Recombinant Human Elongation factor 1-alpha 1(EEF1A1)

Code CSB-EP007409HU
Size US$1726
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP007409HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) EEF1A1.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP007409HU could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) EEF1A1.
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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names EEF1A1
Uniprot No. P68104
Research Area Epigenetics and Nuclear Signaling
Alternative Names CCS 3; CCS3; Cervical cancer suppressor 3; chunp6927; CTCL tumor antigen; EE1A1; EEF 1; EEF1A; eEF1A-1; EEF1A1; EF-1-alpha-1; EF-Tu; EF1A; EF1a like protein; EF1A1_HUMAN; Elongation factor 1 alpha subunit; Elongation factor 1-alpha 1; Elongation factor Tu; Eukaryotic elongation factor 1 A-1; Eukaryotic translation elongation factor 1 alpha 1; Eukaryotic translation elongation factor 1 alpha 1 like 14; Glucocorticoid receptor AF 1 specific elongation factor; GRAF 1EF; HNGC:16303; ik:tdsubc_2a3; ik:tdsubc_2b3; LENG7; Leukocyte receptor cluster (LRC) member 7; Leukocyte receptor cluster member 7; Prostate tumor inducing protein 1; PTI1; tdsubc_2a3; Translation elongation factor 1 alpha 1 like 14; wu:fa91c07; wu:fa94b03; wu:fi13b09; xx:tdsubc_2a3; xx:tdsubc_2b3
Species Homo sapiens (Human)
Source E.coli
Expression Region 1-462aa
Target Protein Sequence MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 66.1kDa
Protein Length Full Length
Tag Info N-terminal 6xHis-SUMO-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Basically, we can dispatch the products out in 3-7 working days after receiving your orders. Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production.
Gene References into Functions
  1. The functional studies of specific methylation sites found them to have distinct effects, notably on Eukaryotic elongation factor 1A (eEF1A)-related processes of translation and tRNA aminoacylation. PMID: 29398204
  2. A strong correlation was found between the dysregulation of eEF1A synthesis and Alzheimer's Disease-associated synaptic failure. PMID: 27567813
  3. the different kinases that recognize the Ser and Thr residues of the eEF1A1 and eEF1A2 isoforms and regulate their involvement in different cellular processes like cell survival and apoptosis. PMID: 27568183
  4. Taken together, these findings enabled us to identify a novel mechanism by which eEF1A1 regulates the cell cycle's G1 phase to promote tumor proliferation by regulating cyclin D1 expression through STAT1 signaling in HCC. PMID: 29079187
  5. Methylation of lysine (K36) in eukaryotic elongation factor alpha (eEF1A) proteins is dependent on EEF1A lysine methyltransferase 4 (eEF1A-KMT4) in vivo. PMID: 28520920
  6. The present study identifies METTL21B as the enzyme responsible for methylation of eEF1A on Lys-165 and shows that this modification is dynamic, inducible and likely of regulatory importance. PMID: 28108655
  7. EEF1A1 is somatically mutated in 9% of follicular lymphoma tumors. PMID: 25713363
  8. we show how FAT10 stabilizes the translation elongation factor eEF1A1, which contributes to cancer cell proliferation PMID: 27312528
  9. The expression of RPL13A and EEF1A1 was not affected by differentiation, thus being these genes the most stable candidates as reference genes for RT-PCR. PMID: 27304673
  10. Study demonstrated that PAK4 interacted with eEF1A1 to promote migration and invasion of gastric cancer cells, thereby providing new insights into the function of PAK4 and eEF1A1 in the progression of gastric cancer. PMID: 28393218
  11. this study demonstrates that eEF1A1 regulates the subcellular location of expanded poly(A) proteins and is therefore a potential therapeutic target for combating the pathogenesis of poly(A) diseases. PMID: 28246169
  12. analysis of eEF1A1 oligomerization reveals that specific cysteine residues are required for this oligomerization activity PMID: 26515794
