Carboxypeptidase B Enzymatic Synthesis of Specific Compounds
Producing Recombinant Polypeptide
Recombinant rat carboxypeptidase B
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, pI is 6.0 and the
optimum pH is 7.5-9.0. Carboxypeptidase B is competitively
inhibited by arginine and lysine. The enzyme is also inhibited by
metal chelating agents, e.g., EDTA. YaxinBio has cloned rat
carboxypeptidase B gene into E.coli for expression with equivalent properties compared to animal
original carboxypeptidase B .Recombinant carboxypeptidase B can
replace native carboxypeptidase B for using in a variety of
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.
Tris salts, NaCl salts and carbohydrates
35% ～ 60%
Single main band on SDS-PAGE
Less than 10 ppm of recombinant trypsin.
Unit Definition:One Unit of carboxypeptidase B activity hydrolyzes one micromole of
hippuryl-L-arginine per minute at 25℃, pH 7.65.