Carboxypeptidase B. Enzymatic Synthesis of Specific Compounds, Producing Recombinant Polypeptide

Carboxypeptidase B, Enzymatic Synthesis of Specific Compounds  Producing Recombinant Polypeptide

Recombinant rat carboxypeptidase B

DESCRIPTION

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 biotechnological processes.

Advantages

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 carboxypeptitase B

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.

High purity:

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 carboxypeptidase A.

3)Less than 10ppm of recombinant trypsin.

Main Features

Unit Definition:One Unit of carboxypeptidase B activity hydrolyzes one micromole of hippuryl-L-arginine per minute at 25℃, pH 7.65.