Recombinant Human Carboxypeptidase A2/CPA2 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant Human Carboxypeptidase A2/CPA2 Protein, CF Summary

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.

Applications/Dilutions

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

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Tris and NaCl.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 200 μg/mL in 25 mM Tris and 150 mM NaCl, pH 7.5.
Assay Procedure
  • Assay Buffer: 50 mM Tris, 150 mM NaCl, 10 mM CaCl2, 0.05% (w/v) Brij-35, pH 7.5 (TCNB)
  • Recombinant Human Carboxypeptidase A2/CPA2 (rhCPA2) (Catalog # 2896-ZN)
  • Trypsin (Sigma, Catalog # T-1426)
  • Substrate: Ac-Phe-Thiaphe-OH (Peptides International, Catalog # STP-3621-PI),10 mM stock in DMSO
  • 5,5’-dithio-bis(2-nitrobenzoic acid) (DTNB), (Sigma, Catalog # D-8130) 10 mM stock in DMSO
  • 96 well clear plate (Costar, Catalog # 92592)
  • Plate Reader (Model: SpectraMax Plus by Molecular Devices) or equivalent
  1. Dilute rhCPA2 to 100 µg/mL with 1.0 µg/mL Trypsin in Assay Buffer.
  2. Incubate at room temperature for 60 minutes.
  3. Dilute active rhCPA2 to 0.1 µg/mL in Assay Buffer.
  4. Combine equal volumes of 10 mM Substrate and 10 mM DTNB. Then, dilute this mixture to 200 μM Substrate, 200 μM DTNB with Assay Buffer.
  5. Load 50 µL of the 0.1 µg/mL rhCPA2 into microplate. Include a Substrate Blank with 50 µL of Assay Buffer in place of rhCPA2.
  6. Start the reaction by adding 50 µL of 200 µM Substrate into wells.
  7. Read in kinetic mode for 5 minutes at an absorbance of 405 nm.
  8. Calculate specific activity using the following formula:

     Specific Activity (pmol/min/µg) =

Adjusted Vmax* (OD/min) x well volume (L) x 1012 pmol/M
ext. coeff** (M-1cm-1) x path corr.*** (cm) x amount of enzyme (µg)

     *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:
  • rhCPA2: 0.005 µg
  • Substrate: 100 µM
  • DTNB: 100 µM

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Carboxypeptidase A2/CPA2 Protein, CF

  • carboxypeptidase A2 (pancreatic)
  • Carboxypeptidase A2
  • CPA2
  • EC 3.4.17
  • EC 3.4.17.15

Background

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.

  1. Auld, D.S. (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, et al.) p. 821, Academic Press, San Diego.

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Bioinformatics

Gene Symbol CPA2
Uniprot