|Reactivity||Human, Mouse, Rat|
|Calculated MW||95338 Da|
|Other Names||Elongation factor 2, EF-2, EEF2, EF2|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminus 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||eEF2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.|
|Cellular Location||Cytoplasm. Nucleus. Note=Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product.|
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Provided below are standard protocols that you may find useful for product applications.
The eukaryotic translation Elongation Factor 2 (eEF2) is a 95 kDa member of the G-protein superfamily. Following peptide bond formation, eEF2 catalyzes translocation of the deacylated tRNA in the P-site and peptidyl tRNA in the A-site into the E- and P- sites, respectively (1). The activity of eEF2 is regulated by phosphorylation (2). To be active, eEF2 must be dephosphorylated, and phosphorylation at Thr-56 causes inactivation, resulting in the termination of mRNA translation (3). eEF2 is phosphorylated by a specific, calcium and calmodulin (Ca/CaM)-dependent eEF2 kinase (4).
1. Rapp, G.; Klaudiny, J.; Hagendorff, G.; Luck, M. R.; Scheit, K. H. : Biol. Chem. Hoppe-Seyler 370: 1071-1075, 1989.
2. Carlberg, U., Nilsson, A. and Nygard, O. (1990) Eur. J. Biochem. 191, 639
3. Price, N.T., Redpath, N.T., Severinov, K.V., Campbell, D.G., Russell, J.M. and Proud, C.G. (1991) FEBS Lett. 282, 253
4. Ryazanov, A.G., Natapov, P.G., Shestakova, E.A., Severin, F.F. and Spirin, A.S. (1988) Biochimie 70, 619
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