Effector Caspases and Substrates Antibody Sampler Kit #12690
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Product Information
Kit Usage Information
Protocols
- 4777: Western Blotting, Immunoprecipitation (Magnetic), Immunohistochemistry (Paraffin), Immunofluorescence, Immunofluorescence, Flow
- 7074: Western Blotting
- 7076: Western Blotting
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- 9665: Western Blotting, Immunoprecipitation (Magnetic)
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- 12586: Western Blotting
- 12827: Western Blotting
Product Description
The Effector Caspases and Substrates Antibody Sampler Kit provides an economical means to evaluate the activation of effector (executioner) caspases. The kit contains enough primary antibody to perform at least four western blots per primary antibody.
Background
Apoptosis is a regulated physiological process leading to cell death. Caspases, a family of cysteine acid proteases, are central regulators of apoptosis. Caspase-3 (CPP-32, Apoptain, Yama, SCA-1), Caspase-6 (Mch2), and Caspase-7 (CMH-1, Mch3, ICE-LAP3) are effector caspases functioning in cellular apoptotic processes (1-6). Upon apoptotic stimulation, initiator caspases such as caspase-9 (ICE-LAP6, Mch6) are cleaved and activated (7). The activated upstream caspases further process downstream executioner caspases by cleaving them into activated large and small subunits, thereby initiating a caspase cascade leading to apoptosis (4,6,8-10).
PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (11). This protein can be cleaved by many ICE-like caspases in vitro (1,12) and is one of the main cleavage targets of caspase-3 in vivo (10,13). In human PARP, cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (10,12). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (14).
Lamins are nuclear membrane structural components that are important in maintaining normal cell functions, such as cell cycle control, DNA replication, and chromatin organization (15-17). Lamins have been subdivided into types A and B. Type-A lamins consist of lamin A and C, which arise from alternative splicing of the lamin A gene LMNA. Lamin A and C are cleaved by caspases into large (41-50 kDa) and small (28 kDa) fragments, which can be used as markers for apoptosis (18,19). Type-B lamins consist of lamin B1 and B2, encoded by separate genes (20-22). Lamin B1 is also cleaved by caspases during apoptosis (23).
PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (11). This protein can be cleaved by many ICE-like caspases in vitro (1,12) and is one of the main cleavage targets of caspase-3 in vivo (10,13). In human PARP, cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (10,12). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (14).
Lamins are nuclear membrane structural components that are important in maintaining normal cell functions, such as cell cycle control, DNA replication, and chromatin organization (15-17). Lamins have been subdivided into types A and B. Type-A lamins consist of lamin A and C, which arise from alternative splicing of the lamin A gene LMNA. Lamin A and C are cleaved by caspases into large (41-50 kDa) and small (28 kDa) fragments, which can be used as markers for apoptosis (18,19). Type-B lamins consist of lamin B1 and B2, encoded by separate genes (20-22). Lamin B1 is also cleaved by caspases during apoptosis (23).
- Cohen, G.M. (1997) Biochem J 326 ( Pt 1), 1-16.
- Fernandes-Alnemri, T. et al. (1994) J Biol Chem 269, 30761-4.
- Faleiro, L. et al. (1997) EMBO J 16, 2271-81.
- Fernandes-Alnemri, T. et al. (1995) Cancer Res 55, 6045-52.
- Duan, H. et al. (1996) J Biol Chem 271, 1621-5.
- Lippke, J.A. et al. (1996) J Biol Chem 271, 1825-8.
- Li, P. et al. (1997) Cell 91, 479-89.
- Slee, E.A. et al. (1999) J Cell Biol 144, 281-92.
- MacFarlane, M. et al. (1997) J Cell Biol 137, 469-79.
- Nicholson, D.W. et al. (1995) Nature 376, 37-43.
- Satoh, M.S. and Lindahl, T. (1992) Nature 356, 356-8.
- Lazebnik, Y.A. et al. (1994) Nature 371, 346-7.
- Tewari, M. et al. (1995) Cell 81, 801-9.
- Oliver, F.J. et al. (1998) J Biol Chem 273, 33533-9.
- Dunbar, J.C. and Lu, H. (2000) Brain Res Bull 52, 123-6.
- Goldberg, M. et al. (1999) Crit Rev Eukaryot Gene Expr 9, 285-93.
- Yabuki, M. et al. (1999) Physiol Chem Phys Med NMR 31, 77-84.
- Rao, L. et al. (1996) J Cell Biol 135, 1441-55.
- Orth, K. et al. (1996) J Biol Chem 271, 16443-6.
- Biamonti, G. et al. (1992) Mol Cell Biol 12, 3499-506.
- Lin, F. and Worman, H.J. (1995) Genomics 27, 230-6.
- Pollard, K.M. et al. (1990) Mol Cell Biol 10, 2164-75.
- Chandler, J.M. et al. (1997) Biochem J 322 ( Pt 1), 19-23.
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