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Render Timestamp: 2024-12-26T11:08:39.989Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-12-10 23:02:07.931
Product last modified at: 2024-12-17T09:00:12.363Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
  1. Products /
  2. Primary Antibodies /
  3. eIF4A3 (F9X7Z) Rabbit mAb
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

eIF4A3 (F9X7Z) Rabbit mAb #52960

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 47
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    eIF4A3 (F9X7Z) Rabbit mAb recognizes endogenous levels of total eIF4A3 protein. This antibody does not cross-react with eIF4A1 or eIF4A2 proteins.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro38 of human eIF4A3 protein.

    Background

    The exon junction complex (EJC) plays a critical role in splicing, translation, mRNA localization, and nonsense-mediated decay (NMD). It is comprised of four core proteins, eukaryotic initiation factor 4A3 (eIF4A3), Mago homolog (MAGOH), and RBM8A or Y18, and metastatic lymph node 51 (MLN51) (1-4). The EJC proteins act as a binding platform for auxiliary factors that control mRNA export and NMD (5). RBM8A and MAGOH bind to key NMD factor UPF3B and dock around 20 nucleosides upstream of exon-exon junctions, which helps facilitate proper splicing and NMD functions (6-8). During translation, ribosomes will determine whether NMD factors are needed when encountering a stop codon. If EJCs exist downstream of the stop codon, the ribosome will recruit the SURF complex, and UPF1 phosphorylation will help facilitate the decay of prematurely terminated mRNAs (9,10). The EJC is also involved in the cell cycle as eIF4A3 is phosphorylated at Thr163 by CDK1 and CDK2, which inhibits NMD function and prevents complex formation (11,12). Aberrant RBM8A expression causes cell cycle dysfunction, while low MAGOH expression affects neurological development and proliferation (13,14). EJC members have been implicated in a wide array of diseases and cancer, including hepatocellular carcinoma, glioblastoma, and neurological disorders (15-17).

    eIF4A3 specifically has been linked to many different cancers by facilitating the formation of a vast array of circular RNAs (circRNAs). These circRNAs often act in opposition to key miRNAs, resulting in a loss of checks and balances and tumorigenesis. eIF4A3-dependent circRNAs have been implicated in glioblastoma, triple-negative breast cancer, and gastric cancer among others (18-20). The critical role of eIF4A3 in global splicing, NMD, and cell cycle makes it an attractive target for selective inhibitors (21,22).
    1. Schlautmann, L.P. and Gehring, N.H. (2020) Biomolecules 10, 866. doi: 10.3390/biom10060866.
    2. Leung, C.S. and Johnson, T.L. (2018) Mol Cell 72, 799-801.
    3. Boehm, V. and Gehring, N.H. (2016) Trends Genet 32, 724-735.
    4. Le Hir, H. and Séraphin, B. (2008) Cell 133, 213-6.
    5. Le Hir, H. et al. (2001) EMBO J 20, 4987-97.
    6. Kim, V.N. et al. (2001) Science 293, 1832-6.
    7. Gehring, N.H. et al. (2003) Mol Cell 11, 939-49.
    8. Fribourg, S. et al. (2003) Nat Struct Biol 10, 433-9.
    9. Isken, O. and Maquat, L.E. (2008) Nat Rev Genet 9, 699-712.
    10. Kashima, I. et al. (2006) Genes Dev 20, 355-67.
    11. Mazloomian, A. et al. (2019) Commun Biol 2, 165.
    12. Ryu, I. et al. (2019) Cell Rep 26, 2126-2139.e9.
    13. Ishigaki, Y. et al. (2013) Exp Biol Med (Maywood) 238, 889-97.
    14. Silver, D.L. et al. (2013) Dev Biol 375, 172-81.
    15. Liang, R. et al. (2017) Oncol Rep 37, 2167-2176.
    16. Lin, Y. et al. (2021) Front Oncol 11, 736941.
    17. Brunetti-Pierri, N. et al. (2008) Nat Genet 40, 1466-71.
    18. Wang, R. et al. (2018) Mol Cancer 17, 166.
    19. Zheng, X. et al. (2020) Mol Cancer 19, 73.
    20. Wang, G. et al. (2021) Cancer Cell Int 21, 324.
    21. Ito, M. et al. (2017) J Med Chem 60, 3335-3351.
    22. Iwatani-Yoshihara, M. et al. (2017) ACS Chem Biol 12, 1760-1768.

    Database Links

    UniProt ID: P38919


    Entrez-Gene Id: 9775


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