EIF5 polyclonal antibody

In mammalian cells, translation is controlled at the level of polypeptide chain initiation by initiation factors. The eukaryotic translation initiation factor 5 (eIF5) catalyzes the hydrolysis of GTP bound to the 40S ribosomal subunit, a function necessary for the subsequent joining of the 40S and 60S subunits to form the 80S initiation complex. eIF-4E specifically binds to the mRNA cap to promote unwinding and exposure of the AUG-initiation codon. Overexpression of eIF-4E can lead to cell transformation and tumorigenesis. An additional initiation factor, eIF-2, is present as a heterotrimer composed of eIF-2a, eIF-2b and eIF-2g subunits. This heterotrimer forms a complex with GTP and tRNA which then binds to the 40S ribosomal subunit. After the formation of the 80S initiation complex, eIF-2 is hydrolyzed and eIF-2-GDP is released from the complex. eIF-2-GDP is subsequently converted to eIF-2-GTP, a reaction catalyzed by eIF-2B, and is then available to catalyze another round of initiation.