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     Western blot analysis of Phospho-eIF4EBP1/2/3 (T46+T46+T32)  expression in 293 treated with FBS+293.    

  
  

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

  
  

The Phospho-eIF4EBP1/2/3 (T46+T46+T32) antibody detects the phosphorylated forms of eukaryotic translation initiation factor 4E-binding proteins 1. 2. and 3 (4E-BP1/2/3) at specific threonine residues (T46 in 4E-BP1/2 and T32 in 4E-BP3). These proteins regulate cap-dependent translation by binding to eIF4E, a key component of the translation initiation complex. When hypophosphorylated, 4E-BPs inhibit eIF4E interaction with eIF4G, blocking assembly of the eIF4F complex and suppressing mRNA translation. Phosphorylation of 4E-BPs, primarily mediated by the mTORC1 signaling pathway, releases eIF4E, enabling translation initiation and promoting cell growth, proliferation, and survival.

The antibody specifically recognizes phosphorylation at T46 in 4E-BP1/2 and T32 in 4E-BP3. sites associated with mTORC1 activation. These phosphorylation events serve as biomarkers for mTOR pathway activity, which is frequently dysregulated in cancers, metabolic disorders, and aging. Researchers use this antibody in techniques like Western blotting or immunofluorescence to study mTOR signaling dynamics, protein synthesis regulation, and therapeutic responses to mTOR inhibitors. Its specificity for multiple 4E-BP isoforms allows broad detection of mTORC1-driven phosphorylation events across diverse biological contexts, linking translational control to disease mechanisms and treatment strategies.