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EEF1A2 encodes an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. Additionally we are shipping EEF1A2 Proteins (6) and many more products for this protein.
Showing 10 out of 64 products:
Human Polyclonal EEF1A2 Primary Antibody for EIA, IHC (p) - ABIN952027
Lee, Surh: eEF1A2 as a putative oncogene. in Annals of the New York Academy of Sciences 2009
Show all 2 references for ABIN952027
Human Polyclonal EEF1A2 Primary Antibody for ELISA, WB - ABIN560693
Scaggiante, Dapas, Bonin, Grassi, Zennaro, Farra, Cristiano, Siracusano, Zanconati, Giansante, Grassi: Dissecting the expression of EEF1A1/2 genes in human prostate cancer cells: the potential of EEF1A2 as a hallmark for prostate transformation and progression. in British journal of cancer 2012
Show all 2 references for ABIN560693
Cow (Bovine) Polyclonal EEF1A2 Primary Antibody for WB - ABIN2783277
Grassi, Scaggiante, Farra, Dapas, Agostini, Baiz, Rosso, Tiribelli: The expression levels of the translational factors eEF1A 1/2 correlate with cell growth but not apoptosis in hepatocellular carcinoma cell lines with different differentiation grade. in Biochimie 2007
Human Polyclonal EEF1A2 Primary Antibody for IHC, IHC (p) - ABIN4307082
Qiu, Huang, Chen, Li, Wu, Wu, Huang: Eukaryotic elongation factor-1α 2 knockdown inhibits hepatocarcinogenesis by suppressing PI3K/Akt/NF-κB signaling. in World journal of gastroenterology 2016
Mouse (Murine) Polyclonal EEF1A2 Primary Antibody for IHC (p), WB - ABIN656488
Yanaka, Kaseda, Tanaka, Nogusa, Sumiyoshi, Kato: Generation of a zinc finger protein ZPR1 mutant that constitutively interacted with translation elongation factor 1alpha. in Bioscience, biotechnology, and biochemistry 2009
eEF1A2 is highly expressed in hepatocellular carcinoma. Its silencing significantly decreases HCC (show FAM126A Antibodies) tumorigenesis, likely by inhibiting PI3K (show PIK3CA Antibodies)/Akt (show AKT1 Antibodies)/NF-kappaB (show NFKB1 Antibodies) signaling.
Differential gene expression analysis demonstrated significant upregulation of PDZK1IP1, EEF1A2 and RPL41 (ENSG00000279483) genes in the intrahepatic cholangiocarcinoma samples when compared with the matched paratumor samples.
In both cases, a de novo recurrent heterozygous mutation in EEF1A2 [c.364G>A (p.E122K)] was identified by whole-exome sequencing. CONCLUSION: This report provides clinical data on epileptic encephalopathy in patients with EEF1A2 mutation. Continuous high-voltage delta activity seen over both parietal areas may be a unique manifestation of EEF1A2 mutation.
Our results provide novel information on the intracellular distribution and interaction of eEF1A (show EEF1A1 Antibodies) isoforms.
By directly targeting eEF1A2.
Both eEF1A1 (show EEF1A1 Antibodies) and eEF1A2 colocalise with all eEF1B (show EEF1B2 Antibodies) subunits, in such close proximity that they are highly likely to be in a complex.
De novo EEF1A2 mutations in patients with characteristic facial features, intellectual disability, autistic behaviors and epilepsy.
Finally, a strong association between the expression of EEF1A2, phosphorylated AKT (show AKT1 Antibodies) and MDM4 (show MDM4 Antibodies) was observed in human HCC (show FAM126A Antibodies) samples. Strong activation of the EEF1A2/PI3K (show PIK3CA Antibodies)/AKT (show AKT1 Antibodies)/mTOR (show FRAP1 Antibodies)/MDM4 (show MDM4 Antibodies) signaling pathway was observed in HCC (show FAM126A Antibodies) patients
Overexpression of eEF1A2 was correlated with worse outcomes in gastric cancer patients, suggesting its critical roles in the carcinogenesis of gastric cancer.
miR (show MLXIP Antibodies)-663 and miR (show MLXIP Antibodies)-744 mediate inhibition of the proto-oncogene (show RAB1A Antibodies) eEF1A2 expression that results in retardation of the MCF7 cancer cells proliferation. We also observed upregulation of miR (show MLXIP Antibodies)-663 and miR (show MLXIP Antibodies)-744 with corresponding downregulation of eEF1A2 in resveratrol-treated MCF7 cells, suggesting that resveratrol may influence eEF1A2 expression through a miRNA-dependent pathway.
eEF1A2 crystals obtained using ammonium sulfate as precipitant diffracted to 2.5 A resolution and belonged to space group P6(1)22 or P6(3)22 (unit-cell parameters a = b = 135.4, c = 304.6 A).
This provides the first in vivo confirmation that eEF1A2 plays an important role in translation.
Heterozygous mutant mice showed no deficit in neuromuscular function or signs of spinal cord pathology, in spite of the low levels of eEF1A2
In-depth analysis using site-directed mutagenesis revealed that PKCbetaI could phosphorylate Ser (show SIGLEC1 Antibodies)(3) of the eEF1A2 isoform and that the association between eEF1A2 and PKCbetaI was dependent on the phosphorylation status of eEF1A2
EEF1A2 may play contribute to the induction or progression of some plasmacytomas and a small percentage of multiple myeloma.
these results suggest an important role for eEF1A2 in driving cap-independent translation of utrophin (show UTRN Antibodies) A in skeletal muscle.
expression of eEF1A-2/S1 protein is activated upon myogenic differentiation
This is a putative oncogene (show RAB1A Antibodies) in ovarian cancer.
Data suggest that spontaneous failure of eEF1A2 expression in the wasted mutant first triggers gliosis in spinal cord and retraction of motor nerve terminals in muscle, and then motor neuron pathology and death.
eEF1A-2 interacts with Prdx-I to functionally provide cells with extraordinary resistance to oxidative stress-induced (show SQSTM1 Antibodies) cell death[eEF1A-2 and Prdx-I]
The above findings suggest that an increase in free-form eEF1A under alkaline conditions plays a critical role in alkalinization-induced cell growth.
This gene encodes an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This isoform (alpha 2) is expressed in brain, heart and skeletal muscle, and the other isoform (alpha 1) is expressed in brain, placenta, lung, liver, kidney, and pancreas. This gene may be critical in the development of ovarian cancer. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
eukaryotic translation elongation factor 1 alpha 2
, elongation factor 1-alpha 1
, elongation factor 1-alpha 2
, elongation factor-1 alpha
, eukaryotic elongation factor 1 A-2
, statin S1
, elongation factor 1 A-2
, elongation factor 1 A2
, Statin-like protein