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

Basic leucine zipper 63 (AtbZIP63) (bZIP protein 63) (Basic leucine zipper OPAQUE 2 homolog 3) (Basic leucine zipper O2 homolog 3)

 BZP63_ARATH             Reviewed;         314 AA.
B9DGI8; F4KA11; Q712P1; Q940U4; Q9FUD2; Q9LKT9;
18-APR-2012, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 1.
25-OCT-2017, entry version 79.
RecName: Full=Basic leucine zipper 63;
Short=AtbZIP63;
Short=bZIP protein 63;
AltName: Full=Basic leucine zipper OPAQUE 2 homolog 3;
Short=Basic leucine zipper O2 homolog 3;
Name=BZIP63; Synonyms=BZO2H3; OrderedLocusNames=At5g28770;
ORFNames=T32B20.4;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia; TISSUE=Rosette leaf;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-191 (ISOFORM 1/3), AND GENE FAMILY.
STRAIN=cv. Columbia;
PubMed=12569427; DOI=10.1007/s00239-002-2386-1;
Vincentz M., Bandeira-Kobarg C., Gauer L., Schloegl P., Leite A.;
"Evolutionary pattern of angiosperm bZIP factors homologous to the
maize Opaque2 regulatory protein.";
J. Mol. Evol. 56:105-116(2003).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-314 (ISOFORM 1), TISSUE SPECIFICITY,
AND GENE FAMILY.
STRAIN=cv. Columbia;
PubMed=12657652; DOI=10.1074/jbc.M210538200;
Lara P., Onate-Sanchez L., Abraham Z., Ferrandiz C., Diaz I.,
Carbonero P., Vicente-Carbajosa J.;
"Synergistic activation of seed storage protein gene expression in
Arabidopsis by ABI3 and two bZIPs related to OPAQUE2.";
J. Biol. Chem. 278:21003-21011(2003).
[7]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11906833; DOI=10.1016/S1360-1385(01)02223-3;
Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
Tiedemann J., Kroj T., Parcy F.;
"bZIP transcription factors in Arabidopsis.";
Trends Plant Sci. 7:106-111(2002).
[8]
INTERACTION WITH LSD1.
PubMed=15469500; DOI=10.1111/j.1365-313X.2004.02219.x;
Walter M., Chaban C., Schuetze K., Batistic O., Weckermann K.,
Naeke C., Blazevic D., Grefen C., Schumacher K., Oecking C.,
Harter K., Kudla J.;
"Visualization of protein interactions in living plant cells using
bimolecular fluorescence complementation.";
Plant J. 40:428-438(2004).
[9]
INTERACTION WITH BZIP53.
PubMed=16810321; DOI=10.1038/sj.emboj.7601206;
Weltmeier F., Ehlert A., Mayer C.S., Dietrich K., Wang X.,
Schuetze K., Alonso R., Harter K., Vicente-Carbajosa J.,
Droege-Laser W.;
"Combinatorial control of Arabidopsis proline dehydrogenase
transcription by specific heterodimerisation of bZIP transcription
factors.";
EMBO J. 25:3133-3143(2006).
[10]
SUBCELLULAR LOCATION.
PubMed=16957775; DOI=10.1038/sj.emboj.7601312;
Kaminaka H., Naeke C., Epple P., Dittgen J., Schuetze K., Chaban C.,
Holt B.F. III, Merkle T., Schaefer E., Harter K., Dangl J.L.;
"bZIP10-LSD1 antagonism modulates basal defense and cell death in
Arabidopsis following infection.";
EMBO J. 25:4400-4411(2006).
[11]
SUBUNIT.
PubMed=16731568; DOI=10.1093/molbev/msl022;
Deppmann C.D., Alvania R.S., Taparowsky E.J.;
"Cross-species annotation of basic leucine zipper factor interactions:
Insight into the evolution of closed interaction networks.";
Mol. Biol. Evol. 23:1480-1492(2006).
[12]
INTERACTION WITH BZIP1; BZIP2; BZIP9; BZIP10; BZIP11; BZIP44 AND
BZIP53.
PubMed=16709202; DOI=10.1111/j.1365-313X.2006.02731.x;
Ehlert A., Weltmeier F., Wang X., Mayer C.S., Smeekens S.,
Vicente-Carbajosa J., Droege-Laser W.;
"Two-hybrid protein-protein interaction analysis in Arabidopsis
protoplasts: establishment of a heterodimerization map of group C and
group S bZIP transcription factors.";
Plant J. 46:890-900(2006).
