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 10 (AtbZIP10) (bZIP protein 10) (Basic leucine zipper OPAQUE 2 homolog 1) (Basic leucine zipper O2 homolog 1)

 BZP10_ARATH             Reviewed;         411 AA.
O22763; C0Z2B4; Q8RXJ3; Q9FUD4;
18-APR-2012, integrated into UniProtKB/Swiss-Prot.
01-JAN-1999, sequence version 2.
22-NOV-2017, entry version 130.
RecName: Full=Basic leucine zipper 10;
Short=AtbZIP10;
Short=bZIP protein 10;
AltName: Full=Basic leucine zipper OPAQUE 2 homolog 1;
Short=Basic leucine zipper O2 homolog 1;
Name=BZIP10; Synonyms=BZO2H1; OrderedLocusNames=At4g02640;
ORFNames=T10P11.9;
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 [MRNA] (ISOFORM 1), FUNCTION, DEVELOPMENTAL STAGE,
TISSUE SPECIFICITY, INTERACTION WITH ABI3, 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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia; TISSUE=Root;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-411 (ISOFORM 1).
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=cv. Columbia;
Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[9]
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).
[10]
FUNCTION, AND 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).
[11]
FUNCTION IN DEFENSE RESPONSES HYALOPERONOSPORA PARASITICA, SUBCELLULAR
LOCATION, AND INTERACTION WITH LSD1.
STRAIN=cv. Columbia;
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).
[12]
INTERACTION WITH BZIP1; BZIP2; BZIP9; BZIP11; BZIP44; BZIP53 AND
BZIP63.
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]
FUNCTION, AND INTERACTION WITH BZIP53 AND ABI3.
PubMed=19531597; DOI=10.1105/tpc.108.062968;
Alonso R., Onate-Sanchez L., Weltmeier F., Ehlert A., Diaz I.,
Dietrich K., Vicente-Carbajosa J., Droege-Laser W.;
"A pivotal role of the basic leucine zipper transcription factor
bZIP53 in the regulation of Arabidopsis seed maturation gene
expression based on heterodimerization and protein complex
formation.";
Plant Cell 21:1747-1761(2009).
[14]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
[15]
FUNCTION, AND INTERACTION WITH BZIP53.
PubMed=19261733; DOI=10.1104/pp.109.136531;
Roschzttardtz H., Fuentes I., Vasquez M., Corvalan C., Leon G.,
Gomez I., Araya A., Holuigue L., Vicente-Carbajosa J., Jordana X.;
"A nuclear gene encoding the iron-sulfur subunit of mitochondrial
complex II is regulated by B3 domain transcription factors during seed
development in Arabidopsis.";
Plant Physiol. 150:84-95(2009).
[16]
INTERACTION WITH BZIP1 AND BZIP63.
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 that binds to the C-box-like motif
(5'-TGCTGACGTCA-3') and G-box-like motif (5'-CCACGTGGCC-3'), ABRE
elements, of gene promoters. Binds to the 5'-ACGT-3' motif of seed
storage protein (SSP) encoding gene promoters (e.g. At2S and CRU3)
and promotes their expression in seeds when in complex with ABI3
and BZIP53. Involved in the defense responses to the biotrophic
pathogen Hyaloperonospora parasitica and oxidative stress
responses; mediates positively cell death (PubMed:12657652,
PubMed:16957775, PubMed:19261733, PubMed:19531597). Promotes
BZIP53-mediated response to hypoosmolarity stress that leads to
POX1/PRODH1 accumulation (PubMed:16810321).
{ECO:0000269|PubMed:12657652, ECO:0000269|PubMed:16810321,
ECO:0000269|PubMed:16957775, ECO:0000269|PubMed:19261733,
ECO:0000269|PubMed:19531597}.
-!- SUBUNIT: Forms a heterodimer with BZIP1, BZIP2, BZIP9, BZIP11,
BZIP44, BZIP53 and BZIP63. Interacts with ABI3 and forms a complex
made of ABI3, BZIP53 and BZIP10. Binding with LSD1 leads to
cytoplasmic retention. {ECO:0000269|PubMed:12657652,
ECO:0000269|PubMed:16709202, ECO:0000269|PubMed:16810321,
ECO:0000269|PubMed:16957775, ECO:0000269|PubMed:19261733,
ECO:0000269|PubMed:19531597, ECO:0000269|PubMed:20080816}.
-!- INTERACTION:
Q9FGX2:BZIP1; NbExp=3; IntAct=EBI-942648, EBI-942623;
O65683:BZIP11; NbExp=3; IntAct=EBI-942648, EBI-942769;
Q9SI15:BZIP2; NbExp=3; IntAct=EBI-942648, EBI-942735;
C0Z2L5:BZIP44; NbExp=3; IntAct=EBI-942648, EBI-942804;
Q9LZP8:BZIP53; NbExp=8; IntAct=EBI-942648, EBI-942845;
B9DGI8-2:BZIP63; NbExp=3; IntAct=EBI-15191815, EBI-15191817;
Q9SFV2:FHA2; NbExp=3; IntAct=EBI-15191815, EBI-15191747;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978, ECO:0000269|PubMed:16957775}. Cytoplasm
{ECO:0000269|PubMed:16957775}. Note=Shuttles between the nucleus
and the cytoplasm. Retained outside the nucleus by LSD1 to prevent
cell death.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O22763-1; Sequence=Displayed;
Name=2;
IsoId=O22763-2; Sequence=VSP_042640;
Note=No experimental confirmation available.;
Name=3;
IsoId=O22763-3; Sequence=VSP_042639;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in roots, shoots, stems, young
leaves, trichomes, hydathodes, siliques, seeds, and flowers,
mostly in vascular tissues. {ECO:0000269|PubMed:12657652,
ECO:0000269|PubMed:18841482}.
-!- DEVELOPMENTAL STAGE: First observed in carpels and seeds at early
stages of development, mostly in embryo and, at lower extent, in
the endosperm. Accumulates and peaks at maturation. Fade out
during late seed development steps, restricted to the inner layer
of the seed coat, and, at very low levels, in the mature embryo
and the remaining endosperm. Also present in the lignified inner
subepidermal layer of the valves. In the anthers, restricted to
the connective tissue at pre- and post-dehiscence stages and
detected in the vascular tissue of the stamen filament.
{ECO:0000269|PubMed:12657652, ECO:0000269|PubMed:18841482}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ010859; CAC79657.1; -; mRNA.
EMBL; AF310222; AAG25727.1; -; mRNA.
EMBL; AC002330; AAC78255.1; -; Genomic_DNA.
EMBL; AL161494; CAB80757.1; -; Genomic_DNA.
EMBL; CP002687; AEE82207.1; -; Genomic_DNA.
EMBL; CP002687; AEE82208.1; -; Genomic_DNA.
EMBL; CP002687; ANM67475.1; -; Genomic_DNA.
EMBL; AK318728; BAH56843.1; -; mRNA.
EMBL; AY080854; AAL87327.1; -; mRNA.
EMBL; BT025558; ABF58976.1; -; mRNA.
EMBL; AY088417; AAM65954.1; -; mRNA.
PIR; T01085; T01085.
RefSeq; NP_001329303.1; NM_001340390.1. [O22763-2]
RefSeq; NP_192173.1; NM_116498.4. [O22763-1]
RefSeq; NP_849290.1; NM_178959.3. [O22763-3]
UniGene; At.25176; -.
ProteinModelPortal; O22763; -.
BioGrid; 13508; 12.
IntAct; O22763; 22.
STRING; 3702.AT4G02640.2; -.
iPTMnet; O22763; -.
PaxDb; O22763; -.
EnsemblPlants; AT4G02640.1; AT4G02640.1; AT4G02640. [O22763-1]
EnsemblPlants; AT4G02640.2; AT4G02640.2; AT4G02640. [O22763-3]
EnsemblPlants; AT4G02640.4; AT4G02640.4; AT4G02640. [O22763-2]
GeneID; 828219; -.
Gramene; AT4G02640.1; AT4G02640.1; AT4G02640.
Gramene; AT4G02640.2; AT4G02640.2; AT4G02640.
Gramene; AT4G02640.4; AT4G02640.4; AT4G02640.
KEGG; ath:AT4G02640; -.
Araport; AT4G02640; -.
TAIR; locus:2132372; AT4G02640.
eggNOG; ENOG410JW8E; Eukaryota.
eggNOG; ENOG4110561; LUCA.
HOGENOM; HOG000240492; -.
InParanoid; O22763; -.
OMA; GQNDFED; -.
PhylomeDB; O22763; -.
PRO; PR:O22763; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; O22763; baseline and differential.
Genevisible; O22763; AT.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
GO; GO:2000693; P:positive regulation of seed maturation; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0002240; P:response to molecule of oomycetes origin; IMP:TAIR.
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_sf.
Pfam; PF00170; bZIP_1; 1.
Pfam; PF12498; bZIP_C; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; DNA-binding;
Hypersensitive response; Nucleus; Phosphoprotein; Plant defense;
Reference proteome; Seed storage protein; Storage protein;
Transcription; Transcription regulation.
CHAIN 1 411 Basic leucine zipper 10.
/FTId=PRO_0000416558.
DOMAIN 215 278 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 217 236 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 243 257 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 219 226 Nuclear localization signal.
{ECO:0000250}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000250|UniProtKB:Q9M1G6}.
VAR_SEQ 164 164 Q -> QGSLMTP (in isoform 3).
{ECO:0000303|PubMed:12569427,
ECO:0000303|Ref.7}.
/FTId=VSP_042639.
VAR_SEQ 406 411 Missing (in isoform 2).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_042640.
SEQUENCE 411 AA; 45358 MW; 9C651436D8D167CF CRC64;
MNSIFSIDDF SDPFWETPPI PLNPDSSKPV TADEVSQSQP EWTFEMFLEE ISSSAVSSEP
LGNNNNAIVG VSSAQSLPSV SGQNDFEDDS RFRDRDSGNL DCAAPMTTKT VIVDSDDYRR
VLKNKLETEC ATVVSLRVGS VKPEDSTSSP ETQLQPVQSS PLTQGELGVT SSLPAEVKKT
GVSMKQVTSG SSREYSDDED LDEENETTGS LKPEDVKKSR RMLSNRESAR RSRRRKQEQT
SDLETQVNDL KGEHSSLLKQ LSNMNHKYDE AAVGNRILKA DIETLRAKVK MAEETVKRVT
GMNPMLLGRS SGHNNNNRMP ITGNNRMDSS SIIPAYQPHS NLNHMSNQNI GIPTILPPRL
GNNFAAPPSQ TSSPLQRIRN GQNHHVTPSA NPYGWNTEPQ NDSAWPKKCV D


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