Product Pathways - Translational Control
Phospho-eIF2α (Ser51) Antibody #9721
|9721L||300 µl (30 western blots)||---||In Stock||---|
|9721S||100 µl (10 western blots)||---||In Stock||---|
|9721||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey, D. melanogaster||Endogenous||38||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
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.
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, 1378-1387.
- Kaufman, R.J. (1999) Genes Dev. 13, 1211-1233.
- Sheikh, M.S. and Fornace Jr., A.J. (1999) Oncogene 18, 6121-6128.
- Cheshire, J.L. et al. (1999) J. Biol. Chem. 274, 4801-4806.
- Zamanian-Daryoush, M. et al. (2000) Mol. Cell. Biol. 20, 1278-1290.
- Koumenis, C. et al. (2002) . Mol Cell Biol 22, 7405-7416. Applications: Western Blotting.
- Li, W. et al. (2004) Mol. Cell. Biol. 24, 3295-3306. Applications: Western Blotting.
- Chen, H.J. et al. (2010) J Biol Chem 285, 40266-81. Applications: Western Blotting.
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