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.

Other species have not been tested.

The antibody reacts with the 18 kDa Phospho-Bad (Ser99) protein.

This antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding S99 of human Bad.

This Anti-Phospho-Bad (Ser99) Antibody is validated for use in WB for the detection of Phospho-Bad (Ser99).

Western Blot Analysis: 1:250 dilution of this antibody detected Phospho-Bad-S99 on HL60 lysate.

18 kDa

Format: Purified

Control
Western Blot : HL60 lysates.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.