|Reactivity||Human, Mouse, Rat|
|Calculated MW||82144 Da|
|Other Names||Eukaryotic elongation factor 2 kinase, eEF-2 kinase, eEF-2K, Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase, EEF2K|
|Target/Specificity||A synthetic peptide corresponding to residues in the Calmodulin binding region of human eEF2 was used as immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|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||eEF-2K Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|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.
Eukaryotic elongation factor-2 kinase (eEF-2k) previously known as Ca2+/calmodulin-dependent protein kinase III, is an abundant cytoplasmic protein highly specific for elongation factor-2 (eEf-2) (1). Phosphorylation of eEF-2 by eEF-2 kinase on specific threonine residues results in the inactivation of eEF-2 and in termination of mRNA translation (2). The activity of eEF2 kinase is not only dependent upon Ca2+ ions, calmodulin (CaM) and insulin, but is also regulated both negatively and positively by phosphorylation by different protein kinases (AMPK, S6K1, p90 RSK) (3-4). There is also evidence that eEF-2 phosphorylation is involved in the regulation of cell cycle progression, cellular differentiation, oogensis and malignant tumors (5-6).
1. Ryazanov et al. Proc Nat Acad Sci 94: 4884-4889, 1997
2. Ryazanov AG, et al. Nature 334:170-173, 1988.
3. Diggle, TA, et al. FEBS Lett 457:189-192, 1999.
4. Wang, XW, EMBO J 20:4370-4379, 2001.
5. End D, et al. J Biol Chem 257:9223-9225, 1988.
6. Severinov, KV, et al. New Biol 2: 887-893, 1990.
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