Human Carboxypeptidase A2/CPA2 (His Tag) recombinant protein

Human Carboxypeptidase A2/CPA2 (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

Human Carboxypeptidase A2 ( CPA2 ) is a secreted pancreatic procarboxy -peptidase, and 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.

Carboxypeptidase A1

CPA2; CARBOXYPEPTIDASE A2

P15085

CPA1; CPA

Human Cells

A DNA sequence encoding the pre pro form of human CPA2 (NP_001859.1) (Met 1-Tyr 417) was expressed with a C-terminal polyhistidine tag.

Human

The secreted recombinant human CPA2 existing as the proform consists of 412 amino acids and has a predicted molecular mass of 46 kDa also as estimated by SDS-PAGE under reducing conditions.

> 90 % as determined by SDS-PAGE

Measured by its ability to cleave a colorimetric peptide substrate, N-acetyl-Phe-Thiaphe-OH (N-Ac-PSP, Peptide International's Catalog# STP-3621-PI), in the presence of 5,5'Dithio-bis (2-nitrobenzoic acid) (DTNB), as measured using the wavelength at 405 nm and the extinction coefficient of 13,260 M-1 cm-1. The specific activity is >4,000 pmoles/min/μg.