Phospho-eIF2α (Ser51) Antibody #9721
- WB
Supporting Data
| REACTIVITY | H M R Mk Dm |
| SENSITIVITY | Endogenous |
| MW (kDa) | 38 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
- Dm-D. melanogaster
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:10 - 1:50 |
Storage
Protocol
Specificity / Sensitivity
Phospho-eIF2alpha (Ser51) Antibody detects endogenous eIF2alpha only when phosphorylated at Ser51. The antibody does not recognize elF2alpha phosphorylated at other sites. Human eIF2alpha residue Ser52 historically has been referenced as Ser51.
Species Reactivity:
Human, Mouse, Rat, Monkey, D. melanogaster
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.
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).
- Kimball, S.R. (1999) Int. J. Biochem. Cell Biol. 31, 25-29.
- de Haro, C. et al. (1996) FASEB J. 10, 1378-87.
- Kaufman, R.J. (1999) Genes Dev. 13, 1211-33.
- Sheikh, M.S. and Fornace Jr., A.J. (1999) Oncogene 18, 6121-8.
- Cheshire, J.L. et al. (1999) J. Biol. Chem. 274, 4801-6.
- Zamanian-Daryoush, M. et al. (2000) Mol. Cell. Biol. 20, 1278-90.
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