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Questions? Please consult our answers to frequently asked questions at http://www.ebioscience.com/faq. DescriptionThe polyclonal antibody reacts with Caspase-3 (also known as CPP32); the antibody was, raised against a peptide mapping to the amino terminus of human caspase-3 precursor. Caspases are a family of mammalian proteases that regulate many of the morphological and biochemical features of apoptosis. The currently identified caspases can be divided into three groups: apoptotic initiators, apoptotic executioners, and inflammatory mediators (1,2). Caspase-2, 8, and 9 have been identified as apoptotic initiators (3,4). Caspase-2 (also designated Nedd-2/ICH-1) can be alternatively spliced to produce two distinct Caspase-2 mRNA species. One mRNA species encodes a protein of 435 amino acids in length and the mRNA splice variant encodes a 312 amino acid protein. The larger protein, Caspase-2L, in an over expressed state, leads to programmed cell death. Conversely the over expression of Caspase-2S protein, a truncated version of Caspase-2L, has been shown to suppress cell death induced by serum deprivation (5). The executioner caspases include caspase-3, 6 and 7. Of these three proteases Caspase-3 is considered to be the essential for the chromatin margination, DNA fragmentation, and nuclear collapse during apoptosis (6). Caspase-1 (also known as ICE) is considered to be a mediator of the inflammatory response by converting the inactive precursor of interleukin-1b to the 17 kDa proinflammatory cytokine, IL-1b (7,8). Applications ReportedFor research use only, not for diagnostic or therapeutic use. Purified anti-human caspase-3 precursor (CPP32) poly has been reported for use in immunoprecipitation, immunoblotting (WB), and immunohistochemical staining. Applications TestedPurified anti-human caspase-3 precursor (CPP32) poly has been tested by immunoblotting (WB) (1:200). References
1. Edadah BA, Faden AI. 2000. Caspase pathways, neuronal apoptosis, and CNS injury. Jounal of Neurotauma 17(10): 811-829 2. Salvesen GS, Dixit VM. 1999. Caspase activation: the induced-proximity model. Proc Natl Acad Sci USA 96(20): 10964-10967 3. Zhang W, He Q, Chan LL, Zhou F, El Naghy M, Thompson EB, Ansari NH. 2001. Involvment of caspases in 4-hydroxy-alkenal-induced apoptosis in human leukemic cells. Free Radic Biol Med 30(6): 699-706 4. Kruidering M, Evan GI. 2000. Caspase-8 in apoptosis: the beginning of ?the end? ? IUBMB 50(2): 85-90 5. Wang L, Miura M, Bergeron L, Zhu H, Yuan J. 1994. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell 78(5): 739-750 6. Slee EA, Adrain C, Martin SJ. 2001. Executioner caspase-3, -6, and ?7 perform distinct, non-redundant roles during the demolition phase of apoptosis. J Biol Chem 276(10): 7320-7326 7. Kostura MJ, Tocci MJ, Limjuco G, Chin J, Cameron P, Hillman AG, Chartrain NA, Schmidt JA. 1989. Identification of a monocyte specific pre-interleukin 1b convertase activity. Proc Natl Acad Sci USA 86(14): 5227-5231 8. Wilson KP, Black JA, Thompson JA, Kim EE, Griffith JP, Navia MA, Murcko MA, Chambers SP, Aldape RA, Raybuck SA, Livingston DJ. 1994. Structure and mechanism of interleukin-1b converting enzyme. Nature 370(6487): 251-252 Related ProductsCat. 18-8816 Rabbit TrueBlot™: Horseradish Peroxidase (HRP) anti-rabbit IgG Cat. 66-P707 Blocking Peptides for anti-human caspase-3 precursor (CPP32) polyclonal |
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