Carboxypeptidase B (CPB) is a metallocarboxypeptidase that specifically hydrolyzes the amino terminus of the C-terminal basic amino acids (lysine, arginine, and ornithine) of polypeptides.

Product Introduction

Carboxypeptidase B, also known as peptidyl-L-lysine (L-lysine) hydrolase, specifically hydrolyzes the amino terminus of protein C-terminal basic amino acids (lysine (Lysine, K), arginine (Arginine, R), and histidine (H)). This product is produced by the fermentation and expression of Escherichia coli or Pichia pastoris. It has no His-tag, and the optimal pH is 7.5-9.0. The activity of carboxypeptidase B is competitively inhibited by arginine and lysine, and metal ion chelating agents such as EDTA inhibit enzyme activity.

Product Application

1. Protein C-terminal amino acid sequencing.

2. Removal of protein C-terminal histidine tag.

3. Used in the production and preparation of recombinant insulin and its analogs and GLP-1 drugs.

4. The productionof other recombinant peptide substances.

Product Advantages

1. High quality: high purity, high specific activity, no residue.

2. GMP production: GMP-grade products can be provided.

3. Customized specifications: specifications can be customized according to customer quality requirement.

4. Stable supply: Stable quality control and long-term supply.

Storage

Freeze-dried powder is stored at 2~8℃ and is valid for two years.

Recommendation

1. Since each freezing and thawing of the protein will cause partial inactivation, after first dissolving it in the storage buffer to prepare a storage solution of corresponding concentration, it must be aliquoted, protected from light, and frozen at -20°C, -70°C or lower to avoid repeated freezing and thawing, and it will be more stable within 6 months.

2. Please refer to the relevant literature for the specific optimal working concentration or explore and optimize it through experiments according to the purpose of the experiment and specific cells and animals.

3. Do not shake vigorously with vortex to avoid protein denaturation and inactivation.