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Mouse Anti-EIF3I (AA 226-326) Recombinant Antibody (CBFYE-0183) (CBMAB-E0426-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYE-0183
Antibody Isotype
IgG2a, κ
Application
ELISA, WB

Basic Information

Immunogen
Partial recombinant from EIF3S2 with GST tag MW of the GST tag alone is 26 KDa
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.2
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 226-326

Target

Full Name
Eukaryotic Translation Initiation Factor 3 Subunit I
Introduction
EIF3I (Eukaryotic Translation Initiation Factor 3 Subunit I) is a Protein Coding gene. Among its related pathways are Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S and Viral mRNA Translation. Gene Ontology (GO) annotations related to this gene include translation initiation factor activity. An important paralog of this gene is STRAP.
Entrez Gene ID
8668
UniProt ID
Q13347
Alternative Names
Eukaryotic Translation Initiation Factor 3 Subunit I; Eukaryotic Translation Initiation Factor 3, Subunit 2 Beta, 36kDa; Eukaryotic Translation Initiation Factor 3 Subunit 2; TGF-Beta Receptor-Interacting Protein 1; EIF3S2; TRIP-1; TRIP1; Eukaryotic Translation Initiation Factor 3, Subunit 2 (Beta, 36kD); Eukaryotic Translation Initiation Factor 3, Subunit I
Research Area
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815).

The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632).

The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773).
Biological Process
Cytoplasmic translational initiation Source: GO_Central
Formation of cytoplasmic translation initiation complex Source: UniProtKB-UniRule
Translational initiation Source: UniProtKB
Cellular Location
Cytoplasm
PTM
Phosphorylated by TGF-beta type II receptor.
More Infomation

Kuai, L., Xiang, Y. W., Chen, Q. L., Ru, Y., Yin, S. Y., Li, W., ... & Li, B. (2022). PD-L1 Triggered by Binding eIF3I Contributes to the Amelioration of Diabetes-Associated Wound Healing Defects by Regulating IRS4. Journal of Investigative Dermatology, 142(1), 220-231.

Lin, Z., Shen, D., Yang, B., & Woo, C. M. (2022). Molecular and structural characterization of lenalidomide-mediated sequestration of eIF3i. bioRxiv.

Ma, S., Dong, Z., Cui, Q., Liu, J. Y., & Zhang, J. T. (2021). eIF3i regulation of protein synthesis, cell proliferation, cell cycle progression, and tumorigenesis. Cancer Letters, 500, 11-20.

Krassnig, S., Wohlrab, C., Golob-Schwarzl, N., Raicht, A., Schatz, C., Birkl-Toeglhofer, A. M., ... & Haybaeck, J. (2021). A profound basic characterization of eIFs in gliomas: Identifying eIF3I and 4H as Potential novel target candidates in glioma therapy. Cancers, 13(6), 1482.

Roobol, A., Roobol, J., Smith, M. E., Carden, M. J., Hershey, J. W., Willis, A. E., & Smales, C. M. (2020). Engineered transient and stable overexpression of translation factors eIF3i and eIF3c in CHOK1 and HEK293 cells gives enhanced cell growth associated with increased c-Myc expression and increased recombinant protein synthesis. Metabolic engineering, 59, 98-105.

Llácer, J. L., Hussain, T., Dong, J., Gordiyenko, Y., & Hinnebusch, A. G. (2020). eIF3b and eIF3i relocate together to the ribosomal subunit interface during translation initiation and modulate start codon selection. bioRxiv, 453688.

Xiao, W., Zhang, W., Huang, H., Xie, Y., Zhang, Y., Guo, X., ... & Song, X. (2019). Cancer targeted gene therapy for inhibition of melanoma lung metastasis with eiF3i shRNA loaded liposomes. Molecular Pharmaceutics, 17(1), 229-238.

Chai, R. C., Wang, N., Chang, Y. Z., Zhang, K. N., Li, J. J., Niu, J. J., ... & Wang, Y. Z. (2019). Systematically profiling the expression of eIF3 subunits in glioma reveals the expression of eIF3i has prognostic value in IDH-mutant lower grade glioma. Cancer Cell International, 19(1), 1-13.

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For research use only. Not intended for any clinical use.

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