Recombinant Human Eukaryotic elongation factor 2 kinase (EEF2K)

Code CSB-YP007435HU
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Source Yeast
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Code CSB-EP007435HU
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Source E.coli
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Code CSB-EP007435HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP007435HU
MSDS
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Source Baculovirus
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Code CSB-MP007435HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
EEF2K
Uniprot No.
Alternative Names
C86191; Calcium/calmodulin dependent eukaryotic elongation factor 2; Calcium/calmodulin dependent eukaryotic elongation factor 2 kinase; Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase; Calmodulin dependent protein kinase III; cb365; EC 2.7.11.20; eEF 2 kinase; eEF 2K ; eEF-2 kinase; eEF-2K; Eef2k; EEF2K protein; EF2K_HUMAN; Elongation factor 2 kinase; Eukaryotic elongation factor 2 kinase; fa04b08; HSU93850; kinase eEF2K; MGC45041; SMEF2K; wu:fa04b08; zgc:100973
Species
Homo sapiens (Human)
Expression Region
1-725
Target Protein Sequence
MADEDLIFRL EGVDGGQSPR AGHDGDSDGD SDDEEGYFIC PITDDPSSNQ NVNSKVNKYY SNLTKSERYS SSGSPANSFH FKEAWKHAIQ KAKHMPDPWA EFHLEDIATE RATRHRYNAV TGEWLDDEVL IKMASQPFGR GAMRECFRTK KLSNFLHAQQ WKGASNYVAK RYIEPVDRDV YFEDVRLQME AKLWGEEYNR HKPPKQVDIM QMCIIELKDR PGKPLFHLEH YIEGKYIKYN SNSGFVRDDN IRLTPQAFSH FTFERSGHQL IVVDIQGVGD LYTDPQIHTE TGTDFGDGNL GVRGMALFFY SHACNRICES MGLAPFDLSP RERDAVNQNT KLLQSAKTIL RGTEEKCGSP QVRTLSGSRP PLLRPLSENS GDENMSDVTF DSLPSSPSSA TPHSQKLDHL HWPVFSDLDN MASRDHDHLD NHRESENSGD SGYPSEKRGE LDDPEPREHG HSYSNRKYES DEDSLGSSGR VCVEKWNLLN SSRLHLPRAS AVALEVQRLN ALDLEKKIGK SILGKVHLAM VRYHEGGRFC EKGEEWDQES AVFHLEHAAN LGELEAIVGL GLMYSQLPHH ILADVSLKET EENKTKGFDY LLKAAEAGDR QSMILVARAF DSGQNLSPDR CQDWLEALHW YNTALEMTDC DEGGEYDGMQ DEPRYMMLAR EAEMLFTGGY GLEKDPQRSG DLYTQAAEAA MEAMKGRLAN QYYQKAEEAW AQMEE
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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 before Lyophilization
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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°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
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced.
Gene References into Functions
  1. that eukaryotic elongation factor 2 kinase might inhibit TGF-beta1-induced normal lung fibroblast (NHLF) proliferation and differentiation and activate NHLF cell apoptosis and autophagy through p38 MAPK signaling PMID: 29355493
  2. Our study provides first evidence that TQ treatment inhibits cell proliferation, migration/invasion, and tumor growth, in part through the inhibition of eEF-2K signaling in Triple-negative breast cancer (TNBC) . Thus, our findings suggest that systemic TQ treatment may be used as a targeted therapeutic strategy for the inhibition of eEF-2K in TNBC tumor growth and progression. PMID: 29971628
  3. The mechanism for Fluoxetine-induced autophagic cell death was associated with inhibition of eEF2K and activation of AMPK-mTOR-ULK complex axis. PMID: 29094413
  4. This study provides new insights into the control of eEF2K by AMPK. PMID: 28502587
  5. Data suggest forkhead box M1 (FOXM1)/eukaryotic elongation factor 2 kinase (eEF2K) axis as a molecular target in breast and other cancers. PMID: 26918606
  6. These new substrates suggest that eEF2K has a more diverse role in regulating cellular energy usage that involves multiple pathways and regulatory feedback. PMID: 27760376
  7. Myostatin inhibits eEF2K-eEF2 by regulating AMPK to suppress protein synthesis. PMID: 29024627
  8. The structural basis for the recognition of EEF2K by calmodulin has been presented. PMID: 27499441
  9. eEF2K activity is increased in postmortem Alzheimer's disease (AD) patient cortex and hippocampus, and in the hippocampus of aged transgenic AD mice. eEF2K inhibition using pharmacological or genetic approaches prevented the toxic effects of Abeta42 oligomers on neuronal viability and dendrite formation in vitro. Findings highlight the potential utility of eEF2K inhibition to reduce Abeta-mediated oxidative stress in AD. PMID: 27752775
  10. Results demonstrated that the promotive effect of eEF-2K on glycolysis resulted from the kinase-mediated restriction of synthesis of the protein phosphatase 2A-A (PP2A-A). PMID: 27181208
  11. This study reports how phosphorylation of a regulatory site (Ser-500) integrates with Ca(2+) and CaM to influence eEF-2K activity. PMID: 27956550
  12. Article reviews recent evidence concerning the role of eEF2K in human diseases; growing evidence links eEF2K to a range of human diseases, including cardiovascular conditions (atherosclerosis, via macrophage survival) and pulmonary arterial hypertension, as well as solid tumors, where eEF2K appears to play contrasting roles depending on tumor type and stage. eEF2K is also involved in neurological disorders. [Review] PMID: 26806303
  13. Recent evidence shows that eEF2K plays an important role in learning and memory, processes that require the synthesis of new proteins and involve Ca-mediated signalling. eEF2K is activated under conditions of nutrient and energy depletion PMID: 26009171
  14. Results show that eEF2K is rapidly activated in response to acidosis in cells, an effect that is followed by its downregulation. PMID: 25776553
  15. silencing of EEF2K promotes autophagic survival via activation of the AMPK-ULK1 pathway in colon cancer cells PMID: 24955726
  16. Deletion of Pten and p53 in mammary epithelium accelerates triple-negative breast cancer with dependency on eEF2K activity. PMID: 25330770
  17. Data show that eEF2K is activated during hypoxia or upon inhibition of prolyl hydroxylases and inhibited by its hydroxylation on a highly conserved proline residue, restricting its activity during normoxia. PMID: 25755286
  18. our results show, for the first time, that eEF-2K is involved in regulation of the invasive phenotype of PaCa cells through promoting a new signalling pathway, which is mediated by TG2/b1 integrin/Src/uPAR/MMP-2 PMID: 25215932
  19. data suggest that achieving an active conformation, rather than eEF2K activity per se, is required for its susceptibility to degradation. PMID: 25670349
  20. data show that the major trigger for activation of eEF2K upon mild cooling is the release of Ca2+ ions from the endoplasmic reticulum (ER) PMID: 25353634
  21. mTORC1 pathway and the oncogenic Ras/Raf/MEK/extracellular signal-regulated kinase (ERK) pathway cooperate to restrict eEF2K activity. PMID: 25182533
  22. eEF-2K activation appears to be analogous to an amplifier, where output volume may be controlled by either toggling the power switch or altering the volume control PMID: 25012662
  23. The roles of specific residues, selected on the basis of structural data for MHCK A and TRPM7, in the function of eEF2K, is studied. PMID: 24732796
  24. down-regulation of eEF-2K leads to induction of intrinsic, extrinsic as well as AIF-dependent apoptosis. PMID: 24193916
  25. Eukaryotic elongation factor 2 kinase regulates the development of hypertension through oxidative stress-dependent vascular inflammation. PMID: 23812389
  26. Data highlight a conserved role for eEF2K in protecting cells from nutrient deprivation and in conferring tumor cell adaptation to metabolic stress. PMID: 23706743
  27. the disruption of eEF-2K expression in breast cancer cells results in the down-regulation of signaling pathways affecting growth, survival and resistance and has potential as a therapeutic approach for the treatment of breast cancer. PMID: 22911754
  28. EEF2 phosphorylation by cyclin A-cyclin-dependent kinase 2 (CDK2) on a novel site, serine 595 (S595), directly regulates T56 phosphorylation by eEF2K. PMID: 23184662
  29. eEF-2 kinase fills critical niches in the life of a cancer cell and the eEF-2/eEF-2 kinase pathway is a key biochemical sensor. PMID: 22932089
  30. Burn induces prolonged activation of eEF2K and eEF2 in pediatric patients. PMID: 22269896
  31. These data indicate that eEF-2K is regulated at multiple levels with phosphorylation playing a critical role in the enzyme's turnover under stressful conditions. PMID: 22749997
  32. several autophosphorylation sites, including Thr(348), Thr(353), Ser(366) and Ser(445), all of which are highly conserved among vertebrate PMID: 22216903
  33. Phosphorylation of Ser-500 lags behind the phosphorylation of Thr-348 and is associated with the Ca(2+)-independent activity of eEF-2K(eEF-2K) PMID: 22329831
  34. highly conserved residues in the C-terminal tip of eEF2K are essential for the phosphorylation of eEF2 PMID: 22115317
  35. results suggest that the expression of eEF-2 kinase contributes to migration and invasion of human glioma cells by protecting them from anoikis. PMID: 21278783
  36. activation of eEF-2 kinase-mediated autophagy plays a protective role for cancer cells under metabolic stress conditions PMID: 20300520
  37. our results suggest that anisomycin or TNF-alpha inhibit eEF2 kinase via the phosphorylation of Ser-359. PMID: 12171600
  38. AMPK and eEF2 kinase may provide a key link between cellular energy status and the inhibition of protein synthesis, a major consumer of metabolic energy PMID: 14709557
  39. Results show that eukaryotic elongation factor 2 kinase is a target for mTOR signaling independently of previously known downstream components of the pathway. PMID: 15024086
  40. Levels of p-eEF2K were significantly increased, and total eEF2 significantly decreased in Alzheimer disease PMID: 16098202
  41. These results suggest that eEF-2 kinase plays a regulatory role in the autophagic process in tumor cells and may promote cancer cell survival under conditions of nutrient deprivation. PMID: 16921268
  42. These data closely match the control of Ser359 phosphorylation and indicate that cdc2 may be regulated by mTORC1. PMID: 18337751
  43. The target cells (HGC-27) expressed EF-2K and MHC-class I together with costimulatory molecules from heat stress. This antigen specific immune mechanism could have a prominent role in the pathogenesis of gastric ulcer. PMID: 19636416

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Protein Families
Protein kinase superfamily, Alpha-type protein kinase family
Database Links

HGNC: 24615

OMIM: 606968

KEGG: hsa:101930123

STRING: 9606.ENSP00000263026

UniGene: Hs.498892

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