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Western blot analysis of Caspase-3 on RSV-3T3 lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of Caspase-3.
Immunofluorescence staining of RSV-3T3 cells.
BD Transduction Laboratories™ Purified Mouse Anti-Caspase-3/CPP32
BD Transduction Laboratories™ Purified Mouse Anti-Caspase-3/CPP32
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- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
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- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
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Apoptosis, a selective process of genetically programmed cell death, occurs during normal cellular differentiation and development of multicellular organisms. Apoptotic cells are characterized by loss of cell volume, plasma membrane blebbing, nuclear condensation, chromatin aggregation, and endonucleocytic degradation of DNA into nucleosomal fragments. Caspase-3 (CPP32, Yama, apopain) is a member of the family of cysteine proteases which includes interleukin-1beta-converting enzyme (ICE) and C. elegans protein, Ced-3. An apoptotic signal such as granzyme B of cytotoxic T-cells (CTLs) or ICE-like proteases induces the intracellular cleavage of Caspase-3 from the inactive proform (32kDa) to the active form which consists of the p20, p17, and p12 subunits. The active form of Caspase-3 cleaves several other apoptotic proteins including proteins such as DNA fragmentation factor (DFF). Apoptosis can be inhibited by coexpression of Bcl-2 as well as inhibitors of Caspase-3 or other members of the family of cysteine proteases. This antibody recognizes the mouse 32 kDa pro-Caspase-3 and the p17 cleaved form of Caspase 3 in T cell lymphocytes treated with camptothecin.
개발 참고 자료 (5)
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Fernandes-Alnemri T, Litwack G, Alnemri ES. 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. 1994; 269(49):30761-30764. (Biology). 참조 보기
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Hatai T, Matsuzawa A, Inoshita S, et al. Execution of apoptosis signal-regulating kinase 1 (ASK1)-induced apoptosis by the mitochondria-dependent caspase activation. J Biol Chem. 2000; 275(34):26576-26581. (Clone-specific: Western blot). 참조 보기
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Jia L, Patwari Y, Srinivasula SM, et al. Bax translocation is crucial for the sensitivity of leukaemic cells to etoposide-induced apoptosis. Oncogene. 2001; 20(35):4817-4826. (Clone-specific: Western blot). 참조 보기
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Li S, Zhao Y, He X, et al. Relief of extrinsic pathway inhibition by the Bid-dependent mitochondrial release of Smac in Fas-mediated hepatocyte apoptosis. J Biol Chem. 2002; 277(30):26912-26920. (Clone-specific: Western blot). 참조 보기
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Liu X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell. 1996; 86(1):147-157. (Biology). 참조 보기
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