Product Pathways - Apoptosis
Bax (D2E11) Rabbit mAb #5023
|5023S||100 µl (10 western blots)||---||In Stock||---|
|5023P||40 µl (4 western blots)||---||In Stock||---|
|5023||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation, IHC-P=Immunohistochemistry (Paraffin)
Specificity / Sensitivity
Bax (D2E11) Rabbit mAb detects endogenous levels of total Bax protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu45 of human Bax protein.
Western blot analysis of extracts from various cell lines using Bax (D2E11) Rabbit mAb. Brimmel et al. demonstated that Jurkat cells lack Bax protein expression (10).
The Bcl-2 family consists of a number of evolutionarily conserved proteins containing Bcl-2 homology domains (BH) that regulate apoptosis through control of mitochondrial membrane permeability and release of cytochrome c (1-3). Four BH domains have been identified (BH1-4) that mediate protein interactions. The family can be separated into three groups based upon function and sequence homology: pro-survival members include Bcl-2, Bcl-xL, Mcl-1, A1 and Bcl-w; pro-apoptotic proteins include Bax, Bak and Bok, and "BH3 only" proteins Bad, Bik, Bid, Puma, Bim, Bmf, Noxa and Hrk. Interactions between death-promoting and death-suppressing Bcl-2 family members has led to a rheostat model in which the ratio of pro-apoptotic and anti-apoptotic proteins controls cell fate (4). Thus, pro-survival members exert their behavior by binding to and antagonizing death-promoting members. In general, the "BH3-only members" can bind to and antagonize the pro-survival proteins leading to increased apoptosis (5). While some redundancy of this system likely exists, tissue specificity, transcriptional and post-translational regulation of many of these family members can account for distinct physiological roles.
Bax is a key component for cellular induced apoptosis through mitochondrial stress (6). Upon apoptotic stimulation, Bax forms oligomers and translocates from the cytosol to the mitochondrial membrane (7). Through interactions with pore proteins on the mitochondrial membrane, Bax increases the membrane's permeability, which leads to the release of cytochrome c from mitochondria, activation of caspase-9 and initiation of the caspase activation pathway for apoptosis (8,9).
- Cory, S. et al. (2003) Oncogene 22, 8590-607.
- Antonsson, B. and Martinou, J.C. (2000) Exp Cell Res 256, 50-7.
- Sharpe, J.C. et al. (2004) Biochim Biophys Acta 1644, 107-13.
- Korsmeyer, S.J. et al. (1993) Semin Cancer Biol 4, 327-32.
- Bouillet, P. and Strasser, A. (2002) J Cell Sci 115, 1567-74.
- Wei, M.C. et al. (2001) Science 292, 727-30.
- Jürgensmeier, J.M. et al. (1998) Proc Natl Acad Sci USA 95, 4997-5002.
- Narita, M. et al. (1998) Proc Natl Acad Sci USA 95, 14681-6.
- Marzo, I. et al. (1998) Science 281, 2027-31.
- Brimmell, M. et al. (1998) Oncogene 16, 1803-12.
- Kim, K.D. et al. (2011) J Immunol 187, 3620-30. Applications: Western Blotting.
- Weisberg, E. et al. (2011) PLoS One 6, e25351. Applications: Western Blotting.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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