Carboxypeptidase A2 Protein, Human, Recombinant (His Tag)

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.

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.

Lyophilized from sterile 25mM Tris, 0.15mM NaCl, pH 7.4 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.

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.

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.