Anti-eEF2K (Ser-500), Phosphospecific Antibody

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.

Our eEF2K (Ser-500) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat eEF2K (Ser-500) and is antigen affinity purified. It is great for use in WB.

Phospho-eEF2K (Ser-500) synthetic peptide (coupled to carrier protein) corresponds to amino acids surrounding Ser-500 in human eEF2K. This sequence is well conserved in rat and mouse eEF2K, and has low homology to other proteins.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

The antibody detects a 105 kDa* protein corresponding to the molecular mass of eEF2K on SDS-PAGE immunoblots of human recombinant eEF2K autophosphorylated in the presence of Ca2+ and Calmodulin. This reactivity is removed after lambda phosphatase treatment. In addition, the antibody detects eEF2K after calyculin A treatment of mouse C2C12 cells, but not in control cells.