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

Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial (EC 1.4.7.1) (Fd-GOGAT 1)

 GLTB1_ARATH             Reviewed;        1622 AA.
Q9ZNZ7; P93649;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
29-MAY-2013, sequence version 3.
25-OCT-2017, entry version 167.
RecName: Full=Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial;
EC=1.4.7.1;
AltName: Full=Fd-GOGAT 1;
Flags: Precursor;
Name=GLU1; Synonyms=GLS1; OrderedLocusNames=At5g04140;
ORFNames=F21E1_60;
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 2).
STRAIN=cv. Columbia;
PubMed=9057836; DOI=10.1111/j.1432-1033.1997.00708.x;
Suzuki A., Rothstein S.;
"Structure and regulation of ferredoxin-dependent glutamase synthase
from Arabidopsis thaliana. Cloning of cDNA expression in different
tissues of wild-type and gltS mutant strains, and light induction.";
Eur. J. Biochem. 243:708-718(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND INDUCTION BY LIGHT AND SUGAR.
STRAIN=cv. Columbia;
PubMed=9596633; DOI=10.1105/tpc.10.5.741;
Coschigano K.T., Melo-Oliveira R., Lim J., Coruzzi G.M.;
"Arabidopsis gls mutants and distinct Fd-GOGAT genes. Implications for
photorespiration and primary nitrogen assimilation.";
Plant Cell 10:741-752(1998).
[3]
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).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=19555410; DOI=10.1111/j.1742-4658.2009.07114.x;
Potel F., Valadier M.H., Ferrario-Mery S., Grandjean O., Morin H.,
Gaufichon L., Boutet-Mercey S., Lothier J., Rothstein S.J., Hirose N.,
Suzuki A.;
"Assimilation of excess ammonium into amino acids and nitrogen
translocation in Arabidopsis thaliana--roles of glutamate synthases
and carbamoylphosphate synthetase in leaves.";
FEBS J. 276:4061-4076(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[7]
INTERACTION WITH SHM1, SUBCELLULAR LOCATION, DUAL TARGETING, FUNCTION,
MUTAGENESIS OF LEU-1270, AND DISRUPTION PHENOTYPE.
PubMed=19223513; DOI=10.1105/tpc.108.063289;
Jamai A., Salome P.A., Schilling S.H., Weber A.P., McClung C.R.;
"Arabidopsis photorespiratory serine hydroxymethyltransferase activity
requires the mitochondrial accumulation of ferredoxin-dependent
glutamate synthase.";
Plant Cell 21:595-606(2009).
[8]
FUNCTION.
PubMed=19468822; DOI=10.1007/s00726-009-0303-2;
Ishizaki T., Ohsumi C., Totsuka K., Igarashi D.;
"Analysis of glutamate homeostasis by overexpression of Fd-GOGAT gene
in Arabidopsis thaliana.";
Amino Acids 38:943-950(2010).
[9]
INDUCTION BY GATA21/GNC AND GATA22/CGA1.
PubMed=22102866; DOI=10.1371/journal.pone.0026765;
Hudson D., Guevara D., Yaish M.W., Hannam C., Long N., Clarke J.D.,
Bi Y.M., Rothstein S.J.;
"GNC and CGA1 modulate chlorophyll biosynthesis and glutamate synthase
(GLU1/Fd-GOGAT) expression in Arabidopsis.";
PLoS ONE 6:E26765-E26765(2011).
-!- FUNCTION: Involved in glutamate biosynthesis in leaf. Required for
the reassimilation of ammonium ions generated during
photorespiration. {ECO:0000269|PubMed:19223513,
ECO:0000269|PubMed:19468822, ECO:0000269|PubMed:19555410,
ECO:0000269|PubMed:9596633}.
-!- CATALYTIC ACTIVITY: 2 L-glutamate + 2 oxidized ferredoxin = L-
glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H(+).
-!- COFACTOR:
Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
Evidence={ECO:0000250};
Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
-!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
pathway; L-glutamate from 2-oxoglutarate and L-glutamine
(ferredoxin route): step 1/1.
-!- PATHWAY: Energy metabolism; nitrogen metabolism.
-!- SUBUNIT: Interacts with SHM1. {ECO:0000269|PubMed:19223513}.
-!- INTERACTION:
Q9SZJ5:SHM1; NbExp=2; IntAct=EBI-2292564, EBI-2292536;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Mitochondrion
matrix. Note=Dual targeting is supposed to depend on alternative
initiation: MET-1 or MET-3 for chloroplast or mitochondrion
location, respectively. {ECO:0000269|PubMed:19223513}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Short;
IsoId=Q9ZNZ7-1; Sequence=Displayed;
Name=2; Synonyms=Long;
IsoId=Q9ZNZ7-2; Sequence=VSP_046513;
Note=May be due to an intron retention. No experimental
confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in leaves. High expression in
the leaf mesophyll and phloem companion cell-sieve element
complex. {ECO:0000269|PubMed:19555410,
ECO:0000269|PubMed:9596633}.
