Cell Signaling Technology

Product Pathways - Apoptosis / Autophagy

Phospho-Bcl-2 (Thr56) Antibody (Human Specific) #2875

Applications Reactivity MW (kDa) Source
W H 28 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-Bcl-2 (Thr56) Antibody (Human Specific) detects endogenous levels of Bcl-2 only when phosphorylated at threonine 56. It does not cross-react with non-phosphorylated Bcl-2 or with other Bcl-2 family members at endogenous levels.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic phospho-peptide (KLH-coupled) corresponding to residues surrounding Thr56 of human Bcl-2. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of Jurkat cells, untreated or treated with pacilitaxel for the indicated times, using Phospho-Bcl-2 (Thr56) Antibody (Human Specific) (top) or Bcl-2 Antibody (Human Specific) #2872 (bottom).

Background

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).

  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 J. 16, 825-832.
  7. Deng, X. et al. (2001) J. Biol. Chem. 276, 23681-23688.

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