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anti-Human EEF2 Anticorps:
anti-Mouse (Murine) EEF2 Anticorps:
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Human Monoclonal EEF2 Primary Antibody pour ICC, IHC - ABIN969090
Maggi, Kuchenruether, Dadey, Schwope, Grisendi, Townsend, Pandolfi, Weber: Nucleophosmin serves as a rate-limiting nuclear export chaperone for the Mammalian ribosome. dans Molecular and cellular biology 2008
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Human Monoclonal EEF2 Primary Antibody pour IF, ELISA - ABIN966028
Rose, Bisiani, Vistisen, Kiens, Richter: Skeletal muscle eEF2 and 4EBP1 phosphorylation during endurance exercise is dependent on intensity and muscle fiber type. dans American journal of physiology. Regulatory, integrative and comparative physiology 2009
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Human Polyclonal EEF2 Primary Antibody pour ELISA, ICC - ABIN6261441
Deng, Luo, Lai, Song, Peng, Wei: Myostatin inhibits eEF2K-eEF2 by regulating AMPK to suppress protein synthesis. dans Biochemical and biophysical research communications 2017
our study indicates that expression of eEF2 protein is a potential biomarker for evaluating prostate cancer
eEF2 may be activated in a positive feedback cycle through inactivation of eEF2K via the PI3K/Akt/mTOR pathway.
the direct interaction of AKT2 and EF2 was found to be dynamically regulated in embryonic rat cardiomyocytes
These results suggest that binding of eEF2 to the ribosome alters its conformation, resulting in a weakened affinity of eIF5A and impairment of this interplay compromises cell growth due to translation elongation defects.
nuclear localization of active eEF-2 depends upon its interaction with p53, as cells lacking p53 contain less active eEF-2 in the nuclear compartment
High serum eukaryotic elongation factor 2 level is associated with non-small cell lung cancer.
Results indicated that the eEF2 gene is overexpressed in the majority of several types of cancers and plays an oncogenic role in cancer cell growth.
The expression levels of three putative HA-regulated proteins (TALDO, ANXA1 and EF2) in control, H2O2-, HA- and HA/H2O2-treated OA chondrocytes were verified by Western blotting and the results indeed support the notion that HA acts in anti-oxidation
Data indicate that the accumulation of the cleaved C-terminal small fragment of eukaryotic elongation factor 2 (eEF2) in the nucleus, and C-terminal Src kinase (Csk) could enhance the proteolytic cleavage of eEF2.
Thiopental inhibits global protein synthesis by repression of eukaryotic elongation factor 2 and protects from hypoxic neuronal cell death.
A single amino acid substitution in eukaryotic elongation factor 2 co-segregates with the disease phenotype of spinocerebellar ataxia 26.
EEF2 phosphorylation by cyclin A-cyclin-dependent kinase 2 (CDK2) on a novel site, serine 595 (S595), directly regulates T56 phosphorylation by eEF2K.
Burn induces prolonged activation of eEF2K and eEF2 in pediatric patients.
PHD2 modulated eEF2 activity and protein translation under acute hypoxia.
NH125 induces eEF2 phosphorylation (peEF2) through multiple pathways in cancer cells
Training in the fasted state, compared with identical training with ample carbohydrate intake, facilitates post-exercise dephosphorylation of eEF2.
results suggest that eEF2 is an anti-apoptotic marker in lung adenocarcinoma
eEF-2 is activated by both lithium and GSK-3, whereas, lithium treatment and inhibition of GSK-3 have opposing effects on eEF-2.
melanoma antigen expressed in G361, a representative melanoma cell line/ reacted with autoantibodies in patient sera
inhibition of protein synthesis under high pressure occurs independent of the phosphorylation of eEF-2
Myostatin inhibits eEF2K-eEF2 by regulating AMPK to suppress protein synthesis.
IL-6 induces the activation of the Stat3 signaling and promotes the downmodulation of the p90RSK/eEF2 and mTOR/p70S6K axes, while it does not affect the activation of AKT.
AMPKalpha2 controls cardiac p70S6K under normoxia and regulates eEF-2 but not the mTOR-p70S6K pathway during ischemia.
The MKK3/6-p38gamma/delta pathway mediated an inhibitory phosphorylation of eukaryotic elongation factor 2 (eEF2) kinase, which in turn promoted eEF2 activation (dephosphorylation) and subsequent TNF-alpha elongation.
Diphthamide modification on eukaryotic elongation factor 2 is needed to assure fidelity of mRNA translation and mouse development
induced by basic fibroblast growth factor via mitogen-activated protein kinase
eEF-2 phosphorylation has a role in protein synthesis for memory consolidation
A mouse that was mutant for the gene, Dph4, was identified.
exogenous ROS inhibit mTOR, eIF2alpha, and eEF2, mTOR and eEF2 were largely refractory to ROS generated under moderate hypoxia (0.5% O(2)).
eIF2alpha phosphorylation is required for phosphorylation of eukaryotic elongation factor 2 (eEF-2) during nutrient starvation
Data show that the levels of active eEF2 increased and decreased in BDNF transgenic and BDNF knock-out mice, respectively.
Eukaryotic elongation factor-2 (eEF2) may be a limiting factor in milk protein synthesis (Review)
EF-2 is a developmentally regulated gene and might play important roles during the early development of zebrafish embryos.
Whole mount in situ hybridization on zebrafish embryos shows that the transcripts of EF-2 gene are detected during the early development of zebrafish embryo and constantly change from 5-somite stage to protruding-mouth stage.
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.
elongation factor 2
, polypeptidyl-tRNA translocase
, elongation factor-2
, eukaryotic translation elongation factor 2
, elongation factor 2-like
, eukaryotic translation elongation factor 2, like
, ETS-related factor2
, LOW QUALITY PROTEIN: elongation factor 2
, CG2238 gene product from transcript CG2238-RD
, ELONGATION FACTOR 2
, elongation factor 2b
, eukaryotic translation elongation factor 2b