Cell Signaling Technology

Product Pathways - Translational Control

Phospho-eIF2α (Ser51) Antibody #9721

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Mk Dm Endogenous 38 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  Dm=D. melanogaster
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-eIF2alpha (Ser51) Antibody detects endogenous eIF2alpha only when phosphorylated at Ser51. The antibody does not recognize elF2alpha phosphorylated at other sites.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser51 of human eIF2alpha. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from PC12 cells, untreated or thapsigargin-treated (300 nM), using Phospho-eIF2alpha (Ser51) Antibody (upper) or eIF2alpha Antibody #9722 (lower).

Background

Phosphorylation of the eukaryotic initiation factor 2 (eIF2) α subunit is a well-documented mechanism to downregulate protein synthesis under a variety of stress conditions. eIF2 binds GTP and Met-tRNAi and transfers Met-tRNA to the 40S subunit to form the 43S preinitiation complex (1,2). eIF2 promotes a new round of translation initiation by exchanging GDP for GTP, a reaction catalyzed by eIF2B (1,2). Kinases that are activated by viral infection (PKR), endoplasmic reticulum stress (PERK/PEK), amino acid deprivation (GCN2), or heme deficiency (HRI) can phosphorylate the α subunit of eIF2 (3,4). This phosphorylation stabilizes the eIF2-GDP-eIF2B complex and inhibits the turnover of eIF2B. Induction of PKR by IFN-γ and TNF-α induces potent phosphorylation of eIF2α at Ser51 (5,6).

  1. Kimball, S.R. (1999) Int. J. Biochem. Cell Biol. 31, 25-29.
  2. De Haro, C. et al. (1996) FASEB J. 10, 1378-1387.
  3. Kaufman, R.J. (1999) Genes Dev. 13, 1211-1233.
  4. Sheikh, M.S. and Fornace Jr., A.J. (1999) Oncogene 18, 6121-6128.
  5. Cheshire, J.L. et al. (1999) J. Biol. Chem. 274, 4801-4806.
  6. Zamanian-Daryoush, M. et al. (2000) Mol. Cell. Biol. 20, 1278-1290.

Application References

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