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Transcription factor HIVEP3 (Human immunodeficiency virus type I enhancer-binding protein 3 homolog) (KB-binding and recognition component) (Kappa-B and V(D)J recombination signal sequences-binding protein) (Kappa-binding protein 1) (KBP-1) (Recombinant component) (Schnurri-3) (Zinc finger protein ZAS3)

 ZEP3_MOUSE              Reviewed;        2348 AA.
A2A884; A2MZW0; Q69ZG6; Q6SNP9;
29-APR-2008, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
05-JUL-2017, entry version 92.
RecName: Full=Transcription factor HIVEP3;
AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 3 homolog;
AltName: Full=KB-binding and recognition component;
AltName: Full=Kappa-B and V(D)J recombination signal sequences-binding protein;
AltName: Full=Kappa-binding protein 1;
Short=KBP-1;
AltName: Full=Recombinant component;
AltName: Full=Schnurri-3;
AltName: Full=Zinc finger protein ZAS3;
Name=Hivep3; Synonyms=KBP1, Kiaa1555, Krc, Rc, shn3, Zas3;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-2341, DOMAIN, FUNCTION, AND TISSUE
SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=8812474; DOI=10.1006/geno.1996.0380;
Wu L.-C., Liu Y., Strandtmann J., Mak C.-H., Lee B., Li Z., Yu C.Y.;
"The mouse DNA binding protein Rc for the kappa B motif of
transcription and for the V(D)J recombination signal sequences
contains composite DNA-protein interaction domains and belongs to a
new family of large transcriptional proteins.";
Genomics 35:415-424(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1281-2348.
TISSUE=Thymus;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1497-2295, FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, DOMAIN, AND REPEAT.
PubMed=8255760; DOI=10.1093/nar/21.22.5067;
Wu L.-C., Mak C.-H., Dear N., Boehm T., Foroni L., Rabbitts T.H.;
"Molecular cloning of a zinc finger protein which binds to the
heptamer of the signal sequence for V(D)J recombination.";
Nucleic Acids Res. 21:5067-5073(1993).
[5]
PHOSPHORYLATION.
PubMed=9862992; DOI=10.1093/nar/27.2.643;
Bachmeyer C., Mak C.H., Yu C.Y., Wu L.-C.;
"Regulation by phosphorylation of the zinc finger protein KRC that
binds the kappaB motif and V(D)J recombination signal sequences.";
Nucleic Acids Res. 27:643-648(1999).
[6]
FUNCTION.
PubMed=11035930; DOI=10.1006/excr.2000.5029;
Allen C.E., Wu L.-C.;
"Downregulation of KRC induces proliferation, anchorage independence,
and mitotic cell death in HeLa cells.";
Exp. Cell Res. 260:346-356(2000).
[7]
FUNCTION.
PubMed=10625627; DOI=10.1074/jbc.275.2.913;
Hjelmsoe I., Allen C.E., Cohn M.A., Tulchinsky E.M., Wu L.-C.;
"The kappaB and V(D)J recombination signal sequence binding protein
KRC regulates transcription of the mouse metastasis-associated gene
S100A4/mts1.";
J. Biol. Chem. 275:913-920(2000).
[8]
FUNCTION, AND DOMAIN ZAS.
PubMed=12193271; DOI=10.1186/1471-2172-3-10;
Allen C.E., Mak C.-H., Wu L.-C.;
"The kappa B transcriptional enhancer motif and signal sequences of
V(D)J recombination are targets for the zinc finger protein
HIVEP3/KRC: a site selection amplification binding study.";
BMC Immunol. 3:10-10(2002).
[9]
SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH TRAF1 AND TRAF2, AND
REGION.
PubMed=11804591; DOI=10.1016/S1097-2765(01)00434-8;
Oukka M., Kim S.T., Lugo G., Sun J., Wu L.-C., Glimcher L.H.;
"A mammalian homolog of Drosophila schnurri, KRC, regulates TNF
receptor-driven responses and interacts with TRAF2.";
Mol. Cell 9:121-131(2002).
[10]
FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
PubMed=12001065; DOI=10.1002/gene.10084;
Hicar M.D., Robinson M.L., Wu L.-C.;
"Embryonic expression and regulation of the large zinc finger protein
KRC.";
Genesis 33:8-20(2002).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14530385; DOI=10.1073/pnas.2133048100;
Hong J.W., Allen C.E., Wu L.-C.;
"Inhibition of NF-kappaB by ZAS3, a zinc-finger protein that also
binds to the kappaB motif.";
Proc. Natl. Acad. Sci. U.S.A. 100:12301-12306(2003).
[12]
FUNCTION, INTERACTION WITH JUN, AND INDUCTION.
PubMed=14707112; DOI=10.1084/jem.20030421;
Oukka M., Wein M.N., Glimcher L.H.;
"Schnurri-3 (KRC) interacts with c-Jun to regulate the IL-2 gene in T
cells.";
J. Exp. Med. 199:15-24(2004).
[13]
ALTERNATIVE PROMOTER USAGE.
PubMed=15627499; DOI=10.1016/j.bbaexp.2004.10.004;
Hong J.-W., Wu L.-C.;
"Structural characterization of the gene encoding the large zinc
finger protein ZAS3: implication to the origin of multiple promoters
in eukaryotic genes.";
Biochim. Biophys. Acta 1681:74-87(2005).
[14]
DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH RUNX2
AND WWP1.
PubMed=16728642; DOI=10.1126/science.1126313;
Jones D.C., Wein M.N., Oukka M., Hofstaetter J.G., Glimcher M.J.,
Glimcher L.H.;
"Regulation of adult bone mass by the zinc finger adapter protein
Schnurri-3.";
Science 312:1223-1227(2006).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Lung;
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).
-!- FUNCTION: Plays a role of transcription factor; binds to
recognition signal sequences (Rss heptamer) for somatic
recombination of immunoglobulin and T-cell receptor gene segments;
Binds also to the kappa-B motif of gene such as S100A4, involved
in cell progression and differentiation. Kappa-B motif is a gene
regulatory element found in promoters and enhancers of genes
involved in immunity, inflammation, and growth and that responds
to viral antigens, mitogens, and cytokines. Involvement of HIVEP3
in cell growth is strengthened by the fact that its down-
regulation promotes cell cycle progression with ultimate formation
of multinucleated giant cells. Strongly inhibits TNF-alpha-induced
NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B
by several mechanisms: as transcription factor, by competing for
Kappa-B motif and by repressing transcription in the nucleus;
through a non transcriptional process, by inhibiting nuclear
translocation of RELA by association with TRAF2, an adapter
molecule in the tumor necrosis factor signaling, which blocks the
formation of IKK complex. Interaction with TRAF proteins inhibits
both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated
responses that include apoptosis and proinflammatory cytokine gene
expression. Positively regulates the expression of IL2 in T-cell.
Essential regulator of adult bone formation.
{ECO:0000269|PubMed:10625627, ECO:0000269|PubMed:11035930,
ECO:0000269|PubMed:11804591, ECO:0000269|PubMed:12001065,
ECO:0000269|PubMed:12193271, ECO:0000269|PubMed:14530385,
ECO:0000269|PubMed:14707112, ECO:0000269|PubMed:8255760,
ECO:0000269|PubMed:8812474}.
-!- SUBUNIT: Interacts with TRAF1 AND TRAF2 as well as with JUN. Forms
a multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1.
{ECO:0000269|PubMed:11804591, ECO:0000269|PubMed:14707112,
ECO:0000269|PubMed:16728642}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11804591}.
Nucleus {ECO:0000269|PubMed:11804591}.
-!- TISSUE SPECIFICITY: Expressed in macrophages, lymphocytes, brain,
thymus, spleen and bone marrow. Expressed in osteoblasts, whole
bone and, to a lesser extent, in osteoclasts.
{ECO:0000269|PubMed:14530385, ECO:0000269|PubMed:16728642,
ECO:0000269|PubMed:8255760, ECO:0000269|PubMed:8812474}.
-!- DEVELOPMENTAL STAGE: Expressed in the thymus with increasing
level, approximately 4-fold, from E15.5 to E16.5, constant level
from E16.5 to birth, then decrease to a low level by P30.
Expressed at E13.5 in the dorsal root ganglia of the peripheral
nervous system and the trigeminal ganglion of the metencephalon
and at relatively low levels in the cerebral cortex; no
significant expression was observed prior to E13.5. Expressed in
the spinal cord at E19, but weakly detected in the lung and the
liver. {ECO:0000269|PubMed:12001065, ECO:0000269|PubMed:8255760}.
-!- INDUCTION: Upon CD3/CD28 stimulation in CD4 T-cells. Induced by
LPS in pre-B-cells. {ECO:0000269|PubMed:12001065,
ECO:0000269|PubMed:14707112}.
-!- DOMAIN: ZAS2 domain binds DNA as dimers, tetramers, and multiple
of tetramers and readily forms highly ordred DNA-protein
structures. {ECO:0000269|PubMed:12193271,
ECO:0000269|PubMed:8255760, ECO:0000269|PubMed:8812474}.
-!- PTM: Phosphorylated on threonine and serine residues.
Phosphorylation by cyclin-dependent kinase CDK1 decreases HIVEP3
DNA binding affinity, and by epidermal growth factor receptor
kinase increases its DNA binding affinity.
{ECO:0000269|PubMed:9862992}.
-!- DISRUPTION PHENOTYPE: Mice display adult-onset osteosclerosis with
increased bone mass due to increased osteoblast activity; the
osteoblasts contain elevated levels of Runx2.
{ECO:0000269|PubMed:16728642}.
-!- MISCELLANEOUS: Hivep3 gene expression is probably controlled by a
combination of differential promoter usage, alternative splicing,
and possible intergenic splicing.
-!- SEQUENCE CAUTION:
Sequence=AAA40039.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA40039.1; Type=Frameshift; Positions=1502, 2242; Evidence={ECO:0000305};
Sequence=AAR88090.1; Type=Frameshift; Positions=752, 781, 1045, 1054, 2242; Evidence={ECO:0000305};
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EMBL; AL607142; CAM27499.1; -; Genomic_DNA.
EMBL; AY454345; AAR88090.1; ALT_FRAME; mRNA.
EMBL; AK173200; BAD32478.1; -; mRNA.
EMBL; L07911; AAA40039.1; ALT_SEQ; mRNA.
CCDS; CCDS38863.1; -.
PIR; S41479; S41479.
PIR; T42717; T42717.
RefSeq; NP_034787.2; NM_010657.3.
RefSeq; XP_006502878.1; XM_006502815.2.
RefSeq; XP_006502879.1; XM_006502816.2.
RefSeq; XP_006502880.1; XM_006502817.2.
RefSeq; XP_011238754.1; XM_011240452.1.
RefSeq; XP_011238755.1; XM_011240453.1.
UniGene; Mm.302758; -.
UniGene; Mm.394479; -.
UniGene; Mm.422538; -.
UniGene; Mm.487430; -.
UniGene; Mm.488325; -.
ProteinModelPortal; A2A884; -.
SMR; A2A884; -.
STRING; 10090.ENSMUSP00000101914; -.
iPTMnet; A2A884; -.
PhosphoSitePlus; A2A884; -.
MaxQB; A2A884; -.
PaxDb; A2A884; -.
PeptideAtlas; A2A884; -.
PRIDE; A2A884; -.
Ensembl; ENSMUST00000106307; ENSMUSP00000101914; ENSMUSG00000028634.
Ensembl; ENSMUST00000166542; ENSMUSP00000130249; ENSMUSG00000028634.
GeneID; 16656; -.
KEGG; mmu:16656; -.
UCSC; uc008una.1; mouse.
CTD; 59269; -.
MGI; MGI:106589; Hivep3.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00530000063161; -.
HOGENOM; HOG000155774; -.
HOVERGEN; HBG095595; -.
InParanoid; A2A884; -.
KO; K09239; -.
OMA; MERIPGE; -.
OrthoDB; EOG091G00EA; -.
PhylomeDB; A2A884; -.
TreeFam; TF331837; -.
ChiTaRS; Hivep3; mouse.
PRO; PR:A2A884; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028634; -.
ExpressionAtlas; A2A884; baseline and differential.
Genevisible; A2A884; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IBA:GO_Central.
InterPro; IPR034729; ZF_CCHC_HIVEP.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS51811; ZF_CCHC_HIVEP; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
1: Evidence at protein level;
Coiled coil; Complete proteome; Cytoplasm; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 2348 Transcription factor HIVEP3.
/FTId=PRO_0000331628.
REPEAT 1897 1900 1. {ECO:0000269|PubMed:8255760}.
REPEAT 1927 1930 2. {ECO:0000269|PubMed:8255760}.
REPEAT 1933 1936 3. {ECO:0000269|PubMed:8255760}.
REPEAT 1961 1964 4. {ECO:0000269|PubMed:8255760}.
REPEAT 2024 2027 5. {ECO:0000269|PubMed:8255760}.
ZN_FING 185 207 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 213 235 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 633 663 CCHC HIVEP-type. {ECO:0000255|PROSITE-
ProRule:PRU01154}.
ZN_FING 1720 1742 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1748 1772 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 185 235 ZAS1.
REGION 204 1055 No DNA binding activity or
transactivation activity, but complete
prevention of TRAF-dependent NF-Kappa-B
activation; associates with TRAF2 and
JUN.
REGION 257 280 Acidic 1.
REGION 844 865 Acidic 2.
REGION 1720 1772 ZAS2.
REGION 1783 1841 Acidic 3.
REGION 2053 2148 5 X 4 AA tandem repeats of [ST]-P-X-[RK].
COILED 1409 1433 {ECO:0000255}.
MOTIF 885 891 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 301 327 Ser-rich.
COMPBIAS 371 407 Ser-rich.
COMPBIAS 780 802 Ser-rich.
COMPBIAS 826 862 Glu/Pro-rich.
COMPBIAS 898 930 Ser-rich.
COMPBIAS 1873 1902 Ser-rich.
CONFLICT 131 131 L -> S (in Ref. 2; AAR88090).
{ECO:0000305}.
CONFLICT 583 584 QP -> HA (in Ref. 2; AAR88090).
{ECO:0000305}.
CONFLICT 721 722 GS -> AC (in Ref. 2; AAR88090).
{ECO:0000305}.
CONFLICT 872 872 S -> T (in Ref. 2; AAR88090).
{ECO:0000305}.
CONFLICT 1129 1129 E -> Q (in Ref. 2; AAR88090).
{ECO:0000305}.
CONFLICT 1507 1507 K -> F (in Ref. 4; AAA40039).
{ECO:0000305}.
CONFLICT 1660 1660 L -> V (in Ref. 2; AAR88090 and 4;
AAA40039). {ECO:0000305}.
CONFLICT 1880 1880 Q -> E (in Ref. 2; AAR88090 and 4;
AAA40039). {ECO:0000305}.
CONFLICT 1944 1944 L -> V (in Ref. 2; AAR88090 and 4;
AAA40039). {ECO:0000305}.
CONFLICT 1994 1994 L -> P (in Ref. 2; AAR88090 and 4;
AAA40039). {ECO:0000305}.
CONFLICT 1998 1998 C -> R (in Ref. 2; AAR88090 and 4;
AAA40039). {ECO:0000305}.
CONFLICT 2014 2014 R -> P (in Ref. 4; AAA40039).
{ECO:0000305}.
CONFLICT 2105 2105 A -> G (in Ref. 2; AAR88090 and 4;
AAA40039). {ECO:0000305}.
SEQUENCE 2348 AA; 253413 MW; E226133774AD50C8 CRC64;
MDPDQSIKGT KKADGSPRKR LTKGEAIQTS VSSSAPYPGS GTTAPSESAT QELLATQPFS
GPSQEKTGQQ QKPARRPSIE ASVHISQLPQ HPLTPAFMSP GKPEHLLEGS TWQLVDPMRP
GPSGSFVAPG LHPQSQLLPS HASILPPEEL PGIPKVFVPR PSQVSLKPAE EAHKKERKPQ
KPGKYICQYC SRPCAKPSVL QKHIRSHTGE RPYPCGPCGF SFKTKSNLYK HRKSHAHRIK
AGLASGSSSE MYPPGLEMER IPGEEFEEPT EGESTDSEEE TGAASGPSTD VLPKPKHPLL
SSSLYSSGSH GSSQERCSLS QSSTGPSLED PAPFAEASSE HPLSHKPEDT HTIKQKLALR
LSERKKLIEE QTFLSPGSKG STESGYFSRS ESAEQQVSPP NTNAKSYAEI IFGKCGRIGQ
RTSMLASTST QPLLPLSSED KPSLVPLSVP RTQVIEHITK LITINEAVVD TSEIDSVKPR
RSSLTRRSSV ESPKSSLYRD SLSSHGEKTK QEQSLLSLQH PPSSTHPVPL LRSHSMPSAA
CTISTHHHTF RGSYSFDDHV ADPEVPSRNT PVFTSHPRML KRQPAIELPL GGEYSSEEPG
PSSKDPTSKP SDEPEPKESD LTKKTKKGFK TKGANYECTI CGARYKKRDN YEAHKKYYCS
ELQITKAHSV GAHEVEKTQA EPEPWSQMMH YKLGATLELT PLRKRRKEKS LGDEEEPPAF
GSPGPSETAH NRPLGSTKSP AEASKSAPSL EGPTSFQPRT PKPGAGSEPG KERRTMSKEI
SVIQHTSSFE KSDPPEQPSG LEEDKPPAQF SSPPPAPHGR SAHSLQPRLV RQPNIQVPEI
LVTEEPDRPD TEPEPPPKEP EKTEEFQWPQ RSQTLAQLPA EKLPPKKKRL RLAEMAQSSG
ESSFESSVPL SRSPSQESSI SLSGSSRSAS FDREDHGKAE APGPFSDTRS KTLGSHMLTV
PSHHPHAREM RRSASEQSPN VPHSSHMTET RSKSFDYGSL SPTGPSLAVP AAPPPPAAPP
ERRKCFLVRQ ASLNRPPEAE LEAVPKGKQE SSEEPAASKP STKSSVPQIS VGTTQGGPSG
GKSQMQDRPP LGSSPPYTEA LQVFQPLGTQ LPPPASLFSL QQLLPQEQEQ SSEFFPTQAM
AGLLSSPYSM PPLPPSLFQA PPLPLQPTVL HPSQLHLPQL LPHAADIPFQ QPPSFLPMPC
PAPSTLSGYF LPLQSQFALQ LPGEIESHLP PVKTSLPPLA TGPPGPSSST EYSSDIQLPP
VTPQATSPAP TSAPPLALPA CPDAMVSLVV PVRIQTHMPS YGSAMYTTLS QILVTQSPGS
PASTALTKYE EPSSKSMTVC EADVYEAEPG PSSISKEQNR GYQTPYLRVP ERKGTSLSSE
GILSLEGCSS TASGSKRVLS PAGSLELTME TQQQKRVKEE EASKADEKLE LVSTCSVVLT
STEDRKKTEK PHVGGQGRSR REAETLSSLS SDVSDPKELS PLSHSTLSHG TAPGSEALKE
YAQPSSKAHR RGLPPMSVKK EDPKEQTDLP PLAPPSSLPL SDTSPKPAKL QEGTDSKKVL
QFPSLHTTTN VSWCYLNYIK PNHIQHADRR SSVYAGWCIS LYNPNLPGVS TKAALSLLRS
KQKVSKETYT MATAPHPEAG RLVPSNSRKP RMTEVHLPSL VSPESQKDPA RVEKEEKQGK
AEEGTPTSKR GEPARVKIFE GGYKSNEEYI YVRGRGRGRY VCEECGIRCK KPSMLKKHIR
THTDVRPYVC KHCHFAFKTK GNLTKHMKSK AHSKKCQETG VLEELEAEEG TSDDLHQDSE
GQEGAEAVEE HQFSDLEDSD SDSDLDEDEE EEEEEEESQD ELSGPCSEAA PPCLPPTLQE
NSSPVEGPQA PDSTSDEVPQ GSSISEATHL TASSCSTPSR GTQGLPRLGL APLEKDMSSA
PSPKATSPRR PWSPSKEAGS RPSLTRKHSL TKNDSSPQQC SPAREAQASV TSTPGPQMGP
GRDLGPHLCG SPRLELSCLT PYPIGREAPA GLERATDTGT PRYSPTRRWS LGQAESPPQT
VLPGKWALAG PCSPSADKSG LGLGPVPRAL LQPVPLPHTL LSRSPETCTS AWRKTESRSP
SAGPAPLFPR PFSAPHDFHG HLPSRSEENL FSHLPLHSQL LSRAPCPLIP IGGIQMVQAR
PGAQPTVLPG PCAAWVSGFS GGGSDLTGAR EAQERSRWSP TESPSASVSP VAKVSKFTLS
SELEEERTGR GPGRPPDWEP HRAEAPPGPM GTHSPCSPQL PQGHQVAPSW RGLLGSPHTL
ANLKASSFPP LDRSSSMDCL AETSTYSPPR SRNLSGEPRT RQGSPELLGR GELRTPLFLP
KGSGPPSI


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EIAAB47034 Agie-bp1,Angiotensinogen gene-inducible enhancer-binding protein 1,DNA-binding protein AGIE-BP1,Hivep2,Human immunodeficiency virus type I enhancer-binding protein 2 homolog,Mibp1,MIBP-1,Myc intron-bi
EIAAB47036 Hivep2,Human immunodeficiency virus type I enhancer-binding protein 2 homolog,Mibp1,MIBP-1,Mouse,Mus musculus,Myc intron-binding protein 1,Transcription factor HIVEP2
EIAAB40542 CBF-1,Homo sapiens,Human,IGKJRB,IGKJRB1,J kappa-recombination signal-binding protein,RBPJ,RBP-J,RBP-J kappa,RBPJK,RBP-JK,RBPSUH,Recombining binding protein suppressor of hairless,Renal carcinoma antig
EIAAB40543 Bos taurus,Bovine,J kappa-recombination signal-binding protein,RBPJ,RBP-J kappa,RBPSUH,Recombining binding protein suppressor of hairless
EIAAB40541 Igkjrb1,Igkrsbp,J kappa-recombination signal-binding protein,Mouse,Mus musculus,Rbpj,RBP-J kappa,Rbpsuh,Recombining binding protein suppressor of hairless
18-003-42028 Recombining binding protein suppressor of hairless - J kappa-recombination signal-binding protein; RBP-J kappa; RBP-J; RBP-JK; CBF-1; NY-REN-30 antigen Polyclonal 0.05 mg Aff Pur
18-003-43011 Recombining binding protein suppressor of hairless - J kappa-recombination signal-binding protein; RBP-J kappa; RBP-J; RBP-JK; CBF-1; NY-REN-30 antigen Polyclonal 0.1 mg Protein A
20-372-60085 recombining binding protein suppressor of hairless (Drosophila) (RBPSUH) - Mouse monoclonal anti-human RBPSUH antibody; J kappa-recombination signal-binding protein; RBP-J kappa; RBP-J; RBP-JK; CBF-1; 0.1 mg
EIAAB47035 HIVEP2,HIV-EP2,Homo sapiens,Human,Human immunodeficiency virus type I enhancer-binding protein 2,MBP-2,MHC-binding protein 2,Transcription factor HIVEP2
HJURP HIVEP3 Gene human immunodeficiency virus type I enhancer binding protein 3
HIVEP3 HIVEP1 Gene human immunodeficiency virus type I enhancer binding protein 1
EIAAB47028 Rat,Rattus norvegicus,Tcf8,TCF-8,Transcription factor 8,Zeb1,Zfhep,Zinc finger E-box-binding homeobox 1,Zinc finger homeodomain enhancer-binding protein
EIAAB47360 GC-box-binding zinc finger protein 1,GZP1,Homo sapiens,Human,Transcription factor ZBP-99,ZBP99,Zinc finger DNA-binding protein 99,Zinc finger protein 281,ZNF281
EIAAB35961 FINB,Finger protein in nuclear bodies,Homo sapiens,Human,Raf-responsive zinc finger protein LZ321,Ras-responsive element-binding protein 1,RREB1,RREB-1,Zep-1,Zinc finger motif enhancer-binding protein
EIAAB47268 Beta enolase repressor factor 1,G-rich box-binding protein,Mouse,Mus musculus,Transcription factor BFCOL1,Transcription factor ZBP-89,Zbp89,Zfp148,Zinc finger DNA-binding protein 89,Zinc finger protei
EIAAB27094 DNA-binding protein R kappa-B,Homo sapiens,Human,INO80 complex subunit G,INO80G,NFRKB,Nuclear factor related to kappa-B-binding protein
EIAAB27093 DNA-binding protein R kappa-B,Mouse,Mus musculus,Nfrkb,Nuclear factor related to kappa-B-binding protein
EIAAB46626 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Homo sapiens,Human,NSEP1,Nuclease-sensitive element-binding protein 1,YB1,YB-1,Y-box t
CSB-EL010466HU Human human immunodeficiency virus type I enhancer binding protein 3 (HIVEP3) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL010466MO Mouse human immunodeficiency virus type I enhancer binding protein 3 (HIVEP3) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
EIAAB46625 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Mouse,Msy1,Msy-1,Mus musculus,Nsep1,Nuclease-sensitive element-binding protein 1,Yb1,Y


 

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