|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Cpa1, 0910001L12Rik, Cpa|
|A DNA sequence encoding the mouse CPA1 (NP_079626.2) (Met 1-Tyr 419) precusor was expressed with a C-terminal polyhistidine tag.|
|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.
|> 96 % as determined by SDS-PAGE|
|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 >6,000 pmoles/min/μg .|
|< 1.0 EU per μg of the protein as determined by the LAL method|
|Samples are stable for up to twelve months from date of receipt at -70℃|
|The secreted recombinant pro form of mouse CPA1 comprises 414 amino acids and has a calculated molecular mass of 47 kDa. The recombinant protein migrates as an approximately 42 kDa band in SDS-PAGE under reducing conditions.|
|Lyophilized from sterile 20mM Tris, 150mM NaCl, pH 7.5|
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.
|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.|
|A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
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.