[13]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY GLUCOSE.
STRAIN=cv. Columbia;
PubMed=18841482; DOI=10.1007/s11103-008-9410-9;
Weltmeier F., Rahmani F., Ehlert A., Dietrich K., Schuetze K.,
Wang X., Chaban C., Hanson J., Teige M., Harter K.,
Vicente-Carbajosa J., Smeekens S., Droege-Laser W.;
"Expression patterns within the Arabidopsis C/S1 bZIP transcription
factor network: availability of heterodimerization partners controls
gene expression during stress response and development.";
Plant Mol. Biol. 69:107-119(2009).
[14]
PHOSPHORYLATION, AND MUTAGENESIS OF SER-160; SER-164 AND SER-168.
PubMed=20047775; DOI=10.1016/j.ejcb.2009.11.023;
Kirchler T., Briesemeister S., Singer M., Schuetze K., Keinath M.,
Kohlbacher O., Vicente-Carbajosa J., Teige M., Harter K., Chaban C.;
"The role of phosphorylatable serine residues in the DNA-binding
domain of Arabidopsis bZIP transcription factors.";
Eur. J. Cell Biol. 89:175-183(2010).
[15]
INTERACTION WITH BZIP1; BZIP10 AND BZIP25, AND SUBUNIT.
PubMed=20080816; DOI=10.1093/mp/ssp115;
Kang S.G., Price J., Lin P.-C., Hong J.C., Jang J.-C.;
"The arabidopsis bZIP1 transcription factor is involved in sugar
signaling, protein networking, and DNA binding.";
Mol. Plant 3:361-373(2010).
-!- FUNCTION: Transcription factor. {ECO:0000250}.
-!- SUBUNIT: Homodimer. Forms a heterodimer with LSD1, BZIP1, BZIP2,
BZIP9, BZIP10, BZIP11, BZIP25, BZIP44 and BZIP53.
{ECO:0000269|PubMed:16709202, ECO:0000269|PubMed:16731568,
ECO:0000269|PubMed:16810321, ECO:0000269|PubMed:20080816}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-942713, EBI-942713;
C0SUZ3:At1g35490; NbExp=3; IntAct=EBI-15191817, EBI-15192249;
Q9FGX2:BZIP1; NbExp=4; IntAct=EBI-942713, EBI-942623;
O22763-3:BZIP10; NbExp=3; IntAct=EBI-15191817, EBI-15191815;
O65683:BZIP11; NbExp=4; IntAct=EBI-942713, EBI-942769;
Q9SI15:BZIP2; NbExp=4; IntAct=EBI-942713, EBI-942735;
C0Z2L5:BZIP44; NbExp=4; IntAct=EBI-942713, EBI-942804;
Q9LZP8:BZIP53; NbExp=8; IntAct=EBI-942713, EBI-942845;
O81002:bZIP6; NbExp=3; IntAct=EBI-15191817, EBI-3133475;
Q9SSE5:COL9; NbExp=3; IntAct=EBI-15191817, EBI-15197469;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978, ECO:0000269|PubMed:16957775}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=B9DGI8-1; Sequence=Displayed;
Name=2;
IsoId=B9DGI8-2; Sequence=VSP_042641;
Note=No experimental confirmation available.;
Name=3;
IsoId=B9DGI8-3; Sequence=VSP_042642, VSP_042643;
Note=Derived from EST data. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Expressed in roots, shoots, young leaves,
pollen, and flowers. {ECO:0000269|PubMed:12657652,
ECO:0000269|PubMed:18841482}.
-!- DEVELOPMENTAL STAGE: Present in silique valves, vasculature and
funiculi. {ECO:0000269|PubMed:18841482}.
-!- INDUCTION: Strongly repressed by glucose.
{ECO:0000269|PubMed:18841482}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:20047775}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF67360.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAC79656.1; 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; AF262041; AAF67360.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED93832.1; -; Genomic_DNA.
EMBL; CP002688; AED93833.1; -; Genomic_DNA.
EMBL; CP002688; AED93834.1; -; Genomic_DNA.
EMBL; AF446876; AAL38609.1; -; mRNA.
EMBL; AY052688; AAK96592.1; -; mRNA.
EMBL; AK317169; BAH19855.1; -; mRNA.
EMBL; AF310224; AAG25729.1; -; mRNA.
EMBL; AJ010858; CAC79656.1; ALT_INIT; mRNA.
RefSeq; NP_001031962.1; NM_001036885.2. [B9DGI8-3]
RefSeq; NP_568508.2; NM_122760.4. [B9DGI8-1]
RefSeq; NP_851088.1; NM_180757.3. [B9DGI8-2]
UniGene; At.15754; -.
ProteinModelPortal; B9DGI8; -.
SMR; B9DGI8; -.
BioGrid; 18262; 12.
IntAct; B9DGI8; 28.
STRING; 3702.AT5G28770.2; -.
iPTMnet; B9DGI8; -.
PaxDb; B9DGI8; -.
EnsemblPlants; AT5G28770.1; AT5G28770.1; AT5G28770. [B9DGI8-2]
EnsemblPlants; AT5G28770.2; AT5G28770.2; AT5G28770. [B9DGI8-1]
EnsemblPlants; AT5G28770.3; AT5G28770.3; AT5G28770. [B9DGI8-3]
GeneID; 832990; -.
Gramene; AT5G28770.1; AT5G28770.1; AT5G28770.
Gramene; AT5G28770.2; AT5G28770.2; AT5G28770.
Gramene; AT5G28770.3; AT5G28770.3; AT5G28770.
KEGG; ath:AT5G28770; -.
Araport; AT5G28770; -.
TAIR; locus:2184251; AT5G28770.
eggNOG; ENOG410IIE6; Eukaryota.
eggNOG; ENOG4111S51; LUCA.
HOGENOM; HOG000240492; -.
InParanoid; B9DGI8; -.
OMA; GNAMNRC; -.
OrthoDB; EOG09360JUP; -.
PhylomeDB; B9DGI8; -.
PRO; PR:B9DGI8; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; B9DGI8; baseline and differential.
Genevisible; B9DGI8; AT.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:TAIR.
GO; GO:0071215; P:cellular response to abscisic acid stimulus; IEP:TAIR.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.880.10; -; 1.
InterPro; IPR020983; Basic_leucine-zipper_C.
InterPro; IPR004827; bZIP.
InterPro; IPR008917; TF_DNA-bd.
Pfam; PF00170; bZIP_1; 1.
Pfam; PF12498; bZIP_C; 2.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; DNA-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation.
CHAIN 1 314 Basic leucine zipper 63.
/FTId=PRO_0000416560.
DOMAIN 151 214 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 153 172 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 179 193 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 155 162 Nuclear localization signal 1.
{ECO:0000250}.
MOTIF 295 302 Nuclear localization signal 2.
{ECO:0000250}.
VAR_SEQ 90 96 Missing (in isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_042641.
VAR_SEQ 227 250 MAEETVKRLTGFNPMFHNMPQIVS -> YFLLSLCLPKLAI
EACLFLAGENG (in isoform 3).
{ECO:0000305}.
/FTId=VSP_042642.
VAR_SEQ 251 314 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_042643.
MUTAGEN 160 160 S->A: Normal DNA-binding.
{ECO:0000269|PubMed:20047775}.
MUTAGEN 160 160 S->D: Reduced DNA-binding to C-box motif.
{ECO:0000269|PubMed:20047775}.
MUTAGEN 164 164 S->A: Normal DNA-binding.
{ECO:0000269|PubMed:20047775}.
MUTAGEN 164 164 S->D: Impaired DNA-binding to C-box
motif. {ECO:0000269|PubMed:20047775}.
MUTAGEN 168 168 S->A: Normal DNA-binding.
{ECO:0000269|PubMed:20047775}.
MUTAGEN 168 168 S->D: Impaired DNA-binding to C-box
motif. {ECO:0000269|PubMed:20047775}.
SEQUENCE 314 AA; 34311 MW; 37B85F20425DFF8B CRC64;
MEKVFSDEEI SGNHHWSVNG MTSLNRSASE WAFNRFIQES SAAADDGEST TACGVSVSSP
PNVPVDSEEY RAFLKSKLNL ACAAVAMKRG TFIKPQDTSG RSDNGGANES EQASLASSKA
TPMMSSAITS GSELSGDEEE ADGETNMNPT NVKRVKRMLS NRESARRSRR RKQAHLSELE
TQVSQLRVEN SKLMKGLTDV TQTFNDASVE NRVLKANIET LRAKVKMAEE TVKRLTGFNP
MFHNMPQIVS TVSLPSETSN SPDTTSSQVT TPEIISSGNK GKALIGCKMN RTASMRRVES
LEHLQKRIRS VGDQ


Related products :

Catalog number Product name Quantity
25-090 BATF is a nuclear basic leucine zipper protein that belongs to the AP-1_ATF superfamily of transcription factors. The leucine zipper of this protein mediates dimerization with members of the Jun famil 0.05 mg
27-516 D-site-binding protein (DBP) is a member of the PAR bZIP (proline and acidic amino acid-rich basic leucine zipper) transcription factor family. 0.05 mg
27-371 DBP is a member of the PAR bZIP (proline and acidic amino acid-rich basic leucine zipper) transcription factor family (Khatib et al., 1994. 0.05 mg
29-831 THOC4 is a heat stable, nuclear protein and functions as a molecular chaperone. It is thought to regulate dimerization, DNA binding, and transcriptional activity of basic region-leucine zipper (bZIP) 0.1 mg
28-990 MAFF is a basic leucine zipper (bZIP) transcription factor that lacks a transactivation domain. It is known to bind the US-2 DNA element in the promoter of the oxytocin receptor (OTR) gene and most li 0.1 mg
BZW1_RAT Rat ELISA Kit FOR Basic leucine zipper and W2 domain-containing protein 1 96T
28-160 CREB3L2 is a member of the old astrocyte specifically induced substance (OASIS) DNA binding and basic leucine zipper dimerization (bZIP) family of transcription factors, which includes CREB3 (MIM 6064 0.1 mg
27-921 MAFB is a basic leucine zipper (bZIP) transcription factor that plays an important role in the regulation of lineage-specific hematopoiesis. The nuclear protein represses ETS1-mediated transcription o 0.1 mg
27-922 MAFB is a basic leucine zipper (bZIP) transcription factor that plays an important role in the regulation of lineage-specific hematopoiesis. The nuclear protein represses ETS1-mediated transcription o 0.05 mg
28-768 BACH1 is a transcription factor that belongs to the cap'n'collar type of basic region leucine zipper factor family (CNC-bZip). The encoded protein contains broad complex, tramtrack, bric-a-brac_poxvir 0.1 mg
CSB-EL002898RA Rat Basic leucine zipper and W2 domain-containing protein 2(BZW2) ELISA kit 96T
CSB-EL002896RA Rat Basic leucine zipper and W2 domain-containing protein 1(BZW1) ELISA kit 96T
BZW1_MOUSE Mouse ELISA Kit FOR Basic leucine zipper and W2 domain-containing protein 1 96T
28-932 NFE2 (MIM 601490), NFE2L1 (MIM 163260), and NFE2L2 comprise a family of human genes encoding basic leucine zipper (bZIP) transcription factors. They share highly conserved regions that are distinct fr 0.1 mg
20-372-60050 BTB and CNC homology 1. basic leucine zipper transcription factor 1 - Mouse monoclonal anti-human BACH1 antibody; BTB and CNC homolog 1; HA2303 Monoclonal 0.1 mg
CSB-EL002898HU Human Basic leucine zipper and W2 domain-containing protein 2(BZW2) ELISA kit 96T
CSB-EL002896HU Human Basic leucine zipper and W2 domain-containing protein 1(BZW1) ELISA kit 96T
CSB-EL002896RA Rat Basic leucine zipper and W2 domain-containing protein 1(BZW1) ELISA kit SpeciesRat 96T
CSB-EL002898RA Rat Basic leucine zipper and W2 domain-containing protein 2(BZW2) ELISA kit SpeciesRat 96T
CSB-EL002898MO Mouse Basic leucine zipper and W2 domain-containing protein 2(BZW2) ELISA kit 96T
CSB-EL002896MO Mouse Basic leucine zipper and W2 domain-containing protein 1(BZW1) ELISA kit 96T
CSB-EL002896CH Chicken Basic leucine zipper and W2 domain-containing protein 1(BZW1) ELISA kit 96T
CSB-EL002898CH Chicken Basic leucine zipper and W2 domain-containing protein 2(BZW2) ELISA kit 96T
E2494h Human BTB And CNC Homology 1, Basic Leucine Zipper 96T
BZX BZW1 Gene basic leucine zipper and W2 domains 1


 

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