-!- INDUCTION: Up-regulated by GATA21/GNC and GATA22/CGA1. Induced by
light or sucrose. {ECO:0000269|PubMed:22102866,
ECO:0000269|PubMed:9596633}.
-!- DISRUPTION PHENOTYPE: Displays photorespiratory chlorosis when
grown at ambient CO2. {ECO:0000269|PubMed:19223513}.
-!- SIMILARITY: Belongs to the glutamate synthase family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y09667; CAA70862.1; -; mRNA.
EMBL; U39287; AAC78551.1; -; mRNA.
EMBL; AL391716; CAC05496.1; -; Genomic_DNA.
EMBL; CP002688; AED90703.1; -; Genomic_DNA.
EMBL; CP002688; AED90704.1; -; Genomic_DNA.
RefSeq; NP_568134.1; NM_120496.3. [Q9ZNZ7-1]
RefSeq; NP_850763.1; NM_180432.2. [Q9ZNZ7-2]
UniGene; At.21961; -.
UniGene; At.67926; -.
ProteinModelPortal; Q9ZNZ7; -.
SMR; Q9ZNZ7; -.
BioGrid; 15572; 4.
IntAct; Q9ZNZ7; 2.
STRING; 3702.AT5G04140.2; -.
MEROPS; C44.951; -.
iPTMnet; Q9ZNZ7; -.
PaxDb; Q9ZNZ7; -.
PRIDE; Q9ZNZ7; -.
EnsemblPlants; AT5G04140.1; AT5G04140.1; AT5G04140. [Q9ZNZ7-1]
EnsemblPlants; AT5G04140.2; AT5G04140.2; AT5G04140. [Q9ZNZ7-2]
GeneID; 830292; -.
Gramene; AT5G04140.1; AT5G04140.1; AT5G04140.
Gramene; AT5G04140.2; AT5G04140.2; AT5G04140.
KEGG; ath:AT5G04140; -.
Araport; AT5G04140; -.
TAIR; locus:2146718; AT5G04140.
eggNOG; KOG0399; Eukaryota.
eggNOG; COG0067; LUCA.
eggNOG; COG0069; LUCA.
eggNOG; COG0070; LUCA.
HOGENOM; HOG000031558; -.
InParanoid; Q9ZNZ7; -.
KO; K00284; -.
OMA; PKFYLVK; -.
BioCyc; ARA:AT5G04140-MONOMER; -.
BRENDA; 1.4.7.1; 399.
UniPathway; UPA00045; -.
UniPathway; UPA00634; UER00691.
PRO; PR:Q9ZNZ7; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9ZNZ7; baseline and differential.
Genevisible; Q9ZNZ7; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0016041; F:glutamate synthase (ferredoxin) activity; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019676; P:ammonia assimilation cycle; IBA:GO_Central.
GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009853; P:photorespiration; IMP:TAIR.
GO; GO:0080114; P:positive regulation of glycine hydroxymethyltransferase activity; IDA:TAIR.
GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
CDD; cd00982; gltB_C; 1.
CDD; cd02808; GltS_FMN; 1.
Gene3D; 2.160.20.60; -; 1.
Gene3D; 3.20.20.70; -; 2.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR017932; GATase_2_dom.
InterPro; IPR002489; Glu_synth_asu_C.
InterPro; IPR036485; Glu_synth_asu_C_sf.
InterPro; IPR006982; Glu_synth_centr_N.
InterPro; IPR002932; Glu_synthdom.
InterPro; IPR029055; Ntn_hydrolases_N.
Pfam; PF00310; GATase_2; 1.
Pfam; PF04898; Glu_syn_central; 1.
Pfam; PF01645; Glu_synthase; 1.
Pfam; PF01493; GXGXG; 1.
SUPFAM; SSF56235; SSF56235; 1.
SUPFAM; SSF69336; SSF69336; 1.
PROSITE; PS51278; GATASE_TYPE_2; 1.
1: Evidence at protein level;
3Fe-4S; Alternative splicing; Amino-acid biosynthesis; Chloroplast;
Complete proteome; FAD; Flavoprotein; FMN; Glutamate biosynthesis;
Glutamine amidotransferase; Iron; Iron-sulfur; Metal-binding;
Mitochondrion; Oxidoreductase; Plastid; Reference proteome;
Transit peptide.
TRANSIT 1 105 Chloroplast and mitochondrion.
{ECO:0000255}.
CHAIN 106 1622 Ferredoxin-dependent glutamate synthase
1, chloroplastic/mitochondrial.
/FTId=PRO_0000011614.
DOMAIN 106 505 Glutamine amidotransferase type-2.
{ECO:0000255|PROSITE-ProRule:PRU00609}.
NP_BIND 1184 1241 FMN. {ECO:0000250}.
ACT_SITE 106 106 For GATase activity. {ECO:0000250}.
METAL 1237 1237 Iron-sulfur (3Fe-4S). {ECO:0000250}.
METAL 1243 1243 Iron-sulfur (3Fe-4S). {ECO:0000250}.
METAL 1248 1248 Iron-sulfur (3Fe-4S). {ECO:0000250}.
VAR_SEQ 92 92 Q -> QVRFFTDINFTNTQRAKFHPLWGSFKQ (in
isoform 2). {ECO:0000303|PubMed:9057836}.
/FTId=VSP_046513.
MUTAGEN 1270 1270 L->F: In glu1-201; Abolishes interaction
with SHM1. Displays photorespiratory
chlorosis when grown at ambient CO2.
{ECO:0000269|PubMed:19223513}.
CONFLICT 96 96 L -> W (in Ref. 2; AAC78551).
{ECO:0000305}.
CONFLICT 211 211 G -> R (in Ref. 2; AAC78551).
{ECO:0000305}.
CONFLICT 385 385 S -> C (in Ref. 1; CAA70862).
{ECO:0000305}.
CONFLICT 621 624 EGLV -> KVWF (in Ref. 1; CAA70862).
{ECO:0000305}.
CONFLICT 734 734 A -> T (in Ref. 1; CAA70862).
{ECO:0000305}.
CONFLICT 1473 1474 IF -> DI (in Ref. 1; CAA70862).
{ECO:0000305}.
CONFLICT 1585 1585 E -> K (in Ref. 2; AAC78551).
{ECO:0000305}.
SEQUENCE 1622 AA; 176752 MW; FAE7D097490F8A97 CRC64;
MAMQSLSPVP KLLSTTPSSV LSSDKNFFFV DFVGLYCKSK RTRRRLRGDS SSSSRSSSSL
SRLSSVRAVI DLERVHGVSE KDLSSPSALR PQVANLEDIL SERGACGVGF IANLDNIPSH
GVVKDALIAL GCMEHRGGCG ADNDSGDGSG LMSSIPWDFF NVWAKEQSLA PFDKLHTGVG
MIFLPQDDTF MQEAKQVIEN IFEKEGLQVL GWREVPVNVP IVGKNARETM PNIQQVFVKI
AKEDSTDDIE RELYICRKLI ERAVATESWG TELYFCSLSN QTIVYKGMLR SEALGLFYLD
LQNELYESPF AIYHRRYSTN TSPRWPLAQP MRFLGHNGEI NTIQGNLNWM QSREASLKAA
VWNGRENEIR PFGNPRGSDS ANLDSAAEIM IRSGRTPEEA LMILVPEAYK NHPTLSVKYP
EVVDFYDYYK GQMEAWDGPA LLLFSDGKTV GACLDRNGLR PARYWRTSDN FVYVASEVGV
VPVDEAKVTM KGRLGPGMMI AVDLVNGQVY ENTEVKKRIS SFNPYGKWIK ENSRFLKPVN
FKSSTVMENE EILRSQQAFG YSSEDVQMVI ESMASQGKEP TFCMGDDIPL AGLSQRPHML
YDYFKQRFAQ VTNPAIDPLR EGLVMSLEVN IGKRGNILEL GPENASQVIL SNPVLNEGAL
EELMKDQYLK PKVLSTYFDI RKGVEGSLQK ALYYLCEAAD DAVRSGSQLL VLSDRSDRLE
PTRPSIPIML AVGAVHQHLI QNGLRMSASI VADTAQCFST HHFACLVGYG ASAVCPYLAL
ETCRQWRLSN KTVAFMRNGK IPTVTIEQAQ KNYTKAVNAG LLKILSKMGI SLLSSYCGAQ
IFEIYGLGQD VVDLAFTGSV SKISGLTFDE LARETLSFWV KAFSEDTTKR LENFGFIQFR
PGGEYHSNNP EMSKLLHKAV REKSETAYAV YQQHLSNRPV NVLRDLLEFK SDRAPIPVGK
VEPAVAIVQR FCTGGMSLGA ISRETHEAIA IAMNRIGGKS NSGEGGEDPI RWKPLTDVVD
GYSPTLPHLK GLQNGDIATS AIKQVASGRF GVTPTFLVNA DQLEIKVAQG AKPGEGGQLP
GKKVSAYIAR LRSSKPGVPL ISPPPHHDIY SIEDLAQLIF DLHQINPNAK VSVKLVAEAG
IGTVASGVAK GNADIIQISG HDGGTGASPI SSIKHAGGPW ELGLTETHQT LIANGLRERV
ILRVDGGLKS GVDVLMAAAM GADEYGFGSL AMIATGCVMA RICHTNNCPV GVASQREELR
ARFPGVPGDL VNYFLYVAEE VRGILAQLGY NSLDDIIGRT ELLRPRDISL VKTQHLDLSY
LLSSVGTPSL SSTEIRKQEV HTNGPVLDDD ILADPLVIDA IENEKVVEKT VKICNVDRAA
CGRVAGVIAK KYGDTGFAGQ VNLTFLGSAG QSFGCFLIPG MNIRLIGESN DYVGKGMAGG
EIVVTPVEKI GFVPEEATIV