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     Western blot analysis of extracts from HeLa cells, using ZNF18 antibody P41912.    

  
  

Phospho-eIF2α (Ser51) antibodies are essential tools for studying cellular stress responses and translational regulation. The eukaryotic translation initiation factor 2 alpha subunit (eIF2α) plays a critical role in protein synthesis by delivering initiator tRNA to ribosomes. Phosphorylation at Ser51. mediated by stress-activated kinases (e.g., PERK, PKR, GCN2. or HRI), converts eIF2α from a substrate to a competitive inhibitor of its guanine nucleotide exchange factor eIF2B. This inhibits global protein synthesis while allowing selective translation of stress-responsive mRNAs, such as ATF4. to initiate adaptive pathways like the integrated stress response (ISR) or unfolded protein response (UPR).

These antibodies specifically recognize eIF2α phosphorylated at Ser51. enabling researchers to detect and quantify this modification under conditions like endoplasmic reticulum stress, viral infection, nutrient deprivation, or oxidative stress. They are widely used in techniques such as Western blotting, immunofluorescence, and immunoprecipitation to investigate stress signaling dynamics in diseases including neurodegeneration, cancer, and metabolic disorders. Validation often involves using positive controls (e.g., thapsigargin-treated cells) or kinase/phosphatase modulators to confirm specificity. Understanding eIF2α phosphorylation provides insights into cellular survival/death decisions and therapeutic targeting of stress-related pathologies.