Apoptosis Antibody Sampler Kit (Mouse Preferred) #9930
Product Information
Kit Usage Information
Protocols
- 4927: Western Blotting
- 7074: Western Blotting
- 7076: Western Blotting
- 8592: Western Blotting, Immunoprecipitation (Agarose), Immunofluorescence, Flow
- 9504: Western Blotting
- 9509: Western Blotting, Immunofluorescence
- 9548: Western Blotting
- 9664: Western Blotting, Immunoprecipitation (Agarose), Immunohistochemistry (Paraffin), Immunofluorescence, Flow
- 14220: Western Blotting, Immunoprecipitation (Agarose)
- 58208: Western Blotting
Product Description
The Apoptosis Antibody Sampler Kit (Mouse Specific) is designed for use with mouse samples and offers an economical means to evaluate the levels of active and inactive caspases. The kit contains enough primary and secondary antibodies to perform two Western blot experiments with each antibody.
Specificity / Sensitivity
Each antibody in the Apoptosis Antibody Sampler Kit (Mouse Preferred) recognizes endogenous levels of its respective target. Caspase-3 (D3R6Y) Rabbit mAb detects full-length caspase-3 (35 kDa) as well as the large subunit (17/19 kDa) of caspase-3 resulting from cleavage during apoptosis. Cleaved Caspase-3 (Asp175) (5A1) Rabbit mAb detects the large fragment (17/19 kDa) of caspase-3 resulting from cleavage adjacent to Asp175. Caspase-8 Antibody (Mouse Specific) detects full length (57 kDa) and the cleaved intermediate (p43) of mouse caspase-8. Cleaved Caspase-8 (Asp387) (D5B2) XP® Rabbit mAb (Mouse Specific) detects the p18 subunit of mouse caspase-8 resulting from cleavage at Asp387and the cleavage product containing the pro-domain (p43). Caspase-9 Antibody (Mouse Specific) detects both full length (49 kDa) and the large fragments of mouse caspase-9 resulting from cleavage at aspartic acid 353 (37 kDa) and/or aspartic acid 368 (39 kDa). Cleaved Caspase-9 (Asp353) Antibody (Mouse Specific) detects the 37kDa subunit of mouse caspase-9 only after cleavage at aspartic acid 353. Non-specific proteins that are induced by apoptosis under certain conditions may be detected. Caspase-12 (E9T3W) Rabbit mAb detects full-length mouse caspase-12 protein (55 kDa) and the large subunit of Caspase-12 associated with activation. Cleaved PARP (Asp214) (7C9) mouse mAb detects the large fragment (89 kDa) of PARP1 resulting from caspase cleavage.
Source / Purification
Monoclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to residues surrounding Asp387 of mouse caspase-8 protein, or carboxy-terminal residues surrounding Asp214 in mouse PARP protein. Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the p20 subunit of human caspase-3 protein, or recombinant protein specific to a region within the large subunit of mouse Caspase-12 protein. Polyclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to a region within the large 18 kDa subunit of mouse caspase-8 protein, or residues adjacent to Asp353 of mouse caspase-9 protein. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
Background
Apoptosis is a regulated physiological process leading to cell death. Caspases, a family of cysteine acid proteases, are central regulators of apoptosis. Initiator caspases (including 8, 9, 10, and 12) are closely coupled to proapoptotic signals. Once activated, these caspases cleave and activate downstream effector caspases (including 3, 6, and 7), which in turn cleave cytoskeletal and nuclear proteins like PARP, α-fodrin, DFF, and lamin A and induce apoptosis. Cytochrome c released from mitochondria is coupled to the activation of caspase-9, a key initiator caspase (1). Proapoptotic stimuli include FasL, TNF-α, DNA damage and ER stress. Fas and TNFR activate caspase-8 and -10 (2), DNA damage leads to the activation of caspase-9 and ER stress leads to the calcium-mediated activation of caspase-12 (3). The inhibitor of apoptosis protein (IAP) family includes XIAP and survivin and functions by binding and inhibiting several caspases (4,5). Smac/Diablo, a mitochondrial protein, is released into the cytosol upon mitochondrial stress and competes with caspases for binding of IAPs. The interaction of Smac/Diablo with IAPs relieves the inhibitory effects of IAPs on caspases (6).
- Baker, S.J. and Reddy, E.P. (1998) Oncogene 17, 3261-3270.
- Budihardjo, I. et al. (1999) Annu. Rev. Cell Dev. Biol. 15, 269-290.
- Nakagawa, T. et al. (2000) Nature 403, 98-103.
- Deveraux, Q. L. et al. (1998) EMBO J. 17, 2215-2223.
- Li, F. et al. (1998) Nature 396, 580-584.
- Du, C. et al. (2000) Cell 102, 33-42.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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