Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Transcription factor E2F8 (E2F-8)

 E2F8_HUMAN              Reviewed;         867 AA.
A0AVK6; A8K9H3; Q2VPJ3; Q3C1U6; Q5BKY4; Q8N340; Q9H5M0;
21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 1.
25-OCT-2017, entry version 107.
RecName: Full=Transcription factor E2F8;
Short=E2F-8;
Name=E2F8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, Mammary gland, Skin, and Testis;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-139.
Totoki Y., Yada T., Sakaki Y., Takeda T.;
"Identification of novel human genes predicted by combining multiple
gene finders.";
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=16179649; DOI=10.1093/nar/gki855;
Christensen J., Cloos P., Toftegaard U., Klinkenberg D., Bracken A.P.,
Trinh E., Heeran M., Di Stefano L., Helin K.;
"Characterization of E2F8, a novel E2F-like cell-cycle regulated
repressor of E2F-activated transcription.";
Nucleic Acids Res. 33:5458-5470(2005).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-156 AND
ARG-314.
PubMed=15897886; DOI=10.1038/sj.onc.1208703;
Logan N., Graham A., Zhao X., Fisher R., Maiti B., Leone G.,
La Thangue N.B.;
"E2F-8: an E2F family member with a similar organization of DNA-
binding domains to E2F-7.";
Oncogene 24:5000-5004(2005).
[7]
SUBUNIT.
PubMed=18194653; DOI=10.1016/j.devcel.2007.10.017;
Li J., Ran C., Li E., Gordon F., Comstock G., Siddiqui H.,
Cleghorn W., Chen H.-Z., Kornacker K., Liu C.-G., Pandit S.K.,
Khanizadeh M., Weinstein M., Leone G., de Bruin A.;
"Synergistic function of E2F7 and E2F8 is essential for cell survival
and embryonic development.";
Dev. Cell 14:62-75(2008).
[8]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-156 AND ARG-314.
PubMed=18202719; DOI=10.1038/sj.embor.7401158;
Zalmas L.P., Zhao X., Graham A.L., Fisher R., Reilly C., Coutts A.S.,
La Thangue N.B.;
"DNA-damage response control of E2F7 and E2F8.";
EMBO Rep. 9:252-259(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[10]
FUNCTION, AND INTERACTION WITH HIF1A.
PubMed=22903062; DOI=10.1038/emboj.2012.231;
Weijts B.G., Bakker W.J., Cornelissen P.W., Liang K.H.,
Schaftenaar F.H., Westendorp B., de Wolf C.A., Paciejewska M.,
Scheele C.L., Kent L., Leone G., Schulte-Merker S., de Bruin A.;
"E2F7 and E2F8 promote angiogenesis through transcriptional activation
of VEGFA in cooperation with HIF1.";
EMBO J. 31:3871-3884(2012).
[11]
LACK OF RESPONSE TO DNA DAMAGE.
PubMed=22802528; DOI=10.1101/gad.184911.111;
Carvajal L.A., Hamard P.J., Tonnessen C., Manfredi J.J.;
"E2F7, a novel target, is up-regulated by p53 and mediates DNA damage-
dependent transcriptional repression.";
Genes Dev. 26:1533-1545(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-102; SER-413 AND
SER-417, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Atypical E2F transcription factor that participates in
various processes such as angiogenesis and polyploidization of
specialized cells. Mainly acts as a transcription repressor that
binds DNA independently of DP proteins and specifically recognizes
the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses
transcription of classical E2F transcription factors such as E2F1:
component of a feedback loop in S phase by repressing the
expression of E2F1, thereby preventing p53/TP53-dependent
apoptosis. Plays a key role in polyploidization of cells in
placenta and liver by regulating the endocycle, probably by
repressing genes promoting cytokinesis and antagonizing action of
classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for
placental development by promoting polyploidization of trophoblast
giant cells. Acts as a promoter of sprouting angiogenesis,
possibly by acting as a transcription activator: associates with
HIF1A, recognizes and binds the VEGFA promoter, which is different
from canonical E2 recognition site, and activates expression of
the VEGFA gene. {ECO:0000269|PubMed:15897886,
ECO:0000269|PubMed:16179649, ECO:0000269|PubMed:18202719,
ECO:0000269|PubMed:22903062}.
-!- SUBUNIT: Homodimer and heterodimer: mainly forms homodimers and,
to a lesser extent, heterodimers with E2F8. Dimerization is
important for DNA-binding. Interacts with HIF1A.
{ECO:0000269|PubMed:18194653, ECO:0000269|PubMed:18202719,
ECO:0000269|PubMed:22903062}.
-!- INTERACTION:
Q96AV8:E2F7; NbExp=4; IntAct=EBI-7779316, EBI-1386765;
Q13643:FHL3; NbExp=3; IntAct=EBI-7779316, EBI-741101;
Q12800:TFCP2; NbExp=3; IntAct=EBI-7779316, EBI-717422;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15897886}.
-!- INDUCTION: Following DNA damage (PubMed:18202719). Up-regulation
in response to DNA damage is not confirmed by PubMed:22802528.
{ECO:0000269|PubMed:18202719}.
-!- DOMAIN: In contrast to classical members of the E2F transcription
factor, atypical members contain 2 DNA-binding domains and
regulate transcription in a DP-independent manner. Both DNA-
binding domains are required for DNA-binding and are proposed to
form an intramolecular structure that is similar to the winged
helix structure of the E2F-DP heterodimer (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH28244.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB15605.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK026964; BAB15605.1; ALT_INIT; mRNA.
EMBL; AK292688; BAF85377.1; -; mRNA.
EMBL; CH471064; EAW68354.1; -; Genomic_DNA.
EMBL; BC028244; AAH28244.2; ALT_INIT; mRNA.
EMBL; BC090877; AAH90877.1; -; mRNA.
EMBL; BC108700; AAI08701.1; -; mRNA.
EMBL; BC126400; AAI26401.1; -; mRNA.
EMBL; BC126402; AAI26403.1; -; mRNA.
EMBL; AB231781; BAE46901.1; -; mRNA.
CCDS; CCDS7849.1; -.
RefSeq; NP_001243300.1; NM_001256371.1.
RefSeq; NP_001243301.1; NM_001256372.1.
RefSeq; NP_078956.2; NM_024680.3.
UniGene; Hs.523526; -.
PDB; 4YO2; X-ray; 3.07 A; A=110-341.
PDBsum; 4YO2; -.
ProteinModelPortal; A0AVK6; -.
SMR; A0AVK6; -.
BioGrid; 122847; 8.
IntAct; A0AVK6; 6.
MINT; MINT-6541611; -.
STRING; 9606.ENSP00000250024; -.
iPTMnet; A0AVK6; -.
PhosphoSitePlus; A0AVK6; -.
BioMuta; E2F8; -.
EPD; A0AVK6; -.
MaxQB; A0AVK6; -.
PaxDb; A0AVK6; -.
PRIDE; A0AVK6; -.
DNASU; 79733; -.
Ensembl; ENST00000250024; ENSP00000250024; ENSG00000129173.
Ensembl; ENST00000527884; ENSP00000434199; ENSG00000129173.
Ensembl; ENST00000620009; ENSP00000481103; ENSG00000129173.
GeneID; 79733; -.
KEGG; hsa:79733; -.
UCSC; uc001mpm.4; human.
CTD; 79733; -.
DisGeNET; 79733; -.
EuPathDB; HostDB:ENSG00000129173.12; -.
GeneCards; E2F8; -.
HGNC; HGNC:24727; E2F8.
HPA; HPA064882; -.
MIM; 612047; gene.
neXtProt; NX_A0AVK6; -.
OpenTargets; ENSG00000129173; -.
PharmGKB; PA142671918; -.
eggNOG; KOG2578; Eukaryota.
eggNOG; ENOG4111IGY; LUCA.
GeneTree; ENSGT00530000063616; -.
HOVERGEN; HBG063270; -.
InParanoid; A0AVK6; -.
KO; K09391; -.
OMA; LIPLTQC; -.
OrthoDB; EOG091G0F9Z; -.
PhylomeDB; A0AVK6; -.
TreeFam; TF105567; -.
Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
ChiTaRS; E2F8; human.
GenomeRNAi; 79733; -.
PRO; PR:A0AVK6; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000129173; -.
CleanEx; HS_E2F8; -.
ExpressionAtlas; A0AVK6; baseline and differential.
Genevisible; A0AVK6; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IMP:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0033301; P:cell cycle comprising mitosis without cytokinesis; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0060718; P:chorionic trophoblast cell differentiation; ISS:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0070365; P:hepatocyte differentiation; ISS:UniProtKB.
GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0001890; P:placenta development; ISS:UniProtKB.
GO; GO:0032877; P:positive regulation of DNA endoreduplication; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060707; P:trophoblast giant cell differentiation; ISS:UniProtKB.
Gene3D; 1.10.10.10; -; 2.
InterPro; IPR015633; E2F.
InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR12081; PTHR12081; 1.
Pfam; PF02319; E2F_TDP; 2.
SMART; SM01372; E2F_TDP; 2.
SUPFAM; SSF46785; SSF46785; 2.
1: Evidence at protein level;
3D-structure; Activator; Cell cycle; Complete proteome; DNA-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor;
Transcription; Transcription regulation.
CHAIN 1 867 Transcription factor E2F8.
/FTId=PRO_0000298909.
DNA_BIND 113 182 {ECO:0000255}.
DNA_BIND 261 347 {ECO:0000255}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 674 674 I -> V (in dbSNP:rs793274).
/FTId=VAR_034735.
MUTAGEN 156 156 R->A: Loss of DNA-binding and inhibition
of E2F1-dependent activation. Impairs
DNA-binding and dimerization; when
associated with A-314.
{ECO:0000269|PubMed:15897886,
ECO:0000269|PubMed:18202719}.
MUTAGEN 314 314 R->A: Loss of DNA-binding and inhibition
of E2F1-dependent activation. Impairs
DNA-binding and dimerization; when
associated with A-156.
{ECO:0000269|PubMed:15897886,
ECO:0000269|PubMed:18202719}.
CONFLICT 138 138 N -> I (in Ref. 4; BAE46901).
{ECO:0000305}.
CONFLICT 460 460 K -> R (in Ref. 1; BAB15605).
{ECO:0000305}.
HELIX 114 116 {ECO:0000244|PDB:4YO2}.
HELIX 118 128 {ECO:0000244|PDB:4YO2}.
STRAND 135 137 {ECO:0000244|PDB:4YO2}.
HELIX 142 148 {ECO:0000244|PDB:4YO2}.
HELIX 154 166 {ECO:0000244|PDB:4YO2}.
STRAND 169 174 {ECO:0000244|PDB:4YO2}.
STRAND 177 179 {ECO:0000244|PDB:4YO2}.
HELIX 186 196 {ECO:0000244|PDB:4YO2}.
HELIX 199 209 {ECO:0000244|PDB:4YO2}.
HELIX 266 276 {ECO:0000244|PDB:4YO2}.
HELIX 286 296 {ECO:0000244|PDB:4YO2}.
STRAND 305 307 {ECO:0000244|PDB:4YO2}.
HELIX 308 321 {ECO:0000244|PDB:4YO2}.
STRAND 324 327 {ECO:0000244|PDB:4YO2}.
STRAND 332 334 {ECO:0000244|PDB:4YO2}.
SEQUENCE 867 AA; 94166 MW; AADBCFACB888BD93 CRC64;
MENEKENLFC EPHKRGLMKT PLKESTTANI VLAEIQPDFG PLTTPTKPKE GSQGEPWTPT
ANLKMLISAV SPEIRNRDQK RGLFDNRSGL PEAKDCIHEH LSGDEFEKSQ PSRKEKSLGL
LCHKFLARYP NYPNPAVNND ICLDEVAEEL NVERRRIYDI VNVLESLHMV SRLAKNRYTW
HGRHNLNKTL GTLKSIGEEN KYAEQIMMIK KKEYEQEFDF IKSYSIEDHI IKSNTGPNGH
PDMCFVELPG VEFRAASVNS RKDKSLRVMS QKFVMLFLVS TPQIVSLEVA AKILIGEDHV
EDLDKSKFKT KIRRLYDIAN VLSSLDLIKK VHVTEERGRK PAFKWTGPEI SPNTSGSSPV
IHFTPSDLEV RRSSKENCAK NLFSTRGKPN FTRHPSLIKL VKSIESDRRK INSAPSSPIK
TNKAESSQNS APFPSKMAQL AAICKMQLEE QSSESRQKVK VQLARSGPCK PVAPLDPPVN
AEMELTAPSL IQPLGMVPLI PSPLSSAVPL ILPQAPSGPS YAIYLQPTQA HQSVTPPQGL
SPTVCTTHSS KATGSKDSTD ATTEKAANDT SKASASTRPG SLLPAPERQG AKSRTREPAG
ERGSKRASML EDSGSKKKFK EDLKGLENVS ATLFPSGYLI PLTQCSSLGA ESILSGKENS
SALSPNHRIY SSPIAGVIPV TSSELTAVNF PSFHVTPLKL MVSPTSVAAV PVGNSPALAS
SHPVPIQNPS SAIVNFTLQH LGLISPNVQL SASPGSGIVP VSPRIESVNV APENAGTQQG
RATNYDSPVP GQSQPNGQSV AVTGAQQPVP VTPKGSQLVA ESFFRTPGGP TKPTSSSCMD
FEGANKTSLG TLFVPQRKLE VSTEDVH


Related products :

Catalog number Product name Quantity
E2F8_MOUSE ELISA Kit FOR Transcription factor E2F8; organism: Mouse; gene name: E2f8 96T
EIAAB12269 E2F8,E2F-8,Homo sapiens,Human,Transcription factor E2F8
CSB-EL007349HU Human Transcription factor E2F8(E2F8) ELISA kit SpeciesHuman 96T
CSB-EL007349MO Mouse Transcription factor E2F8(E2F8) ELISA kit SpeciesMouse 96T
EIAAB12270 E2f8,E2F-8,Mouse,Mus musculus,Transcription factor E2F8
CSB-EL007349HU Human Transcription factor E2F8(E2F8) ELISA kit 96T
H7236 Transcription factor E2F8 (E2F8), Human, ELISA Kit 96T
H7237 Transcription factor E2F8 (E2F8), Mouse, ELISA Kit 96T
CSB-EL007349MO Mouse Transcription factor E2F8(E2F8) ELISA kit 96T
EA3 E2F8 Gene E2F transcription factor 8
E2F8 E2F6 Gene E2F transcription factor 6
E2F8_MOUSE Mouse ELISA Kit FOR Transcription factor E2F8 96T
CSB-EL007349MO Mouse E2F transcription factor 8 (E2F8) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL007349HU Human E2F transcription factor 8 (E2F8) ELISA kit, Species Human, Sample Type serum, plasma 96T
EIAAB42084 Homo sapiens,Human,Mitochondrial transcription factor 1,MtTF1,mtTFA,TCF6,TCF-6,TCF6L2,TFAM,Transcription factor 6,Transcription factor 6-like 2,Transcription factor A, mitochondrial
18-003-42098 Ets domain transcription factor - ESE3 transcription factor; EHF protein; DJ875K15.1.2 (Ets homologous factor (Ets-domain transcription factor. ESE-3B (Isoform 2))); ETS-family transcription factor EH 0.1 mg Protein A
EIAAB42103 Immunoglobulin enhancer-binding factor E12_E47,Pan,Pancreas specific transcription factor 1c,Ptf1c,Rat,Rattus norvegicus,Tcf3,TCF-3,Tcfe2a,Transcription factor 3,Transcription factor E2-alpha,Transcri
EIAAB42104 Alf2,Immunoglobulin enhancer-binding factor E12_E47,Me2,Mouse,Mus musculus,Tcf3,TCF-3,Tcfe2a,Transcription factor 3,Transcription factor A1,Transcription factor E2-alpha
31-248 Transcription initiation factor IIA . and . chains (GTranscription Factor Antibodies2A1, Transcription Factor AntibodiesIIA p35 and p19 subunits, Transcription Factor AntibodiesIIAL) binding ability o 0.05 mg
EIAAB12290 E4F transcription factor 1,E4f1,Mouse,Mus musculus,p120E4F,Putative E3 ubiquitin-protein ligase E4F1,Transcription factor E4F,Transcription factor E4F1,Transcription factor phi AP3
A1135 E2F8 Primary Antibody, E2F8, Species: Human Recombinant Protein Source: Rabbit Polyclonal 50ug
18-003-44075 Transcription factor E2-alpha - Immunoglobulin enhancer-binding factor E12_E47; Transcription factor 3; TCF-3; Immunoglobulin transcription factor 1; Transcription factor ITF-1; Kappa-E2-binding facto 0.1 mg Protein A
EIAAB25650 Homo sapiens,Human,Metal regulatory transcription factor 1,MRE-binding transcription factor,MTF1,Transcription factor MTF-1
EIAAB42050 Basic transcription factor 2 52 kDa subunit,BTF2 p52,General transcription factor IIH polypeptide 4,General transcription factor IIH subunit 4,GTF2H4,Homo sapiens,Human,TFIIH basal transcription facto
EIAAB42045 Basic transcription factor 2 34 kDa subunit,BTF2 p34,General transcription factor IIH polypeptide 3,General transcription factor IIH subunit 3,GTF2H3,Homo sapiens,Human,TFIIH basal transcription facto


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur