4E-BP1(Phospho-Thr70) polyclonal antibody detects endogenous levels of 4E-BP1 protein only when phosphorylated at Thr70.
Translation repressor protein 4E-BP1 (also known as PHAS-1) inhibits cap-dependent translation by binding to the translation initiation factor eIF4E. Hyperphosphorylation of 4E-BP1 disrupts this interaction and results in activation of cap-dependent translation. Both the PI3 kinase/Akt pathway and FRAP/mTOR kinase regulate 4E-BP1 activity. Multiple 4E-BP1 residues are phosphorylated in vivo. While phosphorylation by FRAP/mTOR at Thr37 and Thr46 does not prevent the binding of 4E-BP1 to eIF4E, it is thought to prime 4E-BP1 for subsequent phosphorylation at Ser65 and Thr70.
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