Clone: AM1 4.
Background: Caspase-3 along with caspase 7 and 6 form the group of effector caspases that are responsible for the cleavage of multiple substrates including the cytokeratins, PARP, alpha fodrin, NuMA and others. Caspase-7 occurs in three varient forms.
Caspase-3-like activities are required for Fas-mediated apoptosis. However, the role of caspase-1 and caspase-3 in mediating Fas-induced cell death is not clear. Although wild-type, caspase-1(-/-), and caspase-3(-/-) hepatocytes were killed at a similar rate when cocultured with FasL expressing NIH 3T3 cells, caspase-3(-/-) hepatocytes displayed drastically different morphological changes as well as significantly delayed DNA fragmentation. For both wild-type and caspase-1 (-/-) apoptotic hepatocytes, typical apoptotic features such as cytoplasmic blebbing and nuclear fragmentation are seen within 6 hr, but neither event was observed for caspase-3(-/-) hepatocytes. In thymocytes apoptotic caspase-3 (-/-) thymocytes exhibit similar abnormal morphological changes and delayed DNA fragmentation observed in hepatocytes. Cleavage of various caspase substrates implicates apoptotic events, including gelsolin, fodrin, laminB, and DFF45/ICAD are delayed or absent. The altered cleavage of these key substrates is likely responsible for the aberrant apoptosis observed in both hepatocytes and thymocytes deficient in caspase-3.
Immunogen: Hybridoma produced by the fusion of splenocytes from mice immunized with recombinant human Caspase-3 protein and mouse myeloma cells.
Purification Method: Protein A/G Chromatography.
Formulation: Provided as solution in phosphate buffered saline with 0.08% sodium azide.
References: 1. Slee, E.A., et al. Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner. J. Cell Biol. 1999, 144, 281-292
2. Ueda, S., et al. Redox regulation of caspase-3(-like) protease activity: regulatory roles of thioredoxin and cytochrome c. J. Immunol. 1998, 161, 6689-6695
3. Samali, A., et al. Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. EMBO J. 1999, 18, 2040-2048
4. Cohen, G.M., et al. Caspases: the executioners of apoptosis. Biochem. J. 1997, 326, 1-16.
UniProt: P42574.
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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