For immunochemical detection of caspase-3
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Caspase-3 Rabbit Monoclonal Antibody (Clone RM250)

Item No. 32203

Technical Information
Synonyms
  • Apoptosis-related Cysteine Protease
  • CASP-3
  • Caspase-3
  • CPP32
  • Cysteine Protease CPP32
  • PARP Cleavage Protease
  • Protein Yama
Immunogen
Synthetic peptide corresponding to human caspase-3 subunit p17
Clone Designation
RM250
100 µl of protein A-affinity purified monoclonal antibody
Storage Buffer
PBS with 50% glycerol, 1% BSA, and 0.09% sodium azide
Host
Rabbit
Isotype
IgG
Applications
IHC, WB
Cross Reactivity
(+) Caspase-3
Species Reactivity
(+) Human
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    Caspase-3 is a cysteinyl aspartic protease with roles in both extrinsic and intrinsic apoptosis.1,2 Upon apoptotic signaling via death receptors or mitochondrial assembly of pro-apoptotic factors, the zymogen procaspase-3 is cleaved into two subunits, p17 and p12, which form an active heterodimer that recognizes and cleaves proteins containing the canonical peptide sequence DEVD to drive apoptosis.3,4 Substrates for caspase-3 include the death substrate poly(ADP-ribose) polymerase (PARP), DNA-PK, actin, GAS2, and procaspase-6.5,6 The percentage of caspase-3-positive neurons is positively correlated with dopaminergic neuronal loss in the substantia nigra pars compacta of postmortem brains from patients with Parkinson’s disease, as well as several animal models of chronic neurodegenerative disorders.7 Cardiac levels of caspase-3 are increased in patients with ventricular arrhythmia, and activated caspase-3 is found in myocardium isolated from patients with end-stage heart failure.8 Cayman’s Caspase-3 Rabbit Monoclonal Antibody (Clone RM250) can be used for immunohistochemistry (IHC) and Western blot (WB) applications. The antibody recognizes the p17 subunit to detect caspase-3 in human samples.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Ghavami, S., Hashemi, M., Ande, S.R., et alApoptosis and cancer: Mutations within caspase genes. J. Med. Genet. 46(8), 497-510 (2009).

    2. Fernandes-Alnemri, T., Litwack, G., and Alnemri, E.S. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1β-converting enzyme. The Journal of Biological Chemisty 269(49), 30761-30764 (1994).

    3. Fang, B., Boross, P.I., Tozser, J., et alStructural and kinetic analysis of caspase-3 reveals role for s5 binding site in substrate recognition. J. Mol. Biol. 360(3), 654-666 (2006).

    4. Salvesen, G.S. Caspases: Opening the boxes and interpreting the arrows. Cell Death Differ. 9(1), 3-5 (2002).

    5. Tewari, M., Quan, L.T., O'Rourke, K., et alYama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81(5), 801-809 (1995).

    6. Villa, P., Kaufman, S.H., and Earnshaw, W.C. Caspases and caspase inhibitors. Trends Biochem. Sci. 22(10), 388-393 (1997).

    7. Hartmann, A., Hunot, S., Michel, P.P., et alCaspase-3: A vulnerability factor and final effector in apoptotic death of dopaminergic neurons in Parkinson’s disease. Proc. Natl. Acad. Sci. USA 97(6), 2875-2880 (2000).

    8. Yang, B., Ye, D., and Wang, Y. Caspase-3 as a therapeutic target for heart failure. Expert Opin. Ther. Targets 17(3), 255-263 (2013).