EEF2 Antibody
Purified Mouse Monoclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, IHC, ICC, E |
---|---|
Primary Accession | P13639 |
Reactivity | Human |
Host | Mouse |
Clonality | Monoclonal |
Clone Names | 5B6 |
Isotype | IgG1 |
Calculated MW | 95kDa |
Description | This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. This protein is completely inactivated by EF-2 kinase phosporylation. (provided by RefSeq) |
Immunogen | Purified recombinant fragment of human EEF2 expressed in E. Coli. |
Formulation | Ascitic fluid containing 0.03% sodium azide. |
Gene ID | 1938 |
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Other Names | Elongation factor 2, EF-2, EEF2, EF2 |
Dilution | E~~1/10000 WB~~1/500 - 1/2000 IHC~~1/200 - 1/1000 IF~~1/200 - 1/1000 |
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. |
Name | EEF2 |
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Synonyms | EF2 |
Function | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:26593721). 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 (PubMed:26593721). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed:26593721). |
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.
References
1. Mol Cell Biol. 2008 Dec;28(23):7050-65. 2. Am J Physiol Regul Integr Comp Physiol. 2009 Feb;296(2):R326-33.

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