The antibody detects endogenous level of BAD only when phosphorylated at serine136.
Purification
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography usingepitope-specific phosphopeptide. The antibody against non-phosphopeptide was removedby chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Immunogen
Peptide sequence around phosphorylation site of pSer136 (S-R-S (p) -A-P) derived from Mouse BAD. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
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Background
The protein encoded by BAD gene 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 were found to be involved in the regulation of this protein. Alternative splicing of this gene results in two transcript variants which encode the same isoform.