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Human Carboxypeptidase A1 / CPA1 Protein (His Tag)

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Human CPA1 Protein Product Information
Synonym:CPA, CPA1
Protein Construction:A DNA sequence encoding the human CPA1 precursor (NP_001859.1) (Met 1-Tyr 419) 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.
Human CPA1 Protein QC Testing
Purity:> 97 % 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 5,5'Dithiobis (2-nitrobenzoic acid) (DTNB). The specific activity is >3,500 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:Lys 17
Molecule Mass:The secreted recombinant human CPA1 (pro form) consists of 414 amino acids and has a predicted molecular mass of 47 kDa. In SDS-PAGE under reducing conditions, it migrates with the apparent molecular mass of 43 kDa.
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.
Human CPA1 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.
Human CPA1 Protein SDS-PAGE
Human Carboxypeptidase A1 / CPA1 Protein (His Tag) SDS-PAGE
Other CPA1 Recombinant Protein Products
Carboxypeptidase A1/CPA1 Background

Human Carboxypeptidase A1 (CPA1)is secreted as a pancreatic procarboxypeptidase, and cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group, with the preference of  residues with aromatic or branched aliphatic side chains. CPA1 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E, and is involved in zymogen inhibition. Three different forms of human pancreatic procarboxypeptidase A have been isolated.

Human Carboxypeptidase A1/CPA1 References
  • Catasus, L. et al., 1992, Biochem. J. 287: 299-303.
  • Moulard, M. et al., 1990, FEBS. Lett. 261: 179-183.
  • Aloy, P. et al., 1998, Biol. Chem. 379: 149-155.
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    Catalog: 10504-H08H-10
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