| Reactivity | HuSpecies Glossary |
| Applications | Enzyme Activity |
| Format | Carrier-Free |
| Details of Functionality | Measured by its ability to cleave the colorimetric peptide substrate Ac-Phe-Thiaphe-OH in the presence of 5,5’Dithio-bis (2-nitrobenzoic acid) (DTNB). Edwards, K.M. et al. (1999) J. Biol. Chem. 274:30468. The specific activity is >3,000 pmol/min/µg, as measured under the described conditions. |
| Source | Mouse myeloma cell line, NS0-derived human Carboxypeptidase A1/CPA1 protein Lys17-Tyr419, with a C-terminal 10-His tag |
| Accession # | |
| N-terminal Sequence | Lys17 |
| Structure / Form | Pro form |
| Protein/Peptide Type | Recombinant Enzymes |
| Gene | CPA1 |
| Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
| Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 47 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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| SDS-PAGE | 42 kDa, reducing conditions |
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| Publications |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Supplied as a 0.2 μm filtered solution in Tris and NaCl. |
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| Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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| Assay Procedure |
*Adjusted for Substrate Blank **Using the extinction coefficient 13260 M-1cm-1 ***Using the path correction 0.32 cm Note: the output of many spectrophotometers is in mOD Per Well:
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Carboxypeptidase A1 encoded by the CPA1 gene cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group (1). It prefers the C-terminal residues with aromatic or branched aliphatic side chains including Phe, Tyr, Trp, Leu or Ile. It is important in the degradation of food proteins to produce essential amino acids such as Phe and Trp. The deduced amino acid sequence of human CPA1 consists of a signal peptide (residues 1 to 16), a pro region (residue 17 to 110), and a mature chain (residues 111 to 419). The purified recombinant human CPA1 corresponds to the pro form, which can be activated as described in Activity Assay Protocol.
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