The translation of proteins from eukaryotic mRNA is initiated by the multisubunit complex eIF-4F, which associates with the mRNA 5'' cap structure. eIF-4E, a component of eIF-4F, is responsible for binding to the 5'' cap structure and for the assembly of the eIF-4F complex. The regulatory protein 4E-BP1, also referred to as PHAS-I, inhibits eIF-4E function. Phosphorylation of 4E-BP1 by S6 kinase p70, MAP kinases or PKCs causes the disassociation of 4E-BP1 from eIF-4E, promoting translation. A protein that is functionally related to 4E-BP1, designated 4E-BP2, also associates with eIF-4E.

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; 4EBP1; PHAS I; PHASI;

q13541

Human,Mouse,Rat

WB,IHC,IP

WB 1:500-1:1000
IHC 1:50-1:200
IP 1:50-1:200

~ 15 to 20 kDa

Rabbit

This antibody detects endogenous levels of 4E-BP1 protein only when phosphorylated at Thr46.

Synthetic phosphopeptide derived from human 4E-BP1 around the phosphorylation site of Threonine 46.

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.