The initiation of protein synthesis in eukaryotic cells is regulated by interactions between protein initiation factors and RNA molecules. The eukaryotic initiation complex eIF2 exists as a heterotrimeric complex of eIF2alpha, eIF2ß and eIF2gamma. eIF2 functions in the early stages of protein synthesis, by forming a ternary complex with GTP and tRNA. This complex binds to the 40S ribosomal subunit, followed by mRNA binding to 40S to form the 43S preinitiation complex, the release of eIF2 from 40S, and the hydrolysis of GTP. Phosphorylation of eIF2a correlates with inhibition of translation initiation .
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:
p-EIF2S2 (S67) polyclonal antibody detects endogenous levels of EIF2S2 protein only when phosphorylated at Ser67.
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