The eukaryotic initiation factor 4A2 (EIF4A2) is a member of the DEAD-box RNA helicase family, playing a critical role in translation initiation by unwinding secondary structures in mRNA 5'UTRs to facilitate ribosome scanning. Unlike its paralog EIF4A1. which is ubiquitously expressed and integral to the canonical cap-binding complex EIF4F, EIF4A2 exhibits tissue-specific expression and participates in both cap-dependent and alternative translation mechanisms. It is implicated in specialized regulatory processes, including microRNA-mediated repression and stress-adaptive translation, often functioning within the EIF4H complex or interacting with RNA-binding proteins like DAP5 (P97) to modulate specific mRNA subsets.
EIF4A2 antibodies are essential tools for studying its expression, localization, and interactions in diverse biological contexts. They are widely used in techniques such as Western blotting, immunoprecipitation, and immunofluorescence to investigate its role in cellular homeostasis, development, and disease. Dysregulation of EIF4A2 has been linked to cancer progression, neurological disorders, and viral infection responses, with studies highlighting its dual roles as a tumor suppressor or promoter depending on cellular context. Researchers also utilize these antibodies to explore EIF4A2's involvement in translational reprogramming under stress conditions, such as hypoxia or nutrient deprivation, and its crosstalk with oncogenic signaling pathways. Specificity validation remains crucial due to high homology with EIF4A1. requiring careful antibody selection and knockout controls.