|Application ||WB, IHC, FC, IF|
|Calculated MW||31608 Da|
|Other Names||Caspase-3, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 1, SCA-1, Caspase-3 subunit p17, Caspase-3 subunit p12, CASP3, CPP32|
|Target/Specificity||A synthetic peptide correscponding to N-terminal residues of Human Pro-Caspase-3 was used as immunogen. The antibody only recognizes the pro-form of Caspase-3. It does not react with the cleaved forms (active enzyme) of Caspase-3.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Caspase-3 Antibody (Pro) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.|
|Tissue Location||Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system|
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Provided below are standard protocols that you may find useful for product applications.
Caspases are a family of cytosolic aspartate-specific cysteine proteases involved in the initiation and execution of apoptosis. Caspase-3 (apopain, SCA-1, Yama and CPP32) is a member of the apoptosis execution functional group of caspases, and is either partially or totally responsible for the proteolytic cleavage of many key proteins during apoptosis, such as poly (ADP-ribose) polymerase (PARP) (1,2,3). Caspase-3 is a cytosolic protein found in cells as an inactive 32 kDa proenzyme. It is activated by proteolytic cleavage into two active subunits only when cells undergo apoptosis (3).
1. Fernandes-Alnemri, T. et al. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme. J. Biol. Chem. 269:30761
2. Tewari, M. et al. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 801
3. Nicholson, D.W. et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 376: 37
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