Catalog # EX4415
phospho-eEF2K (Thr-348) Peptide
Blocking Peptide
| Blocking | 1:1000 |
| ELISA | 50 ng/well |
Size 50 μg
Eukaryotic elongation factor 2 (eEF2) catalyzes the translocation of peptidyl-tRNA from the A site to the P site on the ribosome. eEF2 kinase (eEF2K) phosphorylates and inactivates eEF2, resulting in the inhibition of peptide-chain elongation. eEF2K is normally dependent on Ca2+ ions and calmodulin, and can be activated by PKA in response to elevated cAMP levels during cell stress- or starvation-related conditions. Regulation of eEF2K occurs through phosphorylation at multiple sites. Ser-78 phosphorylation is required for calmodulin binding and eEF2K activity, while phosphorylation of Ser-500 is required for Ca2+/calmodulin-independent kinase activity. Thr-348 is an autophosphorylation site that is required for kinase activity. Inhibitory phosphorylation may also regulate eEF2K, since phosphorylation at Ser-359 by SAPK4/p38δ causes inactivation of eEF2K. Thus, multisite phospho-regulation of eEF2K may be important for proper control of eEF2K activity and protein translation.
References
Tavares, C.D. et al. (2012) Biochemistry. 51(11):2232.
Smith, E.M. & Proud, C.G. (2008) EMBO J. 27(7):1005.
Diggle, T.A., et al. (2001) Biochem J. 353(3):621.
Ryazanov, A.G. et al. (1997) Proc Natl Acad Sci. USA. 94:4884.
*For more information, see UniProt Accession O00418
The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.
*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains:
