Carboxypeptidase A2/CPA2 Protein(C-6His) (recombinant human)

Protein Construction: Recombinant Human Carboxypeptidase A2 is produced by our Mammalian expression system and the target gene encoding Leu17-Tyr417 is expressed with a 6His tag at the C-terminus. Sequence: Leu17-Tyr417. Fusion tag: C-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 50 kDa. Protein function: 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 amino acids 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.