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Mouse Carboxypeptidase A2 / CPA2 Protein (His Tag)

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Mouse CPA2 Protein Product Information
Protein Construction:A DNA sequence encoding the mouse CPA2 (Q504N0) (Met 1-Tyr 417) was expressed, with a C-terminal polyhistidine tag.
Expressed Host:Human Cells
Shipping: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.
Mouse CPA2 Protein QC Testing
Purity:> 92 % as determined by SDS-PAGE
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.
Endotoxin:< 1.0 EU per μg of the protein as determined by the LAL method
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:Gln 17
Molecule Mass: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.
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.
2. Please contact us for any concerns or special requirements.
Mouse CPA2 Protein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Mouse CPA2 Protein SDS-PAGE
Mouse Carboxypeptidase A2 / CPA2 Protein (His Tag) SDS-PAGE
Other CPA2 Recombinant Protein Products
Carboxypeptidase A2/CPA2 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.

Mouse Carboxypeptidase A2/CPA2 References
  • 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.
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    Catalog: 50778-M08H-100
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