Carboxypeptidase A1 (CPA1) is secreted as a pancreatic peptidase that comes from the precursor form of inactive procarboxypeptidase. CPA1 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. It has a free C-terminal carboxyl group, with the preference of residues with aromatic or branched aliphatic side chains. CPA1 cleaves the C-terminal amide or ester bond of peptides and involves in zymogen inhibition. Three different forms of human pancreatic procarboxypeptidase A have been isolated. 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.
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
10 μg | 5 days | $ 184.00 | |
50 μg | 5 days | $ 545.00 | |
500 μg | 5 days | $ 1,900.00 | |
1 mg | 5 days | $ 2,730.00 |
Description | Carboxypeptidase A1 (CPA1) is secreted as a pancreatic peptidase that comes from the precursor form of inactive procarboxypeptidase. CPA1 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. It has a free C-terminal carboxyl group, with the preference of residues with aromatic or branched aliphatic side chains. CPA1 cleaves the C-terminal amide or ester bond of peptides and involves in zymogen inhibition. Three different forms of human pancreatic procarboxypeptidase A have been isolated. 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. |
Species | Human |
Expression System | Human Cells |
Tag | C-6His |
Accession Number | AAH05279.1 |
Synonyms | CPA, Carboxypeptidase A1, CPA1 |
Amino Acid | Lys17-Tyr419 |
Construction | Recombinant Human Carboxypeptidase A1 is produced by our Mammalian expression system and the target gene encoding Lys17-Tyr419 is expressed with a 6His tag at the C-terminus. |
Molecular Weight | 44 KDa, reducing conditions |
Endotoxin | Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
Formulation | Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mm NaCl, pH 7.5. |
Stability & Storage |
Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles. |
Shipping |
The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below. |
Research Background | Carboxypeptidase A1 (CPA1) is secreted as a pancreatic peptidase that comes from the precursor form of inactive procarboxypeptidase. CPA1 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. It has a free C-terminal carboxyl group, with the preference of residues with aromatic or branched aliphatic side chains. CPA1 cleaves the C-terminal amide or ester bond of peptides and involves in zymogen inhibition. Three different forms of human pancreatic procarboxypeptidase A have been isolated. 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. |
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CPA1 Protein, Human, Recombinant (His) CPA 1 CPA-1 CPA Carboxypeptidase A1 CPA1 recombinant recombinant-proteins proteins protein