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Mouse Carboxypeptidase A2 / CPA2 Protein (His Tag)

CPA2

Catalog Number P50778-M08H
Organism Species Mouse
Host Human Cells
Synonyms CPA2
Molecular Weight The secreted recombinant mouse CPA2 (pro form) comprises 412 amino acids and has a calculated molecular mass of 46.6 kDa. It migrates as an approximately 47 kDa in SDS-PAGE under reducing conditions.
predicted N Gln 17
SDS-PAGE
Purity > 92 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mouse CPA2 (Q504N0) (Met 1-Tyr 417) was expressed, with a C-terminal polyhistidine tag.
Bio-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.
Research Area Cancer |Oncoprotein & suppressor & biomarker |Tumor biomarker |Other in cancer biomarker |Globulin
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background 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.
Reference
  • Catasus, L. et al., 1995. J. Biol. Chem. 270: 6651-6657.
  • Aloy, P. et al., 1998, Biol. Chem. 379: 149-155.
  • Laethem, RM. et al., 1996, Arch. Biochem. Biophys.332: 8-18.