The antibody detects endogenous level of 4E-BP1 only when phosphorylated at Threonine 45.
Purification
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Immunogen
Peptide sequence around phosphorylation site of pThr45 (S-T-T (p) -P-G) derived from Human 4E-BP1. Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates.
4E-BP1 encodes one member of a family of translation repressor proteins. The protein directly interacts with eukaryotic translation initiation factor 4E (eIF4E), which is a limiting component of the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs. Interaction of this protein with eIF4E inhibits complex assembly and represses translation. This protein is phosphorylated in response to various signals including UV irradiation and insulin signaling, resulting in its dissociation from eIF4E and activation of mRNA translation. Published Papers Jiumei Cao