CPA4 Human

CPA4 is a secreted enzyme that removes the C-terminal amino acid from peptides having a free C-terminal carboxyl group. It can hydrolyze both amide and ester bonds and has a preference for cleavage at the amino side of hydrophobic residues . The enzyme is characterized by its zinc-binding site, which is essential for its catalytic activity.

Recombinant human CPA4 is produced using a mouse myeloma cell line, NS0, which expresses the human CPA4 protein. The recombinant protein is typically tagged with a C-terminal 10-His tag to facilitate purification . The recombinant form is often used in research to study the enzyme’s function and potential therapeutic applications.

Recombinant CPA4 is used in various biochemical assays to study its enzymatic activity. One common assay involves the cleavage of a colorimetric peptide substrate in the presence of 5,5’-dithio-bis (2-nitrobenzoic acid) (DTNB), which allows for the measurement of the enzyme’s activity . The enzyme’s ability to cleave specific peptide bonds makes it a valuable tool in protein and peptide research.

The recombinant CPA4 protein is supplied as a filtered solution in Tris and NaCl and should be stored at -20 to -70°C to maintain its stability. It is important to avoid repeated freeze-thaw cycles to preserve the enzyme’s activity .