The eukaryotic initiation factor 4B (EIF4B) is a critical RNA-binding protein involved in translation initiation, particularly in ribosome recruitment and mRNA scanning. It interacts with EIF4A to enhance helicase activity, facilitating the unwinding of secondary structures in mRNA 5'UTRs, thus promoting cap-dependent translation. EIF4B activity is tightly regulated by phosphorylation through key signaling pathways like mTOR and MAPK, linking its function to cellular growth, proliferation, and stress responses. Dysregulation of EIF4B has been implicated in cancer, where its overexpression correlates with tumor progression, metastasis, and therapeutic resistance.
EIF4B antibodies are essential tools for studying its expression, post-translational modifications (e.g., phosphorylation at Ser422), and interactions in translational control mechanisms. Researchers use these antibodies in techniques like Western blotting, immunofluorescence, and immunoprecipitation to explore EIF4B's role in diseases or under conditions like nutrient deprivation, hypoxia, or oncogenic signaling. Recent studies also investigate EIF4B as a potential therapeutic target, as inhibiting its activity may suppress tumor-specific translation programs. However, challenges remain in dissecting its context-dependent roles due to overlapping functions with other translation factors. Reliable EIF4B antibodies are crucial for advancing research in translation regulation and its implications in cancer biology.