Carboxypeptidase A2 Protein (recombinant mouse)

Activity: Measured by its ability to cleave the colorimetric peptide substrate Ac-Phe-Thiaphe-OH in the presence of DTNB.The specific activity is >4000 pmoles/min/µg. Protein Construction: Recombinant Mouse Carboxypeptidase A2 is produced by our Mammalian expression system and the target gene encoding Gln17-Tyr417 is expressed with a 6His tag at the C-terminus. Sequence: Gln17-Tyr417. Fusion tag: C-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 41-50 kDa. Protein function: Mouse carboxypeptidase A2(CPA2) is a secreted pancreatic procarboxy -peptidase which belongs to the peptidase M14 family. CPA2 consists of a signal peptide, a pro region and a mature chain. It can be activated after cleavage of the pro peptide. CPA2 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.