EEF2K Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O00418 |
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Other Accession | NP_037434 |
Clone Names | 4011206 |
Gene ID | 29904 |
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Other Names | Eukaryotic elongation factor 2 kinase, eEF-2 kinase, eEF-2K, Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase, EEF2K |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP8162b was selected from the C-term region of human EEF2K. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | EEF2K |
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Function | Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Eukaryotic elongation factor 2 kinase (eEF2k) phosphorylates and inactivates eEF2, thereby inhibiting peptide-chain elongation. eEF2k, which is Ca2+ and calmodulin dependent, can be activated by PKA in response to stress-induced elevation of cAMP levels. eEF2k expression is also modulated by a wide range of stimuli that promote cell growth and protein synthesis. Phosphorylation of eEF2k by p90RSK and p70 S6 kinase at Ser366 or by SAPK4/p38d at Ser359, inactivates eEF2k, which facilitates the dephosphorylation of eEF2, and thus promotes translation.
References
Mol. Cell. Biol. 24 (7), 2986-2997 (2004)J. Biol. Chem. 279 (13), 12220-12231 (2004)Biochem. J. 367 (PT 2), 525-532 (2002)EMBO J. 20 (16), 4370-4379 (2001)
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