Recombinant Human Carboxypeptidase A2/CPA2 Protein (His Tag)(Active)
SKU: PKSH031569-50
Recombinant Human Carboxypeptidase A2/CPA2 Protein (His Tag)(Active)
SKU # | PKSH031569 |
Expression Host | HEK293 Cells |
Description
Synonyms | CPA2, Carboxypeptidase A2 |
Species | Human |
Expression Host | HEK293 Cells |
Sequence | Met 1-Tyr 417 |
Accession | NP_001860.2 |
Calculated Molecular Weight | 46.0 kDa |
Observed Molecular Weight | 46 kDa |
Tag | C-His |
Bio-activity | 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-The specific activity is > 4, 000 pmoles/min/μg. |
Properties
Purity | > 90 % as determined by reducing SDS-PAGE. |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
Formulation | Lyophilized from sterile 25mM Tris, 0.15mM NaCl, pH 7.4 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 printed manual. |
Reconstitution | Please refer to the printed manual for detailed information. |
Background
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.