EIF1 Human
Description
The EIF1 is fused to 37 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
eIF1 is a small protein that binds to the 40S ribosomal subunit-mRNA complex. Together with eIF1A, it induces an “open” conformation of the mRNA binding channel, which is essential for scanning, tRNA delivery, and start codon recognition . The dissociation of eIF1 from the 40S subunit is considered a key step in start codon recognition .
The translation initiation process in eukaryotes is highly regulated and involves multiple steps:
- Formation of the 43S Pre-Initiation Complex (PIC): This complex includes the 40S ribosomal subunit, eIF2-GTP-initiating methionyl tRNA (Met-tRNAi) ternary complex, and several other eIFs including eIF1, eIF1A, eIF3, and eIF5 .
- mRNA Binding and Scanning: The PIC is recruited to the 5’ terminus of the mRNA and scans the 5’ untranslated region (5’UTR) to locate the start codon .
- Formation of the 80S Initiation Complex: Upon recognition of the start codon, the 60S ribosomal subunit joins the complex, forming the 80S initiation complex .
Recombinant human eIF1 is produced using recombinant DNA technology, typically in E. coli. The recombinant protein often includes a His-tag for purification purposes. For example, a recombinant human eIF1 protein with a N-terminal His-tag corresponding to amino acids 1-113 of the human protein has been characterized . This recombinant protein has a predicted molecular mass of 16.9 kDa and is used in various biochemical and structural studies .
eIF1 and other eukaryotic translation initiation factors are fundamental for the translation of mRNA and are primary targets of several signaling pathways that regulate gene expression . Mis-regulated mRNA expression is a common feature of tumorigenesis, and the abnormal activity of eIF complexes triggered by upstream signaling pathways is detected in many tumors . This makes eIFs promising therapeutic targets for various types of cancers .
