Phospho-eEF2 (Thr56) Antibody #2331
- WB
Supporting Data
| REACTIVITY | H M R Hm Mk C |
| SENSITIVITY | Endogenous |
| MW (kDa) | 95 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Hm-Hamster
- Mk-Monkey
- C-Chicken
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Phospho-eEF2 (Thr56) Antibody detects endogenous levels of eEF2 only when phosphorylated at Thr56. It does not recognize eEF2 phosphorylated at other sites.
Species Reactivity:
Human, Mouse, Rat, Hamster, Monkey, Chicken
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr56 of human eEF2. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Eukaryotic elongation factor 2 (eEF2) catalyzes the translocation of peptidyl-tRNA from the A site to the P site on the ribosome. It has been shown that phosphorylation of eEF2 at threonine 56 by eEF2 kinase inhibits its activity (1-4). eEF2 kinase is normally dependent on Ca2+ ions and calmodulin (5,6). eEF2 kinase can also be activated by PKA in response to elevated cAMP levels (7-9), which are generally increased in stress- or starvation-related conditions. A variety of treatments known to raise intracellular Ca2+ or cAMP levels have been shown to result in increased phosphorylation of eEF2, and thus to inhibit peptide-chain elongation. The inactive phosphorylated eEF2 can be converted to its active nonphosphorylated form by a protein phosphatase, most likely a form of protein phosphatase-2A (PP-2A). Insulin, which activates protein synthesis in a wide range of cell types, induces rapid dephosphorylation of eEF2 through mTOR signaling and may involve modulation of the activity of the PP-2A or the eEF2 kinase or both (10).
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