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Recombinant Rat Elongation factor 2 (Eef2), partial

Recombinant Rat Elongation factor 2 (Eef2), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

Eef2

Uniprot NO.

P05197

Alternative Names

Eef2Elongation factor 2; EF-2

Species

Rattus norvegicus (Rat)

Source

Yeast

Expression Region

2-858

Target Protein Sequence

VNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR AGETRFTDTR KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGSGFLI NLIDSPGHVD FSSEVTAALR VTDGALVVVD CVSGVCVQTE TVLRQAIAER IKPVLMMNKM DRALLELQLE PEELYQTFQR IVENVNVIIS TYGEGESGPM GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG EGQLGAAERA KKVEDMMKKL WGDRYFDPAN GKFSKSANSP DGKKLPRTFC QLILDPIFKV FDAIMNFRKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL LQMITIHLPS PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK MVPTSDKGRF YAFGRVFSGV VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV KTGTITTFEH AHNMRVMKFS VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE SGEHIIAGAG ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN RLYMKARPFP DGLAEDIDKG EVSARQELKA RARYLAEKYE WDVAEARKIW CFGPDGTGPN ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV RFDVHDVTLH ADAIHRGGGQ IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ CPEQVVGGIY GVLNRKRGHV FEESQVAGTP MFVVKAYLPV NESFGFTADL RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK RKGLKEGIPA LDNFLDKL
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
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.

Storage Condition

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

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.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. 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. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

Gene References into Functions

The results suggest that one of the possible mechanisms underlying pineal gland dysfunction during aging is the effect of lipid peroxidation on eEF-2, which is a key component of protein synthesis machinery. PMID:27292877
Eukaryotic elongation factor 2 kinase activation in M. soleus under 14-day hindlimb unloading of rats PMID:28726101
Translational inhibition by CORM-2 is a result of eEF2 phosphorylation due to inhibition of PI3K-Akt-mTOR signaling. PMID:23041477
melatonin prevented the molecular changes in eEF-2 and the decline in protein synthesis rate secondary to lipid peroxidation. PMID:22462727
oxidative stress could be involved in the alterations of eEF-2, which forms adducts with malondialdehyde and 4-hydroxynonenal in the aging hypothalamo-hypophyseal system PMID:21172375
Report interleukin-1beta as the first known activator of endogenous ADP-ribosylation of eEF-2. PMID:21088871
results show a causal link between synaptic activity and dendritic spine morphology in rat hippocampal neurons; propose that the eEF2K/eEF2 pathway is a key biochemical sensor that couple neuronal activity to spine plasticity PMID:20427644
These results indicate that eEF2 behaves differently from prokaryotic EF-G in binding to ribosomal RNA. PMID:11849993
effects of ATP depletion on the phosphorylation of eEF2 in adult rat ventricular cardiomyocytes PMID:12435591
phosphorylation/dephosphorylation of EF-2 is regulated by glucose by a protein phosphatase-2A-dependent mechanism in rat cells PMID:12644453
association of p53 with eEF2 and 5.8S rRNA, and the effect of p53 on sensitivity to the translocation inhibitor, Cx, as well as the known molecular interactions of these components in the ribosome suggest involvement of p53 in elongation PMID:12891704
increasing workload resulted in dephosphorylation of eEF2, which was rapamycin-insensitive, while eEF2K activity was unchanged, suggesting that the decrease in eEF2 phosphorylation could result from the activation of an eEF2 phosphatase PMID:12920134
Translation elongation in pancreatic acinar cells is likely regulated by eEF2 through the mTOR, p38, and MEK pathways, and modulated through PP2A PMID:15158453
eEF2 was dephosphorylated after transient cerebral ischemia in rats with and without ischemic tolerance or H2O2-treated cells; however, protein synthesis was significantly inhibited under these three conditions. PMID:15211596
These results suggest that the regulation of L6 myoblast differentiation by PI3-kinase is related to eEF2 phosphorylation. PMID:16682826
EF-2 fragment was a possible candidate for the protein responsible for the radiation adaptive response in cultured astrocytes. PMID:17522089
results attest to the presence of ADP-ribosylation site on 32F at the C-terminal half of eEF-2 PMID:17665640
AMPK activation attenuates eEF2 response to high-frequency electrically stimulated skeletal muscle contractions. PMID:18187610