eIF3-beta, eIF3-p36, EIF3S2, PRO2242, TRIP-1, TRIP1, Eukaryotic translation initiation
factor 3 subunit I, eIF3i, TGF-beta receptor-interacting protein 1, eIF-3-beta.
Greater than 90.0% as determined by SDS-PAGE.
EIF3I Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 331 amino acids (1-325 a.a) and having a molecular mass of 37.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).
EIF3I is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
eIF3-beta, eIF3-p36, EIF3S2, PRO2242, TRIP-1, TRIP1, Eukaryotic translation initiation
factor 3 subunit I, eIF3i, TGF-beta receptor-interacting protein 1, eIF-3-beta.
MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA
DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC
FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT SAVWGPLGEC IIAGHESGEL NQYSAKSGEV
LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN
YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY SSGGEDGYVR IHYFDPQYFE FEFEAHHHHH H.
Eukaryotic Translation Initiation Factor 3I (eIF3I) is a subunit of the eukaryotic translation initiation factor 3 (eIF3) complex, which plays a crucial role in the initiation of protein synthesis in eukaryotic cells. The eIF3 complex is essential for various steps in the translation initiation process, including the recruitment of the 40S ribosomal subunit, mRNA, and other initiation factors to form the pre-initiation complex (PIC).
The eIF3 complex is the largest of the eukaryotic initiation factors and consists of multiple subunits, including eIF3I. The eIF3I subunit, also known as eIF3-beta or TRIP1, is involved in the assembly and stability of the eIF3 complex. It interacts with other subunits and components of the translation machinery to facilitate the accurate selection of the start codon and the formation of the 43S pre-initiation complex (43S PIC) .
The eIF3 complex, including eIF3I, binds to the 40S ribosomal subunit and promotes the recruitment of eIF1, eIF1A, eIF2-GTP-methionyl-tRNAi, and eIF5 to form the 43S PIC. This complex then scans the mRNA for the start codon (AUG) and ensures the correct positioning of the initiator tRNA in the ribosomal P site .
The recombinant production of eIF3I in Sf9 cells involves the use of baculovirus expression systems. Sf9 cells, derived from the fall armyworm (Spodoptera frugiperda), are commonly used for the production of recombinant proteins due to their high expression levels and ability to perform post-translational modifications.
The recombinant eIF3I produced in Sf9 cells is a single, glycosylated polypeptide chain containing 331 amino acids and has a molecular mass of approximately 37.3 kDa. It is fused to a 6-amino acid His-tag at the C-terminus, which facilitates its purification using chromatographic techniques .
The study of eIF3I and its role in the eIF3 complex is essential for understanding the mechanisms of translation initiation and the regulation of protein synthesis. Dysregulation of translation initiation can lead to various diseases, including cancer and neurodegenerative disorders. Therefore, eIF3I is a valuable target for research and potential therapeutic interventions.
Recombinant eIF3I produced in Sf9 cells is used in various biochemical and structural studies to elucidate its function and interactions within the eIF3 complex. It is also utilized in assays to screen for inhibitors or modulators of translation initiation, which could have therapeutic potential.