|Application ||WB, IHC|
|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 on the C-terminus of human eEF2 was used as an 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 (C-term) 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. et al, Biol. Chem. 370: 1071-1075, 1989.
2. Carlberg, U, et al. (1990) Eur. J. Biochem. 191, 639
3. Price, N.T, et al. (1991) FEBS Lett. 282, 253
4. Ryazanov, A.G., et al (1988) Biochimie 70, 619
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