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Elongation factor 1-alpha 1 (EF-1-alpha-1) (Elongation factor Tu) (EF-Tu) (Eukaryotic elongation factor 1 A-1) (eEF1A-1)

 EF1A1_MOUSE             Reviewed;         462 AA.
P10126; Q61511; Q6ZWN2; Q8BMB8; Q8BVS8; Q99KU5;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 3.
31-JAN-2018, entry version 194.
RecName: Full=Elongation factor 1-alpha 1;
Short=EF-1-alpha-1;
AltName: Full=Elongation factor Tu;
Short=EF-Tu;
AltName: Full=Eukaryotic elongation factor 1 A-1;
Short=eEF1A-1;
Name=Eef1a1; Synonyms=Eef1a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3215517; DOI=10.1016/0378-1119(88)90195-3;
Reddy N.S., Roth W.W., Bragg P.W., Wahba A.J.;
"Isolation and mapping of a gene for protein synthesis initiation
factor 4A and its expression during differentiation of murine
erythroleukemia cells.";
Gene 70:231-243(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2911475; DOI=10.1093/nar/17.1.442;
Lu X., Werner D.;
"The complete cDNA sequence of mouse elongation factor 1 alpha (EF 1
alpha) mRNA.";
Nucleic Acids Res. 17:442-442(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Head, Testis, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary tumor, and Olfactory epithelium;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108.
PubMed=3481036; DOI=10.1128/MCB.7.11.3929;
Roth W.W., Bragg P.W., Corrias M.V., Reddy N.S., Dholakia J.N.,
Wahba A.J.;
"Expression of a gene for mouse eucaryotic elongation factor Tu during
murine erythroleukemic cell differentiation.";
Mol. Cell. Biol. 7:3929-3936(1987).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-94.
PubMed=3960725; DOI=10.1093/nar/14.5.2409;
Rao T.R., Slobin L.I.;
"Structure of the amino-terminal end of mammalian elongation factor
Tu.";
Nucleic Acids Res. 14:2409-2409(1986).
[7]
PROTEIN SEQUENCE OF 6-30; 85-96; 135-146; 155-165; 248-290 AND
431-439, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 291-313 AND 372-376, AND ETHANOLAMINYLATION AT
GLU-301 AND GLU-374.
PubMed=2569467;
Whiteheart S.W., Shenbagarmurthi P., Chen L., Cotter R.J., Hart G.W.;
"Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally
modified by novel amide-linked ethanolamine-phosphoglycerol moieties.
Addition of ethanolamine-phosphoglycerol to specific glutamic acid
residues on EF-1 alpha.";
J. Biol. Chem. 264:14334-14341(1989).
[9]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH IFIT1, AND
SUBCELLULAR LOCATION.
PubMed=19856081; DOI=10.1007/s11010-009-0289-9;
Li H.T., Su Y.P., Cheng T.M., Xu J.M., Liao J., Chen J.C., Ji C.Y.,
Ai G.P., Wang J.P.;
"The interaction between interferon-induced protein with
tetratricopeptide repeats-1 and eukaryotic elongation factor-1A.";
Mol. Cell. Biochem. 337:101-110(2010).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165; LYS-172; LYS-273;
LYS-392 AND LYS-439, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-392,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[13]
METHYLATION AT LYS-165.
PubMed=28108655; DOI=10.1093/nar/gkx002;
Malecki J., Aileni V.K., Ho A.Y., Schwarz J., Moen A., Soerensen V.,
Nilges B.S., Jakobsson M.E., Leidel S.A., Falnes P.O.;
"The novel lysine specific methyltransferase METTL21B affects mRNA
translation through inducible and dynamic methylation of Lys-165 in
human eukaryotic elongation factor 1 alpha (eEF1A).";
Nucleic Acids Res. 45:4370-4389(2017).
-!- 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.
{ECO:0000250|UniProtKB:P68104}.
-!- SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran
and aminoacylated tRNA. Interacts with PARP1, TXK, XPO5 and KARS.
May interact with ERGIC2 (By similarity). Interacts with IFIT1
(via TPR repeats 4-7) (PubMed:19856081). Interacts with DLC1,
facilitating distribution to the membrane periphery and ruffles
upon growth factor stimulation. Interacts with ZPR1; the
interaction occurs in a epidermal growth factor (EGF)-dependent
manner (By similarity). Interacts with PPP1R16B (By similarity).
{ECO:0000250|UniProtKB:P68104, ECO:0000269|PubMed:19856081}.
-!- INTERACTION:
Q01534:TSPY1 (xeno); NbExp=5; IntAct=EBI-773865, EBI-1973142;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19856081}.
Nucleus {ECO:0000250|UniProtKB:P68104}. Nucleus, nucleolus
{ECO:0000250|UniProtKB:P68104}. Cell membrane
{ECO:0000250|UniProtKB:P68104}. Note=Colocalizes with DLC1 at
actin-rich regions in the cell periphery. Translocates together
with ZPR1 from the cytoplasm to the nucleus and nucleolus after
treatment with mitogens. Localization at the cell membrane depends
on EEF1A1 phosphorylation status and the presence of PPP1R16B.
{ECO:0000250|UniProtKB:P68104}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: Phosphorylated by TXK. Phosphorylation by PASK increases
translation efficiency. Phosphorylated by ROCK2.
{ECO:0000250|UniProtKB:P68104}.
-!- PTM: Trimethylated at Lys-79 by EEF1AKMT1 (By similarity).
Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is
dynamic as well as inducible by stress conditions, such as ER-
stress, and plays a regulatory role on mRNA translation
(PubMed:28108655). Trimethylated at Lys-318 by EEF1AKMT2 (By
similarity). {ECO:0000250|UniProtKB:P68104,
ECO:0000269|PubMed:28108655}.
-!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
subfamily. {ECO:0000305}.
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EMBL; M22432; AAA50406.1; -; mRNA.
EMBL; X13661; CAA31957.1; -; mRNA.
EMBL; AK032914; BAC28085.1; -; mRNA.
EMBL; AK076696; BAC36446.1; -; mRNA.
EMBL; AK081725; BAC38311.1; -; mRNA.
EMBL; AK083361; BAC38884.1; -; mRNA.
EMBL; BC004005; AAH04005.1; -; mRNA.
EMBL; BC004067; AAH04067.1; -; mRNA.
EMBL; BC005660; AAH05660.1; -; mRNA.
EMBL; BC018223; AAH18223.1; -; mRNA.
EMBL; BC018485; AAH18485.1; -; mRNA.
EMBL; BC083069; AAH83069.1; -; mRNA.
EMBL; M17878; AAA37538.1; -; Genomic_DNA.
EMBL; X03688; CAA27324.1; -; mRNA.
CCDS; CCDS40703.1; -.
PIR; S02114; EFMS1.
RefSeq; NP_034236.2; NM_010106.2.
UniGene; Mm.138471; -.
UniGene; Mm.335315; -.
UniGene; Mm.360075; -.
UniGene; Mm.391071; -.
UniGene; Mm.485669; -.
UniGene; Mm.491424; -.
ProteinModelPortal; P10126; -.
SMR; P10126; -.
BioGrid; 199385; 53.
DIP; DIP-46609N; -.
IntAct; P10126; 64.
MINT; MINT-1862449; -.
STRING; 10090.ENSMUSP00000042457; -.
iPTMnet; P10126; -.
PhosphoSitePlus; P10126; -.
SwissPalm; P10126; -.
SWISS-2DPAGE; P10126; -.
EPD; P10126; -.
PaxDb; P10126; -.
PeptideAtlas; P10126; -.
PRIDE; P10126; -.
TopDownProteomics; P10126; -.
Ensembl; ENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
GeneID; 13627; -.
KEGG; mmu:13627; -.
UCSC; uc009qun.1; mouse.
CTD; 1915; -.
MGI; MGI:1096881; Eef1a1.
eggNOG; KOG0052; Eukaryota.
eggNOG; COG5256; LUCA.
GeneTree; ENSGT00670000097815; -.
HOGENOM; HOG000229291; -.
HOVERGEN; HBG000179; -.
InParanoid; P10126; -.
KO; K03231; -.
OMA; PAKETKM; -.
OrthoDB; EOG091G05LW; -.
PhylomeDB; P10126; -.
TreeFam; TF300304; -.
PRO; PR:P10126; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000037742; -.
ExpressionAtlas; P10126; baseline and differential.
Genevisible; P10126; MM.
GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0032587; C:ruffle membrane; ISO:MGI.
GO; GO:0005516; F:calmodulin binding; IDA:CAFA.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
GO; GO:0000049; F:tRNA binding; ISO:MGI.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
HAMAP; MF_00118_A; EF_Tu_A; 1.
InterPro; IPR004161; EFTu-like_2.
InterPro; IPR031157; G_TR_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000795; TF_GTP-bd_dom.
InterPro; IPR009000; Transl_B-barrel_sf.
InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
Pfam; PF00009; GTP_EFTU; 1.
Pfam; PF03144; GTP_EFTU_D2; 1.
Pfam; PF03143; GTP_EFTU_D3; 1.
PRINTS; PR00315; ELONGATNFCT.
SUPFAM; SSF50447; SSF50447; 1.
SUPFAM; SSF50465; SSF50465; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00483; EF-1_alpha; 1.
PROSITE; PS00301; G_TR_1; 1.
PROSITE; PS51722; G_TR_2; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Elongation factor; GTP-binding; Membrane;
Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
Protein biosynthesis; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P68104}.
CHAIN 2 462 Elongation factor 1-alpha 1.
/FTId=PRO_0000090886.
DOMAIN 5 242 tr-type G.
NP_BIND 14 21 GTP. {ECO:0000250}.
NP_BIND 91 95 GTP. {ECO:0000250}.
NP_BIND 153 156 GTP. {ECO:0000250}.
REGION 14 21 G1. {ECO:0000250}.
REGION 70 74 G2. {ECO:0000250}.
REGION 91 94 G3. {ECO:0000250}.
REGION 153 156 G4. {ECO:0000250}.
REGION 194 196 G5. {ECO:0000250}.
MOD_RES 2 2 N,N,N-trimethylglycine.
{ECO:0000250|UniProtKB:P68104}.
MOD_RES 36 36 N6,N6,N6-trimethyllysine.
{ECO:0000250|UniProtKB:P68105}.
MOD_RES 55 55 N6,N6-dimethyllysine.
{ECO:0000250|UniProtKB:P68104}.
MOD_RES 79 79 N6,N6,N6-trimethyllysine; by EEF1AKMT1.
{ECO:0000250|UniProtKB:P68104}.
MOD_RES 165 165 N6,N6,N6-trimethyllysine; alternate; by
EEF1AKMT3. {ECO:0000269|PubMed:28108655}.
MOD_RES 165 165 N6,N6-dimethyllysine; alternate; by
EEF1AKMT3.
{ECO:0000250|UniProtKB:P68104}.
MOD_RES 165 165 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 165 165 N6-methyllysine; alternate; by EEF1AKMT3.
{ECO:0000250|UniProtKB:P68104}.
MOD_RES 172 172 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000250|UniProtKB:P62632}.
MOD_RES 273 273 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 300 300 Phosphoserine; by TGFBR1.
{ECO:0000250|UniProtKB:P68104}.
MOD_RES 301 301 5-glutamyl
glycerylphosphorylethanolamine.
{ECO:0000269|PubMed:2569467}.
MOD_RES 318 318 N6,N6,N6-trimethyllysine; by EEF1AKMT2.
{ECO:0000250|UniProtKB:P68104}.
MOD_RES 374 374 5-glutamyl
glycerylphosphorylethanolamine.
{ECO:0000269|PubMed:2569467}.
MOD_RES 392 392 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 392 392 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 432 432 Phosphothreonine; by PASK.
{ECO:0000250|UniProtKB:P68104}.
MOD_RES 439 439 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
CONFLICT 7 7 H -> R (in Ref. 5; AAA37538).
{ECO:0000305}.
CONFLICT 15 15 H -> L (in Ref. 5; AAA37538).
{ECO:0000305}.
CONFLICT 23 23 T -> S (in Ref. 5; AAA37538).
{ECO:0000305}.
CONFLICT 77 78 LW -> QR (in Ref. 2; CAA31957).
{ECO:0000305}.
CONFLICT 83 83 S -> A (in Ref. 6; CAA27324).
{ECO:0000305}.
CONFLICT 91 92 DA -> ES (in Ref. 2; CAA31957).
{ECO:0000305}.
CONFLICT 108 108 Q -> R (in Ref. 5; AAA37538).
{ECO:0000305}.
CONFLICT 156 156 D -> G (in Ref. 3; BAC28085).
{ECO:0000305}.
CONFLICT 222 222 S -> H (in Ref. 1; AAA50406).
{ECO:0000305}.
CONFLICT 224 226 SGT -> VAP (in Ref. 2; CAA31957).
{ECO:0000305}.
CONFLICT 225 225 G -> D (in Ref. 4; AAH04005).
{ECO:0000305}.
CONFLICT 239 239 Missing (in Ref. 2; CAA31957).
{ECO:0000305}.
CONFLICT 350 350 P -> T (in Ref. 3; BAC36446).
{ECO:0000305}.
SEQUENCE 462 AA; 50114 MW; 71072871DE7405DC CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK
IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GSASGTTLLE ALDCILPPTR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS
EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV
LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP
LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK


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EIAAB12473 Eef1a2,eEF1A-2,Eef1al,EF-1-alpha-2,Elongation factor 1-alpha 2,Eukaryotic elongation factor 1 A-2,Rat,Rattus norvegicus,Statin-S1,Stn,Stnl
EIAAB12474 EEF1A2,eEF1A-2,EF-1-alpha-2,Elongation factor 1-alpha 2,Eukaryotic elongation factor 1 A-2,Oryctolagus cuniculus,Rabbit,Statin-S1
EIAAB12477 Eef1a2,eEF1A-2,Eef1al,EF-1-alpha-2,Elongation factor 1-alpha 2,Eukaryotic elongation factor 1 A-2,Mouse,Mus musculus,Statin-S1,Stn
EIAAB12476 Bos taurus,Bovine,EEF1A2,eEF1A-2,EF-1-alpha-2,Elongation factor 1-alpha 2,Eukaryotic elongation factor 1 A-2
AS10 934 rabbit polyclonal eEF1a elongation factor | elongation factor 1-alpha 200
10-288-22158F Elongation factor 1-alpha 2 - EF-1-alpha-2; Elongation factor 1 A-2; eEF1A-2; Statin S1 0.05 mg
10-288-22158F Elongation factor 1-alpha 2 - EF-1-alpha-2; Elongation factor 1 A-2; eEF1A-2; Statin S1 0.1 mg
EIAAB12467 Chicken,EEF1A,EF-1-alpha-1,EF-Tu,Elongation factor 1-alpha 1,Elongation factor Tu,Gallus gallus
EIAAB37799 Eefsec,Elongation factor sec,Eukaryotic elongation factor, selenocysteine-tRNA-specific,Mouse,mSelB,Mus musculus,Selb,Selenocysteine-specific elongation factor
EIAAB37798 EEFSEC,Elongation factor sec,Eukaryotic elongation factor, selenocysteine-tRNA-specific,Homo sapiens,Human,SELB,Selenocysteine-specific elongation factor
EIAAB12537 EFG,EFG1,EF-Gmt,Elongation factor G 1, mitochondrial,Elongation factor G, mitochondrial,Elongation factor G1,GFM,GFM1,hEFG1,Homo sapiens,Human,mEF-G 1
EIAAB12504 Calcium_calmodulin-dependent eukaryotic elongation factor 2 kinase,eEF-2 kinase,EEF2K,eEF-2K,Eukaryotic elongation factor 2 kinase,Homo sapiens,Human
EIAAB12536 Efg,Efg1,EF-Gmt,Elongation factor G 1, mitochondrial,Elongation factor G, mitochondrial,Elongation factor G1,Gfm,Gfm1,mEF-G 1,Mouse,Mus musculus
EIAAB12535 Efg,Efg1,EF-Gmt,Elongation factor G 1, mitochondrial,Elongation factor G, mitochondrial,Elongation factor G1,Gfm,Gfm1,mEF-G 1,Rat,Rattus norvegicus
EIAAB12503 Calcium_calmodulin-dependent eukaryotic elongation factor 2 kinase,eEF-2 kinase,Eef2k,eEF-2K,Eukaryotic elongation factor 2 kinase,Mouse,Mus musculus
EIAAB12505 Calcium_calmodulin-dependent eukaryotic elongation factor 2 kinase,eEF-2 kinase,Eef2k,eEF-2K,Eukaryotic elongation factor 2 kinase,Rat,Rattus norvegicus
EIAAB41685 Homo sapiens,Human,TCEA2,Testis-specific S-II,Transcription elongation factor A protein 2,Transcription elongation factor S-II protein 2,Transcription elongation factor TFIIS.l
20-372-60109 transcription elongation factor A (SII). 1 - Mouse monoclonal anti-human TCEA1 antibody; Transcription elongation factor S-II protein 1; Transcription elongation factor TFIIS.o Monoclonal 0.1 mg


 

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