Recombinant Carboxypeptidase B | Introduction |
Reorganization: Carboxypeptidase Enzyme B can be used for the production of recombinant insulin. Using recombinant human proinsulin expression is modeled on the natural pathway to synthesize insulin, mainly divided into: Base engineering bacteria for enzymatic cleavage. Carboxypeptidase Enzyme B is a serine protease specifically hydrolyzed protein C-terminal basic amino acids (Lysine (K), Arginine (R), Histidine (H)). In the process of proinsulin, Carboxypeptidase Enzyme B cuts off the C-chain. |
| Product Advantage |
Free of animal origin: recombinant production, no exogenous virus contamination, rawproduction process does not use any raw materials of animal origin. Quality: Mass production can ensure stable and continuous batch production; there is no difference between product batches and the quality is stable. Purity: specific activity is high; host protein residue is less than the limit requirement of biological products. Freeze dried powder: easy to store and transport. Compliance with regulatory requirements: The production equipment and production environment comply with relevant regulatory requirements, and the production process is fully followed. NSF ISO 9001: 2015quality system and comply GMP guiding principles. Quality documents complete: According to customer needs, can provide relevant regulatory support documents. |
| Enzymatic Properties | It has an animal-derived carboxypeptidaseBthe same enzymatic properties, can replace the animal-derived carboxypeptidase B which is used in various biotechnological processes. |
| Basic Characteristics | Again. called peptidyl-L-lysine (L-arginine) hydrolase; spermin protease. The molecular weight is 33.8kD, the isoelectric point is 6.0, the most suitable pH7.5-9.0. The activity is competitively inhibited by arginine, lysine, and metal ion chelating agents suchEDTAand other inhibition of enzyme activity. |
| Method of Use |
With sterile water or 25mM Tris-HCl (pH 7.6) solubilized recombinant carboxypeptidase B, so that the concentration of enzyme solution is 1-10mg/ml; Enzyme quantity: target protein (mass ratio)= 1: 50-1000, the most suitable pH7.5-9.0. |
| Sizes | 1mg; 10mg; 100mg; 1g |
| Cutting Sites | Carboxypeptidase B specifically hydrolyzes the C-terminal basic amino acids of proteins, including lysine (Lysine, K), arginine (Arginine, R), and histidine (Histidine, H). |
| Amino Acid Sequence | Recombinant Carboxypeptidase B is produced by recombinant Escherichia coli expression, amino acid sequence and rat pancreatic carboxypeptidase B completely consistent. |
| Appearance | White, almost white, like yellow powder |
| Specific Activity | ≥ 170 USP units/mg pro. |
| Protein Electrophoresis | Single Master Strip |
| Molecular Weight (Protein Electrophoresis) | 33.8±3.4 kDa |
| Storage | Storage stability: Recombinant Carboxypeptidase B freeze-dried powder stored in 2-8°C, 24 months; with sterile water or 25 mM Tris-HCl (pH 7.6). Dissolved and stored in -20°C, repeated freezing and thawing 10 times, no loss of activity. |
| Transportation | Transport stability: blue ice insulation transport, stable activity. |
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