Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|Description||Anti-Caspase 3 Antibody, clone 4-1-18|
|Presentation||0.1M Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide before the addition of glycerol to 30%|
|Application||Anti-Caspase 3 Antibody, clone 4-1-18 is an antibody against Caspase 3 for use in WB.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||2 years at -20°C|
|Material Size||100 µg|
|Anti-Caspase 3, clone 4-1-18 (mouse monoclonal IgG2a) - 2343558||2343558|
|Anti-Caspase 3, clone 4-1-18 - 22206||22206|
|Anti-Caspase 3, clone 4-1-18 - 2531918||2531918|
|Reference overview||Pub Med ID|
|Caspases disrupt the nuclear-cytoplasmic barrier.|
Faleiro, L and Lazebnik, Y
J. Cell Biol., 151: 951-9 (2000) 2000
During apoptosis, caspases, a family of proteases, disassemble a cell by cleaving a set of proteins. Caspase-3 plays a major role in the dissassembly of the nucleus by processing several nuclear substrates. The question is how caspase-3 which is usually cytoplasmic, gains access to its nuclear targets. It was suggested that caspase-3 is actively transported to the nucleus through the nuclear pores. We found that caspase-9, which is activated earlier than caspase-3, directly or indirectly inactivates nuclear transport and increases the diffusion limit of the nuclear pores. This increase allows caspase-3 and other molecules that could not pass through the nuclear pores in living cells to enter or leave the nucleus during apoptosis by diffusion. Hence, caspase-9 contributes to cell disassembly by disrupting the nuclear cytoplasmic barrier.
|Oncogene-dependent apoptosis is mediated by caspase-9.|
Fearnhead, H O, et al.
Proc. Natl. Acad. Sci. U.S.A., 95: 13664-9 (1998) 1998
Understanding how oncogenic transformation sensitizes cells to apoptosis may provide a strategy to kill tumor cells selectively. We previously developed a cell-free system that recapitulates oncogene dependent apoptosis as reflected by activation of caspases, the core of the apoptotic machinery. Here, we show that this activation requires a previously identified apoptosis-promoting complex consisting of caspase-9, APAF-1, and cytochrome c. As predicted by the in vitro system, preventing caspase-9 activation blocked drug-induced apoptosis in cells sensitized by E1A, an adenoviral oncogene. Oncogenes, such as E1A, appear to facilitate caspase-9 activation by several mechanisms, including the control of cytochrome c release from the mitochondria.