EIF3I Human, Sf9

Eukaryotic Translation Initiation Factor 3I Human Recombinant, Sf9
Cat. No.
BT4613
Source
Sf9, Baculovirus cells.
Synonyms

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.

Appearance
Sterile Filtered colorless solution.
Purity

Greater than 90.0% as determined by SDS-PAGE.

Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
Eukaryotic translation initiation factor 3, subunit I (EIF3I), a component of the eukaryotic translation initiation factor 3 (eIF-3) complex, plays a crucial role in protein synthesis initiation. The eIF-3 complex facilitates multiple steps, including binding to the 40S ribosome, recruiting essential initiation factors (eIF-1, eIF-1A, eIF-2: GTP: methionyl-tRNAi, and eIF-5) to form the 43S pre-initiation complex (43S PIC), promoting mRNA recruitment to the 43S PIC, and enabling mRNA scanning for AUG recognition. Additionally, the eIF-3 complex participates in post-termination ribosomal complex disassembly and recycling, preventing premature 40S and 60S ribosomal subunit joining. EIF3I has been implicated in diseases like clonorchiasis and tonsillitis.
Description
EIF3I Human Recombinant, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain consisting of 331 amino acids (with a sequence spanning from amino acid 1 to 325) and possessing a molecular weight of 37.3kDa. On SDS-PAGE under reducing conditions, it migrates at a range of 40-57kDa. This recombinant protein is engineered with a 6-amino acid His-tag fused at the C-terminus and is purified through proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The EIF3I protein solution is provided at a concentration of 0.25mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 0.1M NaCl, 40% Glycerol, and 1mM DTT.
Stability
For short-term storage (up to 2-4 weeks), the entire vial can be stored at 4°C. For extended storage, it is recommended to store the protein frozen at -20°C. To further enhance long-term stability, the addition of a carrier protein (either HSA or BSA) at a concentration of 0.1% is advised. Multiple freeze-thaw cycles should be avoided.
Purity
The purity of the protein is determined to be greater than 90.0% using SDS-PAGE analysis.
Synonyms

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.

Source
Sf9, Baculovirus cells.
Amino Acid Sequence

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.

Product Science Overview

Introduction

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).

Structure and Function

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 .

Recombinant Production in Sf9 Cells

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 .

Applications and Importance

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.

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