Recombinant Carboxypeptidase B

1. Product Introduction

Recombinant Carboxypeptidase B  is exclusively used for the hydrolysis of protein C-terminal basic amino acids (lysine, arginine, histidine); also known as peptidyl-L-lysine (L -Arginine) hydrolase; sperminase. The molecular weight is 35kD, the isoelectric point is 6.0, and the optimum pH is 7-9. The activity is competitively inhibited by arginine and lysine, and metal ion chelating agents such as EDTA inhibit enzyme activity.

2. Product advantages

No animal origin: recombinant production, no foreign virus contamination, such as swine flu virus, porcine parvovirus, etc.

High purity: no other miscellaneous enzyme activity: no other side reactions in the digestion reaction, high yield

High specific activity: no less than 120 u/mg pro.; no less than 170 u/mg pro.

Electrophoresis purity: SDS-PAGE electrophoresis identification, 95%

Stable: freeze-dried powder, easy to store and transport

Figure 1. Diagram of the production process of different levels of non-animal origin of biological products

Recombinant carboxypeptidase B is a product of non-animal origin AOF3 level

3. Product use

Production of recombinant insulin and its analogues

Determination of protein C-terminal amino acid

Production of other recombinant peptides

Enzymatic synthesis of some special compounds

4. Product features

Source: Recombinant Escherichia coli

Purification: HPLC

Product properties: white or almost white freeze-dried powder

Electrophoresis identification and Coomassie brilliant blue staining

12%SDS-PAGE: molecular weight 35kD, single main band

Specific activity: not less than 120 u/mg pro.; not less than 170 u/mg pro.

Other enzyme content: no chymotrypsin, carboxypeptidase A, etc., trypsin is not detected. Trypsin content is less than 10ppm

Does not contain any protease inhibitors: No protease inhibitors such as PMSF, EDTA, etc.

Figure 2. SDS-PAGE identification and purity analysis of recombinant carboxypeptidase B freeze-dried powder