Carboxypeptidase B CAS:9025-24-5

Carboxypeptidase B is an enzyme that plays a crucial role in protein digestion and metabolism. Specifically, it catalyzes the hydrolysis of peptide bonds at the C-terminal end of proteins, resulting in the removal of individual amino acids.

Carboxypeptidase B is highly specific for basic amino acids, such as lysine and arginine, and is particularly effective in cleaving these residues. It is commonly found in pancreatic secretions and is involved in the final stage of protein digestion in the small intestine.

This enzyme is also utilized in various laboratory applications, including protein sequencing, peptide synthesis, and protein analysis. The ability of carboxypeptidase B to specifically cleave the C-terminal amino acids of proteins makes it a valuable tool for studying protein structure and function.

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Application and Effect

Protein sequencing: Carboxypeptidase B is used to determine the sequence of amino acids in a protein. By selectively removing C-terminal amino acids one by one, scientists can identify the specific amino acids present in the protein.

Peptide synthesis: Carboxypeptidase B can be used to selectively cleave off C-terminal amino acids during the synthesis of peptides or proteins. This enables the synthesis of customized peptides with desired amino acid sequences.

Protein analysis: Carboxypeptidase B is used in protein characterization studies to determine the presence of C-terminal lysine or arginine residues. This information can be useful in understanding protein structure and function.

Enzyme immobilization: Carboxypeptidase B can be immobilized onto solid supports, such as beads or membranes. This immobilization allows for the continuous enzymatic cleavage of C-terminal amino acids in processes like protein purification or peptide synthesis.

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Additional Information:

Composition	C31H38N4O7S
Assay	99%
Appearance	White powder
CAS No.	9025-24-5
Packing	Small and bulk
Shelf Life	2 years
Storage	Store in cool and dry area
Certification	ISO.