| 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 >4,000 pmol/min/µg, as measured under the described conditions. |
| Source | Mouse myeloma cell line, NS0-derived human Carboxypeptidase A2/CPA2 protein Leu17-Tyr417, with a C-terminal 10-His tag |
| Accession # | |
| N-terminal Sequence | Leu17 |
| Structure / Form | Pro form |
| Protein/Peptide Type | Recombinant Enzymes |
| Gene | CPA2 |
| 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 | 46 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. |
| SDS-PAGE | 43 kDa, reducing conditions |
| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from 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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| Reconstitution Instructions | Reconstitute at 200 μg/mL in 25 mM Tris and 150 mM NaCl, pH 7.5. |
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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 A2 encoded by the CPA2 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 side chains including Phe, Tyr, and Trp. The deduced amino acid sequence of human CPA2 consists of a signal peptide (residues 1 to 16), a pro region (residues 17 to 112), and a mature chain (residues 113 to 417). The purified rhCPA2 corresponds to the pro form, which can be activated and assayed under the conditions described in the Activity Assay Protocol.
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