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.

Eukaryotic translation initiation factor 4E-binding protein 1; 4E-BP1; eIF4E-binding protein 1; Phosphorylated heat- and acid-stable protein regulated by insulin 1; PHAS-I; EIF4EBP1

q13541

Human

WB

WB 1:1000-1:2000

~ 18 kDa

Rabbit

This antibody detects endogenous levels of 4E-BP1 protein only when phosphorylated at Thr70.

Synthetic phosphopeptide derived from human 4E-BP1 around the phosphorylation site of Threonine 70.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.