EIF3G Protein, Human (His-SUMO)

The EIF3G protein is an RNA-binding component of the eIF-3 complex that initiates protein synthesis by promoting the recruitment of factors to form the 43S PIC. EIF3G is critical in both mRNA recruitment and AUG recognition scanning. EIF3G Protein, Human (His-SUMO) is the recombinant human-derived EIF3G protein, expressed by E. coli , with N-SUMO, N-6*His labeled tag.

The EIF3G protein functions as an RNA-binding component within the eukaryotic translation initiation factor 3 (eIF-3) complex, a crucial player in various steps of protein synthesis initiation. The eIF-3 complex, associated with the 40S ribosome, facilitates the recruitment of essential factors, such as eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi, and eIF-5, to form the 43S pre-initiation complex (43S PIC). Subsequently, EIF3G, as part of the eIF-3 complex, promotes mRNA recruitment to the 43S PIC and scanning for AUG recognition. Furthermore, it plays a key role in the disassembly and recycling of post-termination ribosomal complexes, preventing premature joining of the 40S and 60S ribosomal subunits before initiation. The eIF-3 complex, including EIF3G, selectively targets and initiates translation of specific mRNAs involved in cell proliferation, influencing processes like cell cycling, differentiation, and apoptosis. Through different modes of RNA stem-loop binding, EIF3G can exert either translational activation or repression. In the context of microbial infection, such as FCV infection, EIF3G is implicated in the ribosomal termination-reinitiation event leading to the translation of specific viral proteins.

Human

E. coli

N-SUMO;N-6*His

O75821 (P2-N320)

8666  [NCBI]

Full Length of Mature Protein

PTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSPEPELLPGAPLPPPKEVINGNIKTVTEYKIDEDGKKFKIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN

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

<1 EU/μg, determined by LAL method.