMSF are present in the preparation.
Purity: Greater than 95% as determined by SDS-PAGE.
Unit Definition: One Unit hydrolyzes one micromole of
hippuryl-L-arginine per minute at 25°C, pH-7.65.
Bilogical Activity:170 units/mg protein.
Protein structure and sequence analysis, such as hydrolyze basic
amino acids lysine, arginine and histidine from the C-terminal end
Antibody quality control.
Prepare 1-10mg/ml carboxypeptidase B with sterile water or 25mM
Tris-HCl pH 7.65. The ratio to aimed protein is 1:50 to 1:1000
(w/w), the optimum pH is pH 7-9.
Stability:Recombinant Rat Carboxypeptidase-B although stable at
room temp for 1 week, should be stored desiccated below under 2-8℃ in sealed container. For long term storage it is recommended to be stored under -20℃. Please prevent freeze-thaw cycles.