Human CPA2 (His tag) recombinant protein

Human CPA2 (His tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

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.

carboxypeptidase A2(CPA2)

P48052

Human Cells

A DNA sequence encoding the Human CPA2 Leu17-Tyr417 is expressed with a 6His tag at the C-terminus.

Human

>95% as determined by SDS-PAGE.