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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-Bad (Ser112) (40A9) Rabbit mAb 5284 40 µl
Western Blotting Immunohistochemistry Flow Cytometry
H M R Mk 23 Rabbit IgG
Phospho-Bad (Ser136) (D25H8) Rabbit mAb 4366 40 µl
Western Blotting Immunoprecipitation
H M Mk 23 Rabbit IgG
Phospho-Bad (Ser155) Antibody 9297 40 µl
Western Blotting
M 23 Rabbit 
Bad (D24A9) Rabbit mAb 9239 40 µl
Western Blotting
H M R Mk 23 Rabbit IgG
pCMV-Tag4A-mBad/GrpE 20 µg  
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
All Goat 

Product Description

The Phospho-Bad Antibody Sampler Kit provides an economical means to investigate the role of Bad protein in apoptosis. The kit contains primary and secondary antibodies to perform four Western blots with each antibody.


Specificity / Sensitivity

Bad (D24A9) Rabbit mAb detects endogenous levels of total Bad protein. Phospho-Bad (Ser112) (40A9) Rabbit mAb detects endogenous levels of Bad only when phosphorylated at Ser112 (equivalent to Ser75 in human and Ser113 in rat). Phospho-Bad (Ser136) (D25H8) Rabbit mAb detects endogenous levels of Bad only when phosphorylated at Ser136 (equivalent to Ser99 in human and Ser137 in rat). Phospho-Bad (Ser155) Antibody detects transfected levels of Bad only when phosphorylated at Ser155 (equivalent to Ser118 in human and Ser156 in rat).


Source / Purification

Bad (D24A9) Rabbit mAb (#9239) was prepared by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro102 of human Bad protein. Phospho-specific antibodies (#4366, #5284, #9297) were prepared by respectively immunizing animals with synthetic phosphopeptides corresponding to residues surrounding Ser112, Ser136, Ser155 of mouse Bad protein. Polyclonal Phospho-Bad (Ser155) Antibody (#9297) was purified by protein A and peptide affinity chromatography. The construct pCMV-Tag4A-mBad/GrpE expresses a fusion protein of mouse Bad with the E. coli heat shock protein GrpE. The fusion protein runs as a 48 to 52 kDa doublet formed by alternative start sites.

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.


Entrez-Gene Id 572, 12015
Swiss-Prot Acc. Q92934, Q61337

Protein Specific References

Moon EY and Lerner A (2003) Blood 101, 4122–30

Rice PL et al. (2003) Cancer Res 63, 616–20

Zhang B et al. (2004) Mol Cell Biol 24, 6205–14

Hui L et al. (2005) J Biol Chem 280, 35829–35

Xu RH et al. (2005) Cancer Res 65, 613–21

Li YY et al. (2006) Cancer Res 66, 6741–7

Polzien L et al. (2009) J Biol Chem 284, 28004–20

Chen J et al. (2009) Oncogene 28, 2581–92

Ye DZ et al. (2011) PLoS One 6, e27637

Kumar JK et al. (2011) Int J Biochem Cell Biol 43, 594–603

Polzien L et al. (2011) J Biol Chem 286, 17934–44

Marchion DC et al. (2011) Clin Cancer Res 17, 6356–66

Xu D et al. (2011) Carcinogenesis 32, 488–95

Moon EY and Lerner A (2003) Blood 101, 4122–30

Rice PL et al. (2003) Cancer Res 63, 616–20

Zhang B et al. (2004) Mol Cell Biol 24, 6205–14

Hui L et al. (2005) J Biol Chem 280, 35829–35

Xu RH et al. (2005) Cancer Res 65, 613–21

Li YY et al. (2006) Cancer Res 66, 6741–7

Polzien L et al. (2009) J Biol Chem 284, 28004–20

Chen J et al. (2009) Oncogene 28, 2581–92

Ye DZ et al. (2011) PLoS One 6, e27637

Kumar JK et al. (2011) Int J Biochem Cell Biol 43, 594–603

Polzien L et al. (2011) J Biol Chem 286, 17934–44

Marchion DC et al. (2011) Clin Cancer Res 17, 6356–66

Xu D et al. (2011) Carcinogenesis 32, 488–95

Moon EY and Lerner A (2003) Blood 101, 4122–30

Rice PL et al. (2003) Cancer Res 63, 616–20

Zhang B et al. (2004) Mol Cell Biol 24, 6205–14

Hui L et al. (2005) J Biol Chem 280, 35829–35

Xu RH et al. (2005) Cancer Res 65, 613–21

Li YY et al. (2006) Cancer Res 66, 6741–7

Polzien L et al. (2009) J Biol Chem 284, 28004–20

Chen J et al. (2009) Oncogene 28, 2581–92

Ye DZ et al. (2011) PLoS One 6, e27637

Kumar JK et al. (2011) Int J Biochem Cell Biol 43, 594–603

Polzien L et al. (2011) J Biol Chem 286, 17934–44

Marchion DC et al. (2011) Clin Cancer Res 17, 6356–66

Xu D et al. (2011) Carcinogenesis 32, 488–95


For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
U.S. Patent No. 5,675,063.