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POU domain, class 5, transcription factor 1 (NF-A3) (Octamer-binding protein 3) (Oct-3) (Octamer-binding protein 4) (Oct-4) (Octamer-binding transcription factor 3) (OTF-3)

 PO5F1_MOUSE             Reviewed;         352 AA.
P20263; Q63843;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
22-NOV-2017, entry version 175.
RecName: Full=POU domain, class 5, transcription factor 1;
AltName: Full=NF-A3;
AltName: Full=Octamer-binding protein 3;
Short=Oct-3;
AltName: Full=Octamer-binding protein 4;
Short=Oct-4;
AltName: Full=Octamer-binding transcription factor 3;
Short=OTF-3;
Name=Pou5f1; Synonyms=Oct-3, Oct-4, Otf-3, Otf3;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Embryonic carcinoma;
PubMed=1972777; DOI=10.1038/345686a0;
Rosner M.H., Vigano M.A., Ozato K., Timmons P.M., Poirier F.,
Rigby P.W.J., Staudt L.;
"A POU-domain transcription factor in early stem cells and germ cells
of the mammalian embryo.";
Nature 345:686-692(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
TISSUE=Embryonic carcinoma;
PubMed=1690859; DOI=10.1038/344435a0;
Schoeler H.R., Ruppert S., Suzuki N., Chowdhury K., Gruss P.;
"New type of POU domain in germ line-specific protein Oct-4.";
Nature 344:435-439(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1967980; DOI=10.1016/0092-8674(90)90597-8;
Okamoto K., Okazawa H., Okuda A., Sakai M., Muramatsu M., Hamada H.;
"A novel octamer binding transcription factor is differentially
expressed in mouse embryonic cells.";
Cell 60:461-472(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, AND INDUCTION.
PubMed=1915274;
Okazawa H., Okamoto K., Ishino F., Ishino-Kaneko T., Takeda S.,
Toyoda Y., Muramatsu M., Hamada H.;
"The oct3 gene, a gene for an embryonic transcription factor, is
controlled by a retinoic acid repressible enhancer.";
EMBO J. 10:2997-3005(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
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).
[6]
SUMOYLATION AT LYS-118, AND MUTAGENESIS OF LYS-118.
PubMed=17097055; DOI=10.1016/j.bbrc.2006.10.130;
Tsuruzoe S., Ishihara K., Uchimura Y., Watanabe S., Sekita Y.,
Aoto T., Saitoh H., Yuasa Y., Niwa H., Kawasuji M., Baba H., Nakao M.;
"Inhibition of DNA binding of Sox2 by the SUMO conjugation.";
Biochem. Biophys. Res. Commun. 351:920-926(2006).
[7]
BIOTECHNOLOGY.
PubMed=16904174; DOI=10.1016/j.cell.2006.07.024;
Takahashi K., Yamanaka S.;
"Induction of pluripotent stem cells from mouse embryonic and adult
fibroblast cultures by defined factors.";
Cell 126:663-676(2006).
[8]
SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118; GLU-120; LYS-215 AND
LYS-244, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2I.
PubMed=17496161; DOI=10.1096/fj.06-6914com;
Zhang Z., Liao B., Xu M., Jin Y.;
"Post-translational modification of POU domain transcription factor
Oct-4 by SUMO-1.";
FASEB J. 21:3042-3051(2007).
[9]
SUMOYLATION AT LYS-118, MUTAGENESIS OF LYS-118, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=17525163; DOI=10.1074/jbc.M611041200;
Wei F., Schoeler H.R., Atchison M.L.;
"Sumoylation of Oct4 enhances its stability, DNA binding, and
transactivation.";
J. Biol. Chem. 282:21551-21560(2007).
[10]
INTERACTION WITH ESRRB.
PubMed=18662995; DOI=10.1128/MCB.00301-08;
van den Berg D.L., Zhang W., Yates A., Engelen E., Takacs K.,
Bezstarosti K., Demmers J., Chambers I., Poot R.A.;
"Estrogen-related receptor beta interacts with Oct4 to positively
regulate Nanog gene expression.";
Mol. Cell. Biol. 28:5986-5995(2008).
[11]
INTERACTION WITH ZSCAN10.
PubMed=19740739; DOI=10.1074/jbc.M109.016162;
Yu H.B., Kunarso G., Hong F.H., Stanton L.W.;
"Zfp206, Oct4, and Sox2 are integrated components of a transcriptional
regulatory network in embryonic stem cells.";
J. Biol. Chem. 284:31327-31335(2009).
[12]
UBIQUITINATION.
PubMed=19997087; DOI=10.1038/cr.2009.136;
Liao B., Jin Y.;
"Wwp2 mediates Oct4 ubiquitination and its own auto-ubiquitination in
a dosage-dependent manner.";
Cell Res. 20:332-344(2010).
[13]
STRUCTURE BY NMR OF POU DOMAIN.
PubMed=8097478; DOI=10.1016/0014-5793(93)80088-C;
Morita E.H., Shirakawa M., Hayashi F., Imagawa M., Kyogoku Y.;
"Secondary structure of the oct-3 POU homeodomain as determined by 1H-
15N NMR spectroscopy.";
FEBS Lett. 321:107-110(1993).
-!- FUNCTION: Transcription factor that binds to the octamer motif
(5'-ATTTGCAT-3'). Forms a trimeric complex with SOX2 on DNA and
controls the expression of a number of genes involved in embryonic
development such as YES1, FGF4, UTF1 and ZFP206. Critical for
early embryogenesis and for embryonic stem cell pluripotency.
{ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163}.
-!- SUBUNIT: Interacts with PKM. Interacts with WWP2 (By similarity).
Interacts with UBE2I and ZSCAN10 (PubMed:17496161,
PubMed:19740739). Interacts with PCGF1 (By similarity). Interacts
with ESRRB; recruits ESRRB near the POU5F1-SOX2 element in the
NANOG proximal promoter; the intercaction is DNA independent
(PubMed:18662995). {ECO:0000250|UniProtKB:Q01860,
ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:18662995,
ECO:0000269|PubMed:19740739}.
-!- INTERACTION:
P11440:Cdk1; NbExp=4; IntAct=EBI-1606219, EBI-846949;
Q61545:Ewsr1; NbExp=13; IntAct=EBI-1606219, EBI-1606991;
Q9R190:Mta2; NbExp=6; IntAct=EBI-1606219, EBI-904134;
Q80Z64:Nanog; NbExp=4; IntAct=EBI-1606219, EBI-2312517;
Q61066:Nr0b1; NbExp=5; IntAct=EBI-1606219, EBI-2312665;
P11103:Parp1; NbExp=2; IntAct=EBI-1606219, EBI-642213;
P52480:Pkm; NbExp=6; IntAct=EBI-1606219, EBI-647785;
Q8BUN5:Smad3; NbExp=13; IntAct=EBI-1606219, EBI-2337983;
P48432:Sox2; NbExp=4; IntAct=EBI-1606219, EBI-2313612;
Q62318-1:Trim28; NbExp=3; IntAct=EBI-1606219, EBI-6876996;
P61965:Wdr5; NbExp=7; IntAct=EBI-1606219, EBI-1247084;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-
ProRule:PRU00530, ECO:0000269|PubMed:17496161,
ECO:0000269|PubMed:17525163}. Note=Expressed in a diffuse and
slightly punctuate pattern.
-!- TISSUE SPECIFICITY: Expressed the totipotent and pluripotent stem
cells of the pregastrulation embryo. Also expressed in primordial
germ cells and in the female germ line. Absent from adult tissues.
{ECO:0000269|PubMed:1690859, ECO:0000269|PubMed:1972777}.
-!- DEVELOPMENTAL STAGE: Down-regulated during differentiation to
endoderm and mesoderm. {ECO:0000269|PubMed:1972777}.
-!- INDUCTION: Repressed by retinoic acid (RA).
{ECO:0000269|PubMed:1690859, ECO:0000269|PubMed:1915274}.
-!- DOMAIN: The POU-specific domain mediates interaction with PKM.
{ECO:0000250}.
-!- PTM: Sumoylation enhances the protein stability, DNA binding and
transactivation activity. Sumoylation is required for enhanced
YES1 expression. {ECO:0000269|PubMed:17097055,
ECO:0000269|PubMed:17496161, ECO:0000269|PubMed:17525163}.
-!- PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination
by WWP2 leading to proteasomal degradation.
{ECO:0000269|PubMed:19997087}.
-!- PTM: ERK1/2-mediated phosphorylation at Ser-106 promotes nuclear
exclusion and proteasomal degradation. Phosphorylation at Thr-228
and Ser-229 decrease DNA-binding and alters ability to activate
transcription (By similarity). {ECO:0000250}.
-!- BIOTECHNOLOGY: POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four
Yamanaka factors. When combined, these factors are sufficient to
reprogram differentiated cells to an embryonic-like state
designated iPS (induced pluripotent stem) cells. iPS cells exhibit
the morphology and growth properties of ES cells and express ES
cell marker genes. {ECO:0000269|PubMed:16904174}.
-!- SIMILARITY: Belongs to the POU transcription factor family. Class-
5 subfamily. {ECO:0000305}.
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EMBL; M34381; AAA39844.1; ALT_SEQ; mRNA.
EMBL; X52437; CAA36682.1; -; mRNA.
EMBL; S58426; AAB19896.1; -; Genomic_DNA.
EMBL; S58422; AAB19896.1; JOINED; Genomic_DNA.
EMBL; S58423; AAB19896.1; JOINED; Genomic_DNA.
EMBL; S58424; AAB19896.1; JOINED; Genomic_DNA.
EMBL; S58425; AAB19896.1; JOINED; Genomic_DNA.
EMBL; BC068268; AAH68268.1; -; mRNA.
CCDS; CCDS37600.1; -.
PIR; A34672; A34672.
PIR; S17313; S17313.
RefSeq; NP_038661.2; NM_013633.3.
UniGene; Mm.17031; -.
PDB; 1OCP; NMR; -; A=217-282.
PDB; 3L1P; X-ray; 2.80 A; A/B=131-282.
PDBsum; 1OCP; -.
PDBsum; 3L1P; -.
ProteinModelPortal; P20263; -.
SMR; P20263; -.
BioGrid; 202313; 304.
DIP; DIP-29931N; -.
IntAct; P20263; 142.
STRING; 10090.ENSMUSP00000025271; -.
iPTMnet; P20263; -.
PhosphoSitePlus; P20263; -.
PaxDb; P20263; -.
PeptideAtlas; P20263; -.
PRIDE; P20263; -.
Ensembl; ENSMUST00000025271; ENSMUSP00000025271; ENSMUSG00000024406.
GeneID; 18999; -.
KEGG; mmu:18999; -.
UCSC; uc008chu.2; mouse.
CTD; 5460; -.
MGI; MGI:101893; Pou5f1.
eggNOG; KOG3802; Eukaryota.
eggNOG; ENOG410XQ7X; LUCA.
GeneTree; ENSGT00760000118935; -.
HOGENOM; HOG000089941; -.
HOVERGEN; HBG057998; -.
InParanoid; P20263; -.
KO; K09367; -.
OMA; LENMFLQ; -.
OrthoDB; EOG091G0U0S; -.
PhylomeDB; P20263; -.
TreeFam; TF316413; -.
Reactome; R-MMU-452723; Transcriptional regulation of pluripotent stem cells.
EvolutionaryTrace; P20263; -.
PRO; PR:P20263; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024406; -.
CleanEx; MM_POU5F1; -.
ExpressionAtlas; P20263; baseline and differential.
Genevisible; P20263; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:AgBase.
GO; GO:0044798; C:nuclear transcription factor complex; IDA:MGI.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0017053; C:transcriptional repressor complex; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
GO; GO:0019955; F:cytokine binding; IDA:AgBase.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0001158; F:enhancer sequence-specific DNA binding; IDA:AgBase.
GO; GO:0071837; F:HMG box domain binding; IEA:Ensembl.
GO; GO:0035198; F:miRNA binding; ISO:MGI.
GO; GO:0070974; F:POU domain binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:0001824; P:blastocyst development; IEP:BHF-UCL.
GO; GO:0001832; P:blastocyst growth; IGI:MGI.
GO; GO:0003130; P:BMP signaling pathway involved in heart induction; ISO:MGI.
GO; GO:0060913; P:cardiac cell fate determination; ISO:MGI.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0060795; P:cell fate commitment involved in formation of primary germ layer; ISO:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0001712; P:ectodermal cell fate commitment; IDA:MGI.
GO; GO:0001711; P:endodermal cell fate commitment; IDA:MGI.
GO; GO:0001714; P:endodermal cell fate specification; ISO:MGI.
GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:MGI.
GO; GO:0001710; P:mesodermal cell fate commitment; IDA:MGI.
GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IDA:MGI.
GO; GO:0045596; P:negative regulation of cell differentiation; IGI:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IDA:AgBase.
GO; GO:0060965; P:negative regulation of gene silencing by miRNA; ISO:MGI.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0035413; P:positive regulation of catenin import into nucleus; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:MGI.
GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0009786; P:regulation of asymmetric cell division; IEP:BHF-UCL.
GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
GO; GO:0090081; P:regulation of heart induction by regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0090308; P:regulation of methylation-dependent chromatin silencing; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0010033; P:response to organic substance; IDA:MGI.
GO; GO:0032526; P:response to retinoic acid; IDA:MGI.
GO; GO:0035019; P:somatic stem cell population maintenance; ISO:MGI.
GO; GO:0048863; P:stem cell differentiation; IDA:MGI.
GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0001829; P:trophectodermal cell differentiation; IGI:MGI.
CDD; cd00086; homeodomain; 1.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR017970; Homeobox_CS.
InterPro; IPR001356; Homeobox_dom.
InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
InterPro; IPR013847; POU.
InterPro; IPR000327; POU_dom.
InterPro; IPR015585; POU_dom_5.
PANTHER; PTHR11636:SF86; PTHR11636:SF86; 1.
Pfam; PF00046; Homeobox; 1.
Pfam; PF00157; Pou; 1.
PRINTS; PR00028; POUDOMAIN.
SMART; SM00389; HOX; 1.
SMART; SM00352; POU; 1.
SUPFAM; SSF46689; SSF46689; 1.
SUPFAM; SSF47413; SSF47413; 1.
PROSITE; PS00027; HOMEOBOX_1; 1.
PROSITE; PS50071; HOMEOBOX_2; 1.
PROSITE; PS00035; POU_1; 1.
PROSITE; PS00465; POU_2; 1.
PROSITE; PS51179; POU_3; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Developmental protein;
DNA-binding; Homeobox; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 352 POU domain, class 5, transcription factor
1.
/FTId=PRO_0000100749.
DOMAIN 131 205 POU-specific. {ECO:0000255|PROSITE-
ProRule:PRU00530}.
DNA_BIND 223 282 Homeobox. {ECO:0000255|PROSITE-
ProRule:PRU00108}.
MOD_RES 106 106 Phosphoserine; by MAPK.
{ECO:0000250|UniProtKB:Q01860}.
MOD_RES 228 228 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01860}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000250|UniProtKB:Q01860}.
MOD_RES 282 282 Phosphoserine.
{ECO:0000250|UniProtKB:Q01860}.
MOD_RES 347 347 Phosphoserine.
{ECO:0000250|UniProtKB:Q01860}.
CROSSLNK 118 118 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
MUTAGEN 118 118 K->R: Absence of sumoylation. Enhanced
protein degradation. Reduced self-renewal
ability in ES cells. 70% lower expression
of YES1. Reduced DNA binding. No change
in nuclear location. No change in nuclear
localization. Absence of sumoylation;
when associated with R-215 and R-244.
{ECO:0000269|PubMed:17097055,
ECO:0000269|PubMed:17496161,
ECO:0000269|PubMed:17525163}.
MUTAGEN 120 120 E->A: Absence of sumoylation. Enhanced
protein degradation. Reduced self-renewal
ability in ES cells. 55% lower expression
of YES1. {ECO:0000269|PubMed:17496161}.
MUTAGEN 215 215 K->R: No change in sumoylation; when
associated with R-244. Loss of
sumoylation. No change in nuclear
localization; when associated with R-118
and R-244. {ECO:0000269|PubMed:17496161}.
MUTAGEN 244 244 K->R: No change in sumoylation. No change
in sumoylation; when associated with R-
215. Loss of sumoylation; when associated
with R-118 and R-215. No change in
nuclear localization; when associated
with R-118 and R-215.
{ECO:0000269|PubMed:17496161}.
CONFLICT 1 28 Missing (in Ref. 2; CAA36682).
{ECO:0000305}.
CONFLICT 29 29 V -> M (in Ref. 2; CAA36682).
{ECO:0000305}.
CONFLICT 31 31 P -> S (in Ref. 4; AAA39844/AAB19896).
{ECO:0000305}.
HELIX 132 152 {ECO:0000244|PDB:3L1P}.
HELIX 157 168 {ECO:0000244|PDB:3L1P}.
HELIX 174 181 {ECO:0000244|PDB:3L1P}.
HELIX 187 204 {ECO:0000244|PDB:3L1P}.
HELIX 208 212 {ECO:0000244|PDB:3L1P}.
STRAND 223 225 {ECO:0000244|PDB:1OCP}.
HELIX 232 239 {ECO:0000244|PDB:3L1P}.
TURN 240 244 {ECO:0000244|PDB:3L1P}.
HELIX 250 259 {ECO:0000244|PDB:3L1P}.
HELIX 264 279 {ECO:0000244|PDB:3L1P}.
SEQUENCE 352 AA; 38216 MW; 757E41DF52286714 CRC64;
MAGHLASDFA FSPPPGGGDG SAGLEPGWVD PRTWLSFQGP PGGPGIGPGS EVLGISPCPP
AYEFCGGMAY CGPQVGLGLV PQVGVETLQP EGQAGARVES NSEGTSSEPC ADRPNAVKLE
KVEPTPEESQ DMKALQKELE QFAKLLKQKR ITLGYTQADV GLTLGVLFGK VFSQTTICRF
EALQLSLKNM CKLRPLLEKW VEEADNNENL QEICKSETLV QARKRKRTSI ENRVRWSLET
MFLKCPKPSL QQITHIANQL GLEKDVVRVW FCNRRQKGKR SSIEYSQREE YEATGTPFPG
GAVSFPLPPG PHFGTPGYGS PHFTTLYSVP FPEGEAFPSV PVTALGSPMH SN


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U1533p CLIA OCT3,Oct-3,OCT4,Oct-4,Octamer-binding protein 3,Octamer-binding protein 4,Octamer-binding transcription factor 3,OTF-3,Pig,POU domain, class 5, transcription factor 1,POU5F1,Sus scrofa 96T
E1533p ELISA kit OCT3,Oct-3,OCT4,Oct-4,Octamer-binding protein 3,Octamer-binding protein 4,Octamer-binding transcription factor 3,OTF-3,Pig,POU domain, class 5, transcription factor 1,POU5F1,Sus scrofa 96T
U1533m CLIA Mouse,Mus musculus,NF-A3,Oct-3,Oct-3,Oct-4,Oct-4,Octamer-binding protein 3,Octamer-binding protein 4,Octamer-binding transcription factor 3,Otf3,OTF-3,Otf-3,POU domain, class 5, transcription fac 96T
E1533m ELISA Mouse,Mus musculus,NF-A3,Oct-3,Oct-3,Oct-4,Oct-4,Octamer-binding protein 3,Octamer-binding protein 4,Octamer-binding transcription factor 3,Otf3,OTF-3,Otf-3,POU domain, class 5, transcription fa 96T
U1527m CLIA Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2,Mouse,Mus musculus,Oct2,Oct-2,Octamer-binding protein 2,Octamer-binding transcription factor 2,Otf2,OTF-2,POU domain, class 2, tra 96T
E1527m ELISA kit Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2,Mouse,Mus musculus,Oct2,Oct-2,Octamer-binding protein 2,Octamer-binding transcription factor 2,Otf2,OTF-2,POU domain, class 96T
E1527m ELISA Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2,Mouse,Mus musculus,Oct2,Oct-2,Octamer-binding protein 2,Octamer-binding transcription factor 2,Otf2,OTF-2,POU domain, class 2, tr 96T
E1527p ELISA kit Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2,OCT2,Oct-2,Octamer-binding protein 2,Octamer-binding transcription factor 2,OTF2,OTF-2,Pig,POU domain, class 2, transcriptio 96T
U1527h CLIA Homo sapiens,Human,Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2,OCT2,Oct-2,Octamer-binding protein 2,Octamer-binding transcription factor 2,OTF2,OTF-2,POU domain, class 2, tra 96T
E1527h ELISA Homo sapiens,Human,Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2,OCT2,Oct-2,Octamer-binding protein 2,Octamer-binding transcription factor 2,OTF2,OTF-2,POU domain, class 2, tr 96T
E1527h ELISA kit Homo sapiens,Human,Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2,OCT2,Oct-2,Octamer-binding protein 2,Octamer-binding transcription factor 2,OTF2,OTF-2,POU domain, class 96T
E1533m ELISA kit Mouse,Mus musculus,NF-A3,Oct-3,Oct-3,Oct-4,Oct-4,Octamer-binding protein 3,Octamer-binding protein 4,Octamer-binding transcription factor 3,Otf3,OTF-3,Otf-3,POU domain, class 5, transcripti 96T
EIAAB31740 Homo sapiens,Human,Oct-11,Octamer-binding protein 11,Octamer-binding transcription factor 11,OTF11,OTF-11,PLA1,POU domain, class 2, transcription factor 3,POU2F3,Transcription factor PLA-1,Transcripti
E1602h ELISA Homo sapiens,Human,OCT6,Oct-6,Octamer-binding protein 6,Octamer-binding transcription factor 6,OTF6,OTF-6,POU domain transcription factor SCIP,POU domain, class 3, transcription factor 1,POU3F1 96T
U1602h CLIA Homo sapiens,Human,OCT6,Oct-6,Octamer-binding protein 6,Octamer-binding transcription factor 6,OTF6,OTF-6,POU domain transcription factor SCIP,POU domain, class 3, transcription factor 1,POU3F1 96T
EIAAB31741 Oct-11,Octamer-binding protein 11,Octamer-binding transcription factor 11,Otf11,OTF-11,POU domain, class 2, transcription factor 3,Pou2f3,Rat,Rattus norvegicus,Skn1,Skn-1,Transcription factor Skn-1
E1602h ELISA kit Homo sapiens,Human,OCT6,Oct-6,Octamer-binding protein 6,Octamer-binding transcription factor 6,OTF6,OTF-6,POU domain transcription factor SCIP,POU domain, class 3, transcription factor 1,PO 96T
E1602m ELISA kit Mouse,Mus musculus,Oct6,Oct-6,Octamer-binding protein 6,Octamer-binding transcription factor 6,Otf6,OTF-6,Otf-6,POU domain transcription factor SCIP,POU domain, class 3, transcription facto 96T
E1602m ELISA Mouse,Mus musculus,Oct6,Oct-6,Octamer-binding protein 6,Octamer-binding transcription factor 6,Otf6,OTF-6,Otf-6,POU domain transcription factor SCIP,POU domain, class 3, transcription factor 1,P 96T


 

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