The eukaryotic elongation factor 2 kinase (EEF2K), also known as calmodulin-dependent protein kinase III, is a serine/threonine kinase that regulates protein synthesis by phosphorylating and inactivating eukaryotic elongation factor 2 (eEF2). This phosphorylation event slows translational elongation under stress conditions, enabling cells to conserve energy and adapt to metabolic or environmental challenges. EEF2K activity is modulated by nutrient-sensing pathways, including AMPK and mTOR signaling, linking it to cellular energy homeostasis, autophagy, and stress responses.
EEF2K antibodies are essential tools for studying its expression, activation, and functional roles in physiological and pathological contexts. These antibodies enable detection of EEF2K protein levels, phosphorylation status, and interactions via techniques like Western blotting, immunohistochemistry, and immunoprecipitation. Research using EEF2K antibodies has highlighted its involvement in cancer progression, where it promotes survival under hypoxia or nutrient deprivation, and neurodegenerative diseases, where dysregulated eEF2 phosphorylation may contribute to synaptic dysfunction. Additionally, EEF2K knockout models and inhibitor studies have positioned it as a potential therapeutic target. Validated antibodies are critical for distinguishing EEF2K isoforms and assessing its cross-talk with signaling networks, aiding mechanistic exploration in diseases like glioblastoma, Alzheimer’s, and metabolic disorders.