Product Pathways - Apoptosis / Autophagy
Caspase-7 Antibody #9492
| Applications | Reactivity | MW (kDa) | Source |
|---|---|---|---|
| W F | H M R | 20, 35 | Rabbit |
Applications Key:
W=Western Blotting
F=Flow Cytometry
Reactivity Key:
H=Human
M=Mouse
R=Rat
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
Caspase-7 Antibody detects endogenous levels of both full length caspase-7 (35 kDa) and the large fragment of cleaved caspase-7 following cleavage at aspartic acid 198 (20 kDa). The antibody does not recognize other caspases.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH coupled) corresponding to residues surrounding the cleavage site of human caspase-7. Antibodies are purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of extracts from Jurkat cells, untreated or etoposide-treated (25 µM), and Hela cells, untreated or staurosporine-treated (1 µM), using Caspase-7 Antibody.
Flow Cytometry
Flow cytometric analysis of Jurkat cells, untreated (blue) or etoposide-treated (green), using Caspase-7 Antibody compared to a nonspecific negative control antibody (red).
Background
Caspase-7 (CMH-1, Mch3, ICE-LAP3) has been identified as a major contributor to the execution of apoptosis (2-4). Caspase-7 is an effector caspase (along with caspase-2 and -3), meaning that it cleaves essential cellular machinery rather than activating other caspases (5-8). Caspase-7 is cleaved by many enzymes, including caspases-3, -6, -8, -9 and granzyme B (1,4,5). Once activated, caspase-7 cleaves many of the same substrates as caspase-3, including poly (ADP-ribose) polymerase, or PARP (2,4).
- Fernandes-Alnemri, T. et al. (1995) Cancer Res. 55, 6045-6052.
- Duan, H. et al. (1996) J. Biol. Chem. 271, 1621-1625.
- Lippke, J. A. et al. (1996) J. Biol. Chem. 271, 1825-1828.
- Cohen, G.M. (1997) Biochem. J. 326, 1-16.
- Thornberry, N. A. et al. (1997) J. Biol. Chem. 272, 17907-17911.
- Chandler, J. M. et al. (1998) J. Biol. Chem. 273, 10815-10818.
- MacFarlane, M. et al. (1997) J. Cell Biol. 137, 469-479.
- Nu?ez, G. et al. (1998) Oncogene 17, 3237-3245.
Application References
- Erhardt, J. A. et al. (2001) Activation of caspase-3/caspase-3-like activity in rat cardiomyocytes by an RGD peptide, but not the GPIIb/IIIa antagonist lotrafiban. Thromb. Res 103, 143-148. This article references the use of Caspase-7 Antibody in the following applications: Western Blotting
- Lademann, U. et al. (2003) Diarylurea compounds inhibit caspase activation by preventing the formation of the active 700-kilodalton apoptosome complex. Mol. Cell. Biol. 23, 7829-7837. This article references the use of Caspase-7 Antibody in the following applications: Western Blotting
- Guegan, C. et al. (2001) Recruitment of the mitochondrial-dependent apoptotic pathway in amyotrophic lateral sclerosis. J. Neurosci. 21, 6569-6576. This article references the use of Caspase-7 Antibody in the following applications: Western Blotting
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