Anti-eIF-4E from rabbit, purified by affinity chromatography

Eukaryotic translation initiation factor 4E (UniProt: P06730; also known as eIF-4E, eIF4E, eIF-4F 25 kDa subunit, mRNA cap-binding protein) is encoded by the EIF4E (also known as EIF4EL1, EIF4F) gene (Gene ID: 1977) in human. elF-4E is a cytoplasmic factor that recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. It is a component of the CYFIP1-EIF4E-FMR1 complex that binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex. Three isoforms of elf-4E have been described that are generated by alternative splicing. Elf-4E contains four 7-methylguanosine-containing mRNA cap binding regions and three EIF4EBP1/2/3 binding regions. Hypophosphorylated EIF4EBP1, EIF4EBP2, and EIF4EBP3 are shown to compete with EIF4G1/EIF4G3 to interact with elF-4E. Phosphorylation of ElF4EBP1 by insulin-stimulated MAP kinase (MAPK1 and MAPK3) cause dissociation of the complex and allows EIF4G1/EIF4G3 to bind and result in initiation of translation. Mutations in ElF4E gene have been linked to autism with impairments in social interaction and communication and developmental abnormalities.