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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 eIF4E, eIF4A and eIF4G. 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.
Optimal dilution of the Eukaryotic translation initiation factor 4E antibody should be determined by the researcher.
Recombinant full-length human EIF4E/Eukaryotic translation initiation factor 4E protein was used as the immunogen for the Eukaryotic translation initiation factor 4E antibody.
Aliquot the Eukaryotic translation initiation factor 4E antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
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