  13. Data (including data from studies using purified proteins/hepatocyte lysates) suggest eEF1A1/Sgt1a interact as multimer; D2/D3 domains of eEF1A1 and TPR domain of Sgt1 are involved in multimer formation; Sgt1 competes with viral RNA to bind to eEF1A. PMID: 26545799
  14. Data indicate that the methylation of lysine (Lys) in elongation factor 1A (eEF1A) by methyltransferase is conserved from yeast to human. PMID: 26545399
  15. ROCK phosphorylated eEF1A1 is a novel substrate for TIMAP-PP1 underlining the complex regulatory role of TIMAP in the endothelium. PMID: 26497934
  16. Study found reduced levels of hippocampal eEF1A protein in Alzheimer's disease PMID: 26551858
  17. Our results provide novel information on the intracellular distribution and interaction of eEF1A isoforms. PMID: 26212729
  18. These results suggest that the antitumor effects of paclitaxel in breast cancer are mediated by activation of the AMPK/EF1alpha/FOXO3a signaling pathway. PMID: 26397839
  19. These results suggest that miR-33a-5p is downregulated during Japanese encephalitis virus infection, which contributes to viral replication by increasing the intracellular level of EEF1A1, an interaction partner of the viral NS3 and NS5 proteins. PMID: 26819305
  20. Low expression of eEF1A1 was associated with cervical squamous cell carcinoma. PMID: 25893434
  21. eEF1A-1 protein was induced by high palmitate, and partially re-localized from its predominant location at the ER to polymerized actin at the cell periphery, coinciding with the onset of ER stress. PMID: 26102086
  22. The combined evidence indicates a direct interaction between eEF1A and reverse transcriptase is crucial for HIV reverse transcription and replication PMID: 26624286
  23. eEF1A interacts with 5'UTR of HIV-1 genomic RNA and the interaction is important for late DNA synthesis in reverse transcription. PMID: 26242867
  24. Data show that translation elongation factor eEF1A1 coordinates the heat shock response by adjusting transcriptional yield to translational needs. PMID: 25233275
  25. EEF1A1, SSRP1, and XRCC6 are novel interacting partners of the mineralocorticoid receptor PMID: 25000480
  26. eEF1A1 may mediate SAMHD1 turnover by targeting it to the proteosome for degradation through association with Cullin4A and Rbx1. PMID: 25423367
  27. protein expressions of stathmin and EF1alpha were found in DNs of precancerous lesions, whereas they were absent or present at very low levels in normal liver and liver cirrhosis PMID: 24885363
  28. These data provide the experimental evidence that telomere shortening and related inflammatory proteins are associated with human IgAN, and it could be a new direction for the disease progression study. PMID: 24903994
  29. findings suggest that eEF1A contributes to the morphology of postsynaptic membrane specializations at inhibitory synapses PMID: 23839781
  30. Sequence differences in the EF1alpha -3 promoter likely account for the activity differences seen. Investigators need to recognize that all promoters of the same name may not be equivalent in driving transgene expression. PMID: 24688302
  31. Describes a nuclear role for eEF1A and provide a mechanism for protein nuclear export that attenuates the activity of SNAG-containing transcription factors PMID: 24209753
  32. results reveal a novel molecular mechanism for a non-canonical role of eEF1A1 in signal transduction via direct modulation of kinase-dependent phosphorylation events PMID: 24487064
  33. Human eEF1A1 is a negative regulator of the pro-apoptotic function of p53 and p73 PMID: 23799104
  34. We propose that the reduction in SphK1 activity late in DENV-2-infected cells is a consequence of DENV-2 out-competing SphK1 for eEF1A binding and hijacking cellular eEF1A for its own replication strategy. PMID: 23939980
  35. Knocking down eEF1A1 gene has noticeable effects on the proliferation inhibition and apoptosis induction of Jurkat cells. PMID: 22931638
  36. eEF1A binds defective polypeptides released from ribosomes, which generates a signal that triggers aggresome formation. PMID: 22357952
  37. This study identified eEF1A1 as a FAT10-specific binding protein, and when the expression of FAT10 was reduced by siRNA knockdown, this resulted in downregulation of eEF1A1 expression in hepatoma cells. PMID: 22569823
  38. Overexpression of eukaryotic translation elongation factor 1 alpha 1 is associated with nonepithelial ovarian cancer. PMID: 22531302
  39. Results show a new function of eEF1A that contributes to cell regulation, including anoikis. PMID: 22399298
  40. In Huh-7 hepatoma cells, the hepatitis B virus X protein inhibits dimer formation of eEF1A1, hence blocks filamentous actin bundling. PMID: 22499008
  41. High eEF1A1 is associated with metastatic progression of prostate cancer. PMID: 22355332
  42. An immunoreactive protein detected in sera from 21 of 40 infiltrating ductal breast carcinoma patients was isolated and subsequently identified as elongation factor-Tu. PMID: 21704614
  43. Mammalian PUM2-Ago-eEF1A inhibited translation of nonadenylated and polyadenylated reporter mRNAs in vitro. PMID: 22231398
  44. Pilot evaluation in archive prostate tissues showed the presence of EEF1A2 mRNA in near all neoplastic and perineoplastic but not in normal samples or in benign adenoma; in contrast, EEF1A1 mRNA was everywhere detectable PMID: 22095224
  45. A co-localization of SORBS2 and eEF1A was evidenced at level of plasma membrane, thus suggesting the involvement of eEF1A1 in novel key signal transduction complexes. PMID: 21689717
  46. study defines the mechanism regulating eEF1A-mediated SK1 activation, and also establishes SK1 as being integral for PTI-1-induced oncogenesis PMID: 20838377
  47. These findings provide evidence that elongation factor-1 alpha correlates closely with the survival of patients with prostate cancer and may be a novel prognostic factor. PMID: 20545466
  48. Phosphorylation of eEF1A1 by TbetaR-I is a novel regulatory mechanism that provides a direct link to regulation of protein synthesis by TGF-beta, as an important component in the TGF-beta-dependent regulation of protein synthesis and cell proliferation PMID: 20832312
  49. Data show that EF1alpha, RPL13a and YWHAZ are suitable genes for the RT-qPCR analysis and comparison of several sources of human MSC during in vitro characterization and differentiation as well as in an ex vivo animal model of global cerebral ischemia. PMID: 20716364
  50. Proteomics was used to study colonic epithelial aging, for differential proteins in the human normal colonic epithelial tissues from young and old people. Rack1, EF-Tu and Rhodanese, three validated differential proteins, were further investigated. PMID: 20099848
  51. The structures of LppGT/LplGT (lpg1368 and lpl1319) reveal three domains and suggest that a positively charged EF1A loop binds to a negatively charged groove on the LpGT structure, and that two asparagine residues are essential for catalysis. PMID: 20030628
  52. Eukaryotic elongation factor 1A (eEF1A) and tRNA are RanGTP-dependent binding partners of exportin-5 (Exp5). Exp5 stimulates nuclear export of eEF1A and tRNA. PMID: 12426393
  53. The fragile X mental retardation protein FMRP binds elongation factor 1A mRNA and negatively regulates its translation in vivo. PMID: 12594214
  54. TCTP preferentially stabilized the GDP form of eEF1A, and, furthermore, impaired the GDP exchange reaction promoted by eEF1Bbeta. PMID: 14623968
  55. analysis of the relationships between EF-Ts and EF-Tu from both yeasts and humans through functional complementation and coexpression experiments PMID: 15695360
  56. The potential roles of the PTI-1 protein in carcinogenesis and the origin of the PTI-1 gene in the human genome are discussed. PMID: 15716006
  57. Our results indicate that neither EEF1A1 nor IMPG1 could be responsible for RP25 in the studied families due to absence of any pathogenic variants. PMID: 16354621
  58. The cytotoxicity of G-rich GT oligomers was shown to be tightly related to their binding affinity for eEF1A protein. PMID: 16689924
  59. potential tumor suppressor activity of CCS-3 may be mediated by its interaction with PLZF. PMID: 16828757
  60. The interaction between eEF-1A and C-Raf increases eEF-1A stability and induces a survival activity. PMID: 17332776
  61. Endogenous HDM2- EF1alpha complex was detected in cancer cells overexpressing HDM2, suggesting a possible role of this interaction in HDM2-mediated oncogenesis. PMID: 17373842
  62. identified the multifunctional eukaryotic translation elongation factor eEF1A1 as a novel interaction partner of PASKIN in the nuclei of testis germ cells and in the midpiece of sperm tails PMID: 17595531
  63. The expression level of EEF1A1 correlates with cell growth but not apoptosis in hepatocellular carcinoma cell lines with different differentiation grades. PMID: 17825975
  64. Up-regulation of muscle EEF1A1 relates to proteolysis rate, suggesting an involvement of this gene in muscle catabolic response in hypercatabolic traumatized patients. PMID: 17998013
  65. both eEF1A and MYPT1 have roles in EGCG signaling for cancer prevention through 67LR PMID: 18079119
  66. The ability of eEF1A1 rather than eEF1A2 to interact with calmodulin is predicted by MD analysis and showed experimentally. PMID: 18221514
  67. a novel mechanism of regulation of both SK1 and SK2 that is mediated by their interaction with eEF1A. PMID: 18263879
  68. These results indicate that the novel gene AngRem104 is involved in the in vivo regulation of GR expression and the activation of NF-kappaB through interaction with GR-EF in human MCs. PMID: 18331827
  69. It was demonstrated that the N protein of SARS-CoV induces aggregation of EF1, inhibiting protein translation and cytokinesis by blocking F-actin bundling. PMID: 18448518
  70. BPOZ-2 promoted eEF1A1 ubiquitylation and degradation, suggesting that eEF1A1 is a substrate of BPOZ-2. PMID: 18459963
  71. eEF1A1 is a novel endothelial nitric oxide synthase 3'-untranslated region binding protein that plays a critical role in mediating tumor necrosis factor (TNF)-alpha-induced decrease in eNOS mRNA stability. PMID: 18688046
  72. The cell death was associated with downregulation of eukaryotic translation elongation factor-1 alpha 1 (eEF1A1/EF-1alpha) expression in conjunction with accumulation of its mRNA in processing bodies (P bodies). PMID: 18820646
  73. PTI-1 presence parallels Mycoplasma infection suggesting that PTI-1 might not necessarily play a major role in the onset of prostate tumorigenesis. PMID: 18853312
  74. EF1A1 regulation of OPN mRNA stability is actin dependent. EF1A1 is a regulatory factor in OPN expression in cancer. PMID: 19026636
  75. This finding reveals a novel contribution of the SAM-EF1A1 interaction as a potentially important GAP-independent modulation of cell migration by DLC1. PMID: 19158340
  76. confirm the interactions of eEF1A1, p54(nrb), hnRNP-L, GAPDH and ASF/SF2 with the right terminal stem-loop domain of HDV genomic RNA in vitro PMID: 19464723
  77. The molecular interaction between the co-repressors and CCS-3 at the POZ-domain of ZBTB7A protein appears to enhance ZBTB7A protein mediated transcriptional repression. PMID: 19471103
  78. The decapeptide 50GKGSFKYAWV59 of eukaryotic elongation factor 1A is efficiently modified by Legionella pneumophila glucosyltransferase Lgt1. PMID: 19478083
  79. These findings suggest that the interaction between LRRK2 and EF1A may reciprocally modulate their physiological function. PMID: 19559761
  80. created and validated comparative three-dimensional (3-D) models of eEF1A1 and eEF1A2 on the basis of the crystal structure of homologous eEF1A from yeast PMID: 19636410

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Subcellular Location Cytoplasm, Nucleus, Nucleus, nucleolus, Cell membrane
Protein Families TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily
Tissue Specificity Brain, placenta, lung, liver, kidney, pancreas but barely detectable in heart and skeletal muscle.
Database Links

HGNC: 3189

OMIM: 130590

KEGG: hsa:1915

STRING: 9606.ENSP00000330054

UniGene: Hs.535192

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