A synthetic phospho-peptide corresponding to residues surrounding Ser51 of human eIF-2a was used as immunogen. The antibody only detects eIF-2a phosphorylated on Serine 51. Predicted to cross-react with mouse, rat, bovine and pig, based on sequence homology.
Store at -20 °C. Buffer: Antibody buffer, sodium azide, glycerol, and BSA. Stable for 12 months from date of receipt.
Eukaryotic initiation factor 2 (eIF2) plays a central role in initiating translation, and provides for a rate-limiting step in protein synthesis. Phosphorylation of a-subunit of eIF2 effectively prevents formation of the eIF2/GTP/Met-tRNAi complex and inhibits global protein synthesis (1-3). Three distinct protein kinases regulate protein synthesis in eukaryotic cells by phosphorylating the a-subunit of eIF2 at Serine51 (3). Phosphorylation occurs under a wide variety of different stimuli, including heat shock, serum deprivation, glucose starvation, amino acid starvation, exposure to heavy metal ions, and viral infection (3).
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