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     Western blot analysis of eIF4A1 expression in MCF7 cell lysate.    

  
  

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     All lanes use the Antibody at 1:1K dilution for 1 hour at room temperature.    

  
  

The eukaryotic initiation factor 4A1 (eIF4A1) is a critical ATP-dependent RNA helicase and a core component of the eIF4F complex, which regulates the cap-dependent translation initiation in eukaryotes. As a member of the DEAD-box protein family, eIF4A1 facilitates ribosome recruitment to mRNA by unwinding secondary structures in the 5' untranslated region (UTR) of transcripts. Its activity is tightly coordinated with other translation initiation factors, such as eIF4E and eIF4G, and modulated by signaling pathways like mTOR. Dysregulation of eIF4A1 has been implicated in cancer, neurodegeneration, and viral infection due to its role in controlling the translation of oncoproteins, stress-response proteins, or viral RNAs.

Antibodies targeting eIF4A1 are widely used to study translational regulation, protein synthesis dynamics, and cellular stress responses. They enable the detection of eIF4A1 expression levels, subcellular localization, and interactions within the eIF4F complex through techniques like Western blotting, immunoprecipitation, and immunofluorescence. Specific eIF4A1 antibodies are also employed to validate RNA helicase inhibition by compounds such as silvestrol or hippuristanol in cancer research. Notably, eIF4A1-specific antibodies must distinguish it from its paralog eIF4A2. which shares ~90% sequence homology but exhibits distinct functional roles. These tools have advanced studies on translation-driven pathologies and therapeutic targeting of the eIF4F complex in diseases characterized by aberrant protein synthesis.