Caspase-3 precursor antibody, Blocking Peptides conjugate

Contents: caspase-3 p20 (A20) Blocking Peptide
Catalog Number: 66-P707
Formulation: Each vial contains 100 μg of peptide in 0.5 ml PBS with 0.1% NaN₃ and 100 μg BSA.
Storage Conditions: Store at 4°C.
DO NOT FREEZE.

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66-P707-81

50 ug

Available Formats of This Product
Cat. No.	Format	Excite (nm)	Emit (nm)	Reported Applications
66-P707	Blocking Peptides for anti-human caspase-3 precursor (CPP32) polyclonal	N/A	N/A	WB

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Description

This is a peptide mapping to the amino terminus of human caspase-3 precursor. Caspases is 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 Reported

For research use only, not for diagnostic or therapeutic use. This blocking peptide has been reported for use in competition studies.

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

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