eIF5 / Unconjugated / H6-D11
Product Details
Description | 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. | |
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Conjugate | Unconjugated | |
Clone | H6-D11 | |
Target Species | Human | |
Applications | FC, ICC, WB, IHC | |
Supplier | HuaBio | |
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About eIF5
Eukaryotic translation initiation factor-5 (EIF5) interacts with the 40S initiation complex to promote hydrolysis of bound GTP with concomitant joining of the 60S ribosomal subunit to the 40S initiation complex. The resulting functional 80S ribosomal initiation complex is then active in peptidyl transfer and chain elongations (summary by Si et al., 1996 [PubMed 8663286]).[supplied by OMIM, May 2010]
Eukaryotic translation initiation factor-5 (EIF5) interacts with the 40S initiation complex to promote hydrolysis of bound GTP with concomitant joining of the 60S ribosomal subunit to the 40S initiation complex. The resulting functional 80S ribosomal initiation complex is then active in peptidyl transfer and chain elongations (summary by Si et al., 1996 [PubMed 8663286]).[supplied by OMIM, May 2010]
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