Carboxypeptidase B Producing Recombinant Polypeptide C-terminal
lysine EC 188.8.131.52
Source: Expressed in E. Coli.
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 optimum pH 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
|Source||Recombinant E. coli|
|Appearance||White or off white, or yellowish powder|
|Specific activity||≥170 units/mg pro.|
|Purity(SDS-PAGE)||Single major band|
|Molecular Weight(SDS-PAGE)||33.8±3.4 kDa|
UNIT DEFINITION:One unit of carboxypeptidase B activity hydrolyzes one micromole
ofhippuryl-L-arginine per minute at 25℃, pH 7.65.
Animal origin free:YaxinBio recombinant carboxypeptidase B belongs
to the AOF level 3, eliminate the risk of virus presence, or of any
other potential adventitious agents found in animal-derived
Stability:A sterile recombinant carboxypeptidase B lyophilized
eliminates the risk of contamination and decreases the chances of
activity loss in the process of transport and storage.
1) Recombinant carboxypeptidase B provides increased specific
activity and eliminates contaminating proteases activities found in
extracted enzymes with lower purity level.
2) No other contaminating proteases such as chymotrypsin and
3)Less than 10ppm of recombinant trypsin.