Carboxypeptidase A2 (Pancreatic) (CPA2) (C-Term), (AA 115-417) protein
Description
Recombinant Human Carboxypeptidase A2/CPA2 is produced with our mammalian expression system in human cells. The target protein is expressed with sequence (Ser115-Tyr417) of Human CPA2 fused with a polyhistidine tag at the C-terminus. Carboxypeptidase A2 (CPA) is a secreted pancreatic procarboxy-peptidase that cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic AAs in their C-terminal end, particularly tryptophan. CPA2 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. Three different forms of human pancreatic procarboxypeptidase A have been isolated, and the A1 and A2 forms are always secreted as monomeric proteins with different biochemical properties. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E, and is involved in zymogen inhibition.