Cell Signaling Technology

Product Pathways - Apoptosis

Phospho-Bad (Ser112) (7E11) Mouse mAb (Biotinylated) #5193

Applications Reactivity Sensitivity MW (kDa) Isotype
W H M R Mk Endogenous 23 Mouse IgG1

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

Protocols

Specificity / Sensitivity

Phospho-Bad (Ser112) (7E11) Mouse mAb (Biotinylated) recognizes endogenous levels of Bad only when phosphorylated at Ser112. The Ser112 nomenclature is based upon the mouse sequence. The analogous phosphorylation site is Ser75 in human and Ser113 in rat. This antibody does not detect Bad phosphorylated at other sites, nor does it detect related family members.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser112 of mouse Bad protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from OVCAR8 cells, untreated (-) or λ phosphatase-treated (+), using Phospho-Bad (Ser112) (7E11) Mouse mAb (Biotinylated).

Description

This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-Bad (Ser112) (7E11) Mouse mAb #9296.

Background

Bad is a proapoptotic member of the Bcl-2 family that promotes cell death by displacing Bax from binding to Bcl-2 and Bcl-xL (1,2). Survival factors, such as IL-3, inhibit the apoptotic activity of Bad by activating intracellular signaling pathways that result in the phosphorylation of Bad at Ser112 and Ser136 (2). Phosphorylation at these sites promotes binding of Bad to 14-3-3 proteins to prevent an association between Bad with Bcl-2 and Bcl-xL (2). Akt phosphorylates Bad at Ser136 to promote cell survival (3,4). Bad is phosphorylated at Ser112 both in vivo and in vitro by p90RSK (5,6) and mitochondria-anchored PKA (7). Phosphorylation at Ser155 in the BH3 domain by PKA plays a critical role in blocking the dimerization of Bad and Bcl-xL (8-10).

  1. Yang, E. et al. (1995) Cell 80, 285-291.
  2. Zha, J. et al. (1996) Cell 87, 619-628.
  3. Datta, S.R. et al. (1997) Cell 91, 231-241.
  4. Peso, L. et al. (1997) Science 278, 687-689.
  5. Bonni, A. et al. (1999) Science 286, 1358-1362.
  6. Tan, Y. et al. (1999) J. Biol. Chem. 274, 34859-34867.
  7. Harada, H. et al. (1999) Mol. Cell 3, 413-422.
  8. Tan, Y. et al. (2000) J. Biol. Chem. 275, 25865-25869.
  9. Lizcano, J. et al. (2000) Biochem. J. 349, 547-557.
  10. Datta, S. et al. (2000) Mol. Cell 6, 41-51.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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