eIF3A抗体—艾普蒂

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     Western blot analysis of eIF3A expression in Jurkat cell lysate.    

  
  

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     Immunofluorescent analysis using the Antibody at 1:150 dilution.    

  
  

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     Immunofluorescent analysis using the Antibody at 1:200 dilution.    

  
  

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     Immunofluorescent analysis using the Antibody at 1:50 dilution.    

  
  

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     Immunofluorescent analysis using the Antibody at 1:50 dilution.    

  
  

The eukaryotic translation initiation factor 3 subunit A (eIF3A) is a critical component of the eIF3 complex, the largest multiprotein assembly involved in initiating cap-dependent translation in eukaryotes. eIF3A, also known as eIF3-p170. plays a central role in ribosome recruitment to mRNA, scanning for the start codon, and stabilizing interactions between the 40S ribosomal subunit and other initiation factors. Structurally, it contains conserved PCI (Proteasome, COP9. eIF3) and RNA recognition motif (RRM) domains, enabling interactions with ribosomes and regulatory RNAs. Dysregulation of eIF3A has been implicated in cancers, including breast, lung, and ovarian cancers, where its overexpression often correlates with poor prognosis, tumor proliferation, and drug resistance.

Antibodies targeting eIF3A are essential tools for studying its expression, localization, and functional roles. They are widely used in techniques such as Western blotting, immunofluorescence, and immunohistochemistry to investigate eIF3A's involvement in translational control and disease mechanisms. Commercially available eIF3A antibodies are typically raised against specific epitopes within its N-terminal or C-terminal regions and validated for specificity across human, mouse, and rat models. Recent studies also utilize these antibodies to explore eIF3A's non-canonical roles, including its interaction with viral RNAs and stress granule dynamics. However, variability in antibody performance across experimental conditions underscores the need for rigorous validation to ensure reproducibility in translational research.