• Product nameAnti-Bad antibody
    See all Bad primary antibodies
  • Description
    Rabbit polyclonal to Bad
  • SpecificityAntibody detects endogenous levels of Bad protein around Serine 155.
  • Tested applicationsSuitable for: WB, IHC-P, ELISAmore details
  • Species reactivity
    Reacts with: Human
    Predicted to work with: Mouse, Rat
  • Immunogen

    Synthetic non-phosphopeptide derived from Human Bad around the phosphorylation site of Serine 155.

  • Positive control
    • Breast carcinoma tissue and extracts of 293 cells treated with forskolin.



Our Abpromise guarantee covers the use of ab31310 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB 1/500 - 1/1000. Predicted molecular weight: 18 kDa.
IHC-P Use at an assay dependent concentration.
ELISA 1/10000.


  • FunctionPromotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.
  • Tissue specificityExpressed in a wide variety of tissues.
  • Sequence similaritiesBelongs to the Bcl-2 family.
  • DomainIntact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family.
  • Post-translational
    Phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-118, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation. Ser-75 is phosphorylated by AKT/PKB, protein kinase A and PIM2.
  • Cellular localizationMitochondrion outer membrane. Cytoplasm. Upon phosphorylation, locates to the cytoplasm.
  • Information by UniProt
  • Database links
  • Alternative names
    • BAD antibody
    • BAD_HUMAN antibody
    • BBC 2 antibody
    • BBC2 antibody
    • BBC6 antibody
    • Bcl 2 Antagonist of Cell Death antibody
    • Bcl 2 Binding Component 6 antibody
    • BCL X / BCL 2 Binding Protein antibody
    • BCL X Binding Protein antibody
    • Bcl XL/Bcl 2 Associated Death Promoter antibody
    • Bcl-2-binding component 6 antibody
    • Bcl-2-like protein 8 antibody
    • Bcl-XL/Bcl-2-associated death promoter antibody
    • Bcl2 antagonist of cell death antibody
    • BCL2 antagonist of cell death protein antibody
    • BCL2 associated agonist of cell death antibody
    • Bcl2 Associated Death Promoter antibody
    • BCL2 binding component 6 antibody
    • BCL2 binding protein antibody
    • Bcl2 Like 8 Protein antibody
    • Bcl2-L-8 antibody
    • BCL2L8 antibody
    • Proapoptotic BH3 Only Protein antibody
    see all

Anti-Bad antibody images

  • ab31310 at a 1:50-1:100 dilution staining Bad in human breast carcinoma tissue, using Immunohistochemistry Paraffin Embedded Tissue.

    Left image : Un-treated.

    Right image : Antibody pre-incubated with synthesized peptide.

  • All lanes : Anti-Bad antibody (ab31310) at 1/500 dilution

    Lane 1 : Extracts of 293 cells treated with forskolin.
    Lane 2 : Extracts of 293 cells treated with forskolin. Antibody pre-incubated with synthesized peptide.

    Predicted band size : 18 kDa

References for Anti-Bad antibody (ab31310)

ab31310 has not yet been referenced specifically in any publications.

Product Wall

Thank you for your enquiry. The following paper has Western blot images of Bad running heavier than 18kD: Jiping Zha,1 Hisashi Harada,1 Elizabeth Yang,1 Jennifer Jockel,1 and Stanley J Korsmeyer1; Serine Phosphorylation of Death Agonist BAD in R...

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