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Bad is a member of the BCL-2 family. BCL-2 family members are known to be regulators of programmed cell death. This protein positively regulates cell apoptosis by forming heterodimers with BCL-xL and BCL-2, and reversing their death repressor activity. Proapoptotic activity of this protein is regulated through its phosphorylation. Protein kinases AKT and MAP kinase, as well as protein phosphatase calcineurin are found to be involved in the regulation of this protein. Bad is 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.

Target	Bad (pS134)
Reactivity	Human
Host	Rabbit
Clonality	Polyclonal
Tested Applications	IHC
Recommended dilutions	Optimal dilutions/concentrations should be determined by the end user.
Immunogen	Human Bad (phospho-Ser134).
Purification	Peptide Affinity Purified Rabbit Polyclonal Antibody.
Isotype	IgG
Conjugation	Unconjugated
Specificity	This Bad Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding S134 of human Bad.
Storage	Aliquot and store at -20 °C. Avoid repeated freeze/thaw cycles.
Swiss Prot	Q92934
Buffer	PBS with 0.09% (W/V) sodium azide. This antibody is first purified by protein G affinity chromatography. Then, the antibody fraction is peptide affinity purified in a 2-step procedure with control and phosphorylated peptides. The phospho-specific antibody is eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
Availability	Shipped within 5-10 working days.
Note	This product is for research use only.