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Recombinant Human Pro-Caspase-3 Protein, CF

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Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant Human Pro-Caspase-3 Protein, CF Summary

Details of Functionality
The activity of the activated Caspase-3 was measured by its ability to cleave DEVD-AFC. The specific activity is >500 pmol/min/μg, as measured under the described conditions.
Source
E. coli-derived human Caspase-3 protein
Met1-His277, with an N-terminal Met and 6-His tag
Accession #
N-terminal Sequence
Not tested: Met predicted.
Structure / Form
Pro form
Protein/Peptide Type
Recombinant Enzymes
Gene
CASP3
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain

Applications/Dilutions

Dilutions
  • Enzyme Activity
Theoretical MW
33 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
35 kDa, reducing conditions
Publications
Read Publications using
731-C3 in the following applications:

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, NaCl, Sucrose and DTT.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 50 µg/mL in 20 mM Tris, 300 mM NaCl, 5 mM Dithiothreitol, 5% Sucrose and 0.05% CHAPS, pH 8.0.
Assay Procedure
  • Assay Buffer: 20 mM Tris, 0.3 M NaCl, 0.05% (w/v) CHAPS, 5 mM DTT, 5% (w/v) Sucrose, pH 8.0
  • Recombinant Human Pro-Caspase-3 (rhPro-Caspase-3) (Catalog # 731-C3)
  • Recombinant Human Caspase‑8 (rhCaspase-8) (Catalog # 705-C8)
  • Substrate: Ac-Asp-Glu-Val-Asp-AFC (MP Biomedicals, Catalog # AFC138), 10 mM stock in DMSO
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Activate rhPro-Caspase-3 at 10 μg/mL with 10 µg/mL rhCaspase-8 at a final concentration, respectively in Assay Buffer.
  2. Incubate reaction at 37 °C for 90 minutes.
  3. Dilute Substrate to 100 µM in Assay Buffer.
  4. Dilute Activated rhPro-Caspase-3 to 0.4 µg/mL.
  5. In a plate load 50 µL of 0.4 µg/mL rhPro-Caspase-3 and include a Substrate Blank containing 50 µL Assay Buffer.
  6. Start the reaction by adding 50 µL of 100 µM Substrate to wells.
  7. Read at excitation and emission wavelengths of 400 nm and 505 nm (top read), respectively in kinetic mode for 5 minutes.
  8. Calculate specific activity:

     Specific Activity (pmol/min/µg) =

 Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)

     *Adjusted for Substrate Blank
     **Derived using calibration standard 7-amino, 4-(trifluoromethyl), Coumarin (Biomedicals, Catalog # 164580).

Per Well:
  • rhPro-Caspase-3: 0.02 µg
  • Substrate: 50 µM

Notes

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

Alternate Names for Recombinant Human Pro-Caspase-3 Protein, CF

  • Apopain
  • apoptosis-related cysteine protease
  • CASP3
  • CASP-3
  • caspase 3, apoptosis-related cysteine peptidase
  • Caspase3
  • Caspase-3
  • CPP32
  • CPP-32
  • CPP32B
  • CPP32SREBP cleavage activity 1
  • Cysteine protease CPP32
  • EC 3.4.22
  • EC 3.4.22.56
  • LICE-1
  • PARP cleavage protease
  • procaspase3
  • Protein Yama
  • SCA-1
  • YAMA

Background

Caspase-3 (Cysteine-aspartic acid protease 3/Casp3; also Yama, apopain and CPP32) is a 29 kDa member of the peptidase C14A family of enzymes (1, 2, 3). It is widely expressed and is an integral component of the apoptotic cascade. Caspase-3 is considered to be the major executioner caspase; that is, the primary downstream mediator of apoptotic-associated proteolysis (2, 3, 4). Active Caspase-3 is known to utilize a Cys residue to cleave multiple substrates, including PARP, proIL-16, PKC-gamma & -δ, procaspases 6, 7 and 9, and beta -catenin (1). Human procaspase-3 is a 32 kDa, 277 amino acid (aa) protein (5, 6, 7). Normally, it is an inactive, cytosolic homodimer, but following an upstream signal that activates processing proteases, procaspase-3 undergoes proteolytic cleavage (1, 2, 8, 9). This generates an N-terminal 175 aa p20/20 kDa subunit plus a 102 aa C-terminal p12/12 kDa subunit, followed by further processing of the p20 subunit at Asp28 to generate a final p17 subunit (aa 29-175) (9). The p17 and p12 subunits noncovalently heterodimerize, and subsequently associate with another p17/p12 heterodimer to form an active antiparallel homodimer. The p17 subunit contains the enzyme active site (aa 161 - 165), with an embedded catalytic Cys which is normally nitrosylated and inactive. Full activation requires both proteolytic processing and Cys163 denitrosylation (10). Multiple proteases can use Caspase-3 as a substrate including Caspase-6, -8, and -10, granzyme B, and Caspase-3 itself (9, 11, 12, 13). 
  1. Chowdhury, I. et al. (2008) Comp. Biochem. Physiol. B 151:10.
  2. Boatright, K.M. & G.S. Salvesen (2003) Curr. Opin. Cell Biol. 15:725.
  3. Launay, S. et al. (2005) Oncogene 24:5137.
  4. Walsh, J.G. et al. (2008) Proc. Natl. Scad. Sci. USA 105:12815.
  5. Nicholson, D.W. et al. (1995) Nature 376:37.
  6. Tewari, M. et al. (1995) Cell 81:801.
  7. Fernandes-Alnemri, T. et al. (1994) J. Biol. Chem. 269:30761.
  8. Milisav, I. et al. (2009) Apoptosis 14:1070.
  9. Han, Z. et al. (1997) J. Biol. Chem. 272:13432.
  10. Rossig, L. et al. (1999) J. Biol. Chem. 274:6823.
  11. Rank, K.B. et al. (2001) Protein Expr. Purif. 22:258.
  12. Atkinson, E.A. et al. (1998) J. Biol. Chem. 273:21261.
  13. Cohen, G.M. (1997) Biochem. J. 326:1.

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Recombinant Human
Pro-Caspase-3 Protein ...
731-C3
Recombinant Human Pro-Caspase-3 Protein, CF
Species: Hu
Applications: Enzyme Activity

Publications for Caspase-3 (731-C3)(2)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Bioassay.


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Bioinformatics

Gene Symbol CASP3
Uniprot