The initiation of protein synthesis in eukaryotic cells is regulated by interactions between protein initiation factors and RNA molecules. The eukaryotic initiation complex eIF4F exists in vitro as a trimeric complex of eIF4G, eIF4E, and eIF4A. Together, the complex allows ribosome binding to mRNA by inducing the unwinding of mRNA secondary structures. eIF4E binds to the mRNA ''cap during an early step in the initiation of protein synthesis. eIF4A acts as an ATP-dependent RNA helicase. eIF4G acts as a bridge between eIF4E, eIF4A, and the eIF3 complex .
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
EIF4G1 (phospho-S1148) polyclonal antibody detects endogenous levels of EIF4G1 protein around the phosphorylation site of S1148.
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