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Anti-eEF2K (Ser-398), Phosphospecific Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O00418 |
|---|---|
| Reactivity | Bovine |
| Host | Rabbit |
| Clonality | Rabbit Polyclonal |
| Isotype | IgG |
| Calculated MW | 82144 Da |
| Gene ID | 29904 |
|---|---|
| Other Names | eEF-2, eEF-2K, CaMK-III, eukaryotic elongation factor |
| Target/Specificity | 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. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Anti-eEF2K (Ser-398), Phosphospecific Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
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