EIF3M Protein, Human (His-SUMO)

The EIF3M protein is a component of the eIF-3 complex and promotes protein synthesis initiation (eg, mRNA recruitment, scanning, and ribosomal subunit attachment) (PubMed:17403899, PubMed:25849773). EIF3M Protein, Human (His-SUMO) is the recombinant human-derived EIF3M protein, expressed by E. coli , with N-His, N-SUMO labeled tag. The total length of EIF3M Protein, Human (His-SUMO) is 373 a.a., with molecular weight of ~58.4 kDa.

EIF3M protein serves as an integral component of the eukaryotic translation initiation factor 3 (eIF-3) complex, crucial for orchestrating multiple steps in the initiation of protein synthesis. This complex associates with the 40S ribosome, facilitating 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). EIF-3M actively promotes mRNA recruitment to the 43S PIC, scanning of the mRNA for AUG recognition, and subsequent prevention of premature joining of the 40S and 60S ribosomal subunits prior to initiation. Furthermore, the EIF-3 complex plays a pivotal role in the disassembly and recycling of post-termination ribosomal complexes. Remarkably, EIF3M is instrumental in the translation initiation of specific mRNAs associated with cell proliferation, encompassing processes like cell cycling, differentiation, and apoptosis. It employs distinct modes of RNA stem-loop binding to exert either translational activation or repression. Additionally, in the context of microbial infection, EIF3M may facilitate virus entry during infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2).

Human

E. coli

N-His;N-SUMO

Q7L2H7 (2S-374T)

10480  [NCBI]

SVPAFIDISEEDQAAELRAYLKSKGAEISEENSEGGLHVDLAQIIEACDVCLKEDDKDVESVMNSVVSLLLILEPDKQEALIESLCEKLVKFREGERPSLRLQLLSNLFHGMDKNTPVRYTVYCSLIKVAASCGAIQYIPTELDQVRKWISDWNLTTEKKHTLLRLLYEALVDCKKSDAASKVMVELLGSYTEDNASQARVDAHRCIVRALKDPNAFLFDHLLTLKPVKFLEGELIHDLLTIFVSAKLASYVKFYQNNKDFIDSLGLLHEQNMAKMRLLTFMGMAVENKEISFDTMQQELQIGADDVEAFVIDAVRTKMVYCKIDQTQRKVVVSHSTHRTFGKQQWQQLYDTLNAWKQNLNKVKNSLLSLSDT

Approximately 58.4 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.