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Krueppel-like factor 5 (Basic transcription element-binding protein 2) (BTE-binding protein 2) (Colon krueppel-like factor) (GC-box-binding protein 2) (Intestinal-enriched krueppel-like factor) (Transcription factor BTEB2)

 KLF5_HUMAN              Reviewed;         457 AA.
Q13887; A2TJX0; L0R3U5; L0R4T9; Q9UHP8;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
25-OCT-2017, entry version 169.
RecName: Full=Krueppel-like factor 5;
AltName: Full=Basic transcription element-binding protein 2;
Short=BTE-binding protein 2;
AltName: Full=Colon krueppel-like factor;
AltName: Full=GC-box-binding protein 2;
AltName: Full=Intestinal-enriched krueppel-like factor;
AltName: Full=Transcription factor BTEB2;
Name=KLF5; Synonyms=BTEB2, CKLF, IKLF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10572182; DOI=10.1093/nar/27.24.4807;
Shi H., Zhang Z., Wang X., Liu S., Teng C.T.;
"Isolation and characterization of a gene encoding human Kruppel-like
factor 5 (IKLF): binding to the CAAT/GT box of the mouse lactoferrin
gene promoter.";
Nucleic Acids Res. 27:4807-4815(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND ALTERNATIVE
SPLICING.
PubMed=23134681; DOI=10.1096/fj.12-220319;
Camacho-Vanegas O., Till J., Miranda-Lorenzo I., Ozturk B.,
Camacho S.C., Martignetti J.A.;
"Shaking the family tree: Identification of novel and biologically
active alternatively spliced isoforms across the KLF family of
transcription factors.";
FASEB J. 27:432-436(2013).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Ohnishi S., Yoshida T., Ramirez F., Terada M., Friedrich L.;
"Human basic transcription element binding protein 2.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Sur I., Unden A.-B., Toftgard R.;
"Human Kruppel like factor5/KLF5: expression in human skin and hair
follicles.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Dong X., Guo P., Dong J.;
"Functional identification testis-specific transcript of Kruppel-like
factor 5 (tKLF5).";
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Testis;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Placenta;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 239-457 (ISOFORM 1).
TISSUE=Placenta;
PubMed=8479902; DOI=10.1093/nar/21.7.1527;
Sogawa K., Imataka H., Yamasaki Y., Kusume H., Abe H.,
Fujii-Kuriyama Y.;
"cDNA cloning and transcriptional properties of a novel GC box-binding
protein, BTEB2.";
Nucleic Acids Res. 21:1527-1532(1993).
[11]
SUBCELLULAR LOCATION, INTERACTION WITH WWP1, UBIQUITINATION, AND
MUTAGENESIS OF 324-PRO--TYR-328.
PubMed=15735697; DOI=10.1038/sj.onc.1208497;
Chen C., Sun X., Ran Q., Wilkinson K.D., Murphy T.J., Simons J.W.,
Dong J.T.;
"Ubiquitin-proteasome degradation of KLF5 transcription factor in
cancer and untransformed epithelial cells.";
Oncogene 24:3319-3327(2005).
[12]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-52; LYS-94 AND
LYS-110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[13]
STRUCTURE BY NMR OF 363-457.
RIKEN structural genomics initiative (RSGI);
"Solution structure of three tandem repeats of ZF-C2H2 domains from
human kruppel-like factor 5.";
Submitted (FEB-2008) to the PDB data bank.
[14]
VARIANT [LARGE SCALE ANALYSIS] SER-301.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Transcription factor that binds to GC box promoter
elements. Activates the transcription of these genes.
-!- SUBUNIT: Interacts with WWP1. {ECO:0000269|PubMed:15735697}.
-!- INTERACTION:
P0CG48:UBC; NbExp=2; IntAct=EBI-2696013, EBI-3390054;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15735697}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q13887-1; Sequence=Displayed;
Name=2;
IsoId=Q13887-2; Sequence=VSP_047474;
Name=3;
IsoId=Q13887-3; Sequence=VSP_047475, VSP_047476;
Name=4;
IsoId=Q13887-4; Sequence=VSP_057567;
-!- TISSUE SPECIFICITY: Expressed only in testis and placenta.
-!- PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to
proteasomal degradation of this protein.
{ECO:0000269|PubMed:15735697}.
-!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/KLF5ID41074ch13q21.html";
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EMBL; AF132818; AAF18307.1; -; mRNA.
EMBL; HF546203; CCO02789.1; -; mRNA.
EMBL; HF546204; CCO02790.1; -; mRNA.
EMBL; AB030824; BAA96461.1; -; mRNA.
EMBL; AF287272; AAF88068.1; -; mRNA.
EMBL; EF208215; ABM97548.1; -; mRNA.
EMBL; AK302280; BAG63623.1; -; mRNA.
EMBL; AL354720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471093; EAW80526.1; -; Genomic_DNA.
EMBL; BC007695; AAH07695.1; -; mRNA.
EMBL; BC042131; AAH42131.1; -; mRNA.
EMBL; D14520; BAA03393.1; -; mRNA.
CCDS; CCDS66562.1; -. [Q13887-4]
CCDS; CCDS9448.1; -. [Q13887-1]
PIR; S35643; S35643.
RefSeq; NP_001273747.1; NM_001286818.1. [Q13887-4]
RefSeq; NP_001721.2; NM_001730.4. [Q13887-1]
UniGene; Hs.508234; -.
PDB; 2EBT; NMR; -; A=365-457.
PDBsum; 2EBT; -.
ProteinModelPortal; Q13887; -.
SMR; Q13887; -.
BioGrid; 107153; 50.
IntAct; Q13887; 5.
MINT; MINT-3028757; -.
STRING; 9606.ENSP00000366915; -.
BindingDB; Q13887; -.
ChEMBL; CHEMBL1293249; -.
iPTMnet; Q13887; -.
PhosphoSitePlus; Q13887; -.
DMDM; 12644412; -.
EPD; Q13887; -.
PaxDb; Q13887; -.
PeptideAtlas; Q13887; -.
PRIDE; Q13887; -.
DNASU; 688; -.
Ensembl; ENST00000377687; ENSP00000366915; ENSG00000102554. [Q13887-1]
Ensembl; ENST00000539231; ENSP00000440407; ENSG00000102554. [Q13887-4]
GeneID; 688; -.
KEGG; hsa:688; -.
UCSC; uc001vjd.5; human.
CTD; 688; -.
DisGeNET; 688; -.
EuPathDB; HostDB:ENSG00000102554.13; -.
GeneCards; KLF5; -.
HGNC; HGNC:6349; KLF5.
HPA; HPA040398; -.
MIM; 602903; gene.
neXtProt; NX_Q13887; -.
OpenTargets; ENSG00000102554; -.
PharmGKB; PA30139; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00760000118998; -.
HOGENOM; HOG000261607; -.
HOVERGEN; HBG003474; -.
InParanoid; Q13887; -.
KO; K09206; -.
OMA; MPNQFLQ; -.
OrthoDB; EOG091G1BN0; -.
PhylomeDB; Q13887; -.
TreeFam; TF350556; -.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
SignaLink; Q13887; -.
SIGNOR; Q13887; -.
ChiTaRS; KLF5; human.
EvolutionaryTrace; Q13887; -.
GeneWiki; KLF5; -.
GenomeRNAi; 688; -.
PRO; PR:Q13887; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000102554; -.
CleanEx; HS_CKLF; -.
CleanEx; HS_KLF5; -.
ExpressionAtlas; Q13887; baseline and differential.
Genevisible; Q13887; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
GO; GO:0060576; P:intestinal epithelial cell development; IEA:Ensembl.
GO; GO:0030033; P:microvillus assembly; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0032534; P:regulation of microvillus assembly; IEA:Ensembl.
GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR030401; KLF5.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR44295:SF4; PTHR44295:SF4; 1.
SMART; SM00355; ZnF_C2H2; 3.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 457 Krueppel-like factor 5.
/FTId=PRO_0000047169.
ZN_FING 373 397 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 403 427 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 433 455 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 324 328 Interaction with WWP1.
{ECO:0000269|PubMed:15735697}.
CROSSLNK 31 31 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 52 52 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 94 94 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 110 110 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 91 Missing (in isoform 4).
/FTId=VSP_057567.
VAR_SEQ 88 239 Missing (in isoform 2).
{ECO:0000303|PubMed:23134681}.
/FTId=VSP_047474.
VAR_SEQ 105 166 IIPEHKKYRRDSASVVDQFFTDTEGLPYSINMNVFLPDITH
LRTGLYKSQRPCVTHIKTEPV -> MLLQLLLNWQFTIQIY
PPPCQLTHKTSNLSDTIEGVTPIWRNDASTTAITLVAQKFI
PSLLI (in isoform 3).
{ECO:0000303|PubMed:23134681}.
/FTId=VSP_047475.
VAR_SEQ 167 457 Missing (in isoform 3).
{ECO:0000303|PubMed:23134681}.
/FTId=VSP_047476.
VARIANT 301 301 P -> S (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035555.
MUTAGEN 324 328 Missing: Impairs ubiquitination and
degradation.
{ECO:0000269|PubMed:15735697}.
STRAND 377 379 {ECO:0000244|PDB:2EBT}.
STRAND 383 385 {ECO:0000244|PDB:2EBT}.
HELIX 387 397 {ECO:0000244|PDB:2EBT}.
STRAND 407 409 {ECO:0000244|PDB:2EBT}.
STRAND 413 416 {ECO:0000244|PDB:2EBT}.
HELIX 417 427 {ECO:0000244|PDB:2EBT}.
STRAND 436 438 {ECO:0000244|PDB:2EBT}.
HELIX 445 455 {ECO:0000244|PDB:2EBT}.
SEQUENCE 457 AA; 50792 MW; 3BF12BE272716E57 CRC64;
MATRVLSMSA RLGPVPQPPA PQDEPVFAQL KPVLGAANPA RDAALFPGEE LKHAHHRPQA
QPAPAQAPQP AQPPATGPRL PPEDLVQTRC EMEKYLTPQL PPVPIIPEHK KYRRDSASVV
DQFFTDTEGL PYSINMNVFL PDITHLRTGL YKSQRPCVTH IKTEPVAIFS HQSETTAPPP
APTQALPEFT SIFSSHQTAA PEVNNIFIKQ ELPTPDLHLS VPTQQGHLYQ LLNTPDLDMP
SSTNQTAAMD TLNVSMSAAM AGLNTHTSAV PQTAVKQFQG MPPCTYTMPS QFLPQQATYF
PPSPPSSEPG SPDRQAEMLQ NLTPPPSYAA TIASKLAIHN PNLPTTLPVN SQNIQPVRYN
RRSNPDLEKR RIHYCDYPGC TKVYTKSSHL KAHLRTHTGE KPYKCTWEGC DWRFARSDEL
TRHYRKHTGA KPFQCGVCNR SFSRSDHLAL HMKRHQN


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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
EIAAB46624 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Msy-1,Nsep1,Nuclease-sensitive element-binding protein 1,Rat,Rattus norvegicus,Yb1,YB-
EIAAB46627 Bos taurus,Bovine,CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,NSEP1,Nuclease-sensitive element-binding protein 1,YB1,YB-1,Y-box tr
EIAAB46629 CBF-A,CCAAT-binding transcription factor I subunit A,EFI-A,Enhancer factor I subunit A,NSEP1,Nuclease-sensitive element-binding protein 1,Oryctolagus cuniculus,p50,Rabbit,YB1,YB-1,Y-box transcription
EIAAB25653 Homo sapiens,hPCl2,Human,Metal regulatory transcription factor 2,Metal-response element DNA-binding protein M96,Metal-response element-binding transcription factor 2,MTF2,PCL2,Polycomb-like protein 2
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
EIAAB25652 Metal regulatory transcription factor 2,Metal-response element DNA-binding protein M96,Metal-response element-binding transcription factor 2,Mouse,mPCl2,Mtf2,Mus musculus,Pcl2,Polycomb-like protein 2,
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
EIAAB41697 Homo sapiens,Human,KIAA0292,Nuclear factor SPBP,Protein AR1,SPBP,SPRE-binding protein,Stromelysin-1 PDGF-responsive element-binding protein,TCF20,TCF-20,Transcription factor 20
10-782-55004 Cyclic AMP-dependent transcription factor ATF-2 - Activating transcription factor 2; cAMP response element-binding protein CRE-BP1; HB16 N_A 0.2 mg
10-782-55004 Cyclic AMP-dependent transcription factor ATF-2 - Activating transcription factor 2; cAMP response element-binding protein CRE-BP1; HB16 N_A 0.05 mg
18-662-20064 Cyclic AMP-dependent transcription factor ATF-2 - Activating transcription factor 2; cAMP response element-binding protein CRE-BP1; HB16 Polyclonal 0.1 ml
18-003-42489 Cyclic AMP-dependent transcription factor ATF-2 - Activating transcription factor 2; cAMP response element-binding protein CRE-BP1; HB16 Polyclonal 0.1 mg Protein A
31-197 GA Binding Protein . chain (GABP-. subunit, GABPA, nuclear respiratory factor-2 subunit . transcription factor E4TF1-60) is one of three GA-binding protein transcription factor subunits which function 0.1 mg


 

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