Technical Data
Bcl-2 (B Cell Leukemia 2)
Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74 and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway, and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin 3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced antiapoptotic functions (7).

Suitable for use in ELISA, Western Blot and Immunoprecipitation. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000
Immunoprecipitation: 1:100
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
100ul-20CBlue IceHumanRabbit
Not determined.
Synthetic peptide corresponding to residues at the carboxy terminus of Bcl-2 alpha. Species sequence homology: monkey, chicken, bovine, canine.
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, < 0.02% sodium azide, 50% glycerol.
Recognizes endogenous levels of total human Bcl-2 at 26kD. This antibody does not cross-react with other Bcl-2 family members. Species Crossreactivity: mouse, rat.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Murphy, K.M. et al. (2000) Cell Death Differ. 7, 102-111. 2. Zhu, L. et al. (1999) J. Biol. Chem. 274, 33267-33273. 3. Maundrell, K. et al. (1997) J. Biol. Chem. 272, 25238-25242. 4. Yamamoto, K. et al. (1999) Mol. Cell. Biol. 19, 8469-8478. 5. Ling, Y.H. et al. (1998) J. Biol. Chem. 273, 18984-18991. 6. Huang, S.J. and Cidlowski, J.A. (2002) FASEB 16, 825-832. 7. Deng, X. et al. (2001) J. Biol. Chem. 276, 23681-23688.