EIF1 Protein, Human (GST)

The EIF1 protein is a key member of the 43S preinitiation complex (43S PIC), binding to the mRNA cap-proximal region, scanning the 5′-untranslated region, and localizing the initiation codon. EIF1 Protein, Human (GST) is the recombinant human-derived EIF1 protein, expressed by E. coli , with N-GST labeled tag.

EIF1 is a vital component of the 43S pre-initiation complex (43S PIC) and plays a crucial role in the intricate process of translation initiation. As part of the 43S PIC, EIF1 binds to the mRNA cap-proximal region, engages in mRNA scanning, and precisely locates the initiation codon. Teaming up with eIF1A (EIF1AX), EIF1 is indispensable for the recognition of the start codon, dependent on the AUG nucleotide context and its position relative to the 5'-cap. EIF1 actively contributes to initiation codon selection by influencing the conformation of the 40S ribosomal subunit and the positioning of the bound mRNA and initiator tRNA. It regulates the opening and closing of the mRNA binding channel, ensuring mRNA recruitment, scanning, and the accuracy of initiation codon selection. Continuously surveilling and guarding against premature and partial base-pairing of codons in the 5'-UTR with the anticodon of the initiator tRNA, EIF1, together with eIF1A (EIF1AX), orchestrates ribosomal scanning, promotes the assembly of the 48S complex at the initiation codon, and facilitates the dissociation of aberrant complexes. Interaction with EIF4G1 supports ribosome scanning, leaky scanning, and discrimination against cap-proximal AUG. Maintaining an open conformation within the 43S PIC through interaction with EIF1A-EIF5, EIF1 undergoes a conformational shift upon reaching the correct start codon, moving the PIC into a closed conformation and halting it at the start codon. This multifaceted role highlights EIF1's essential contributions to the precision and fidelity of translation initiation.

Human

E. coli

N-GST

P41567 (M1-F113)

10209  [NCBI]

Full Length

MSAIQNLHSFDPFADASKGDDLLPAGTEDYIHIRIQQRNGRKTLTTVQGIADDYDKKKLVKAFKKKFACNGTVIEHPEYGEVIQLQGDQRKNICQFLVEIGLAKDDQLKVHGF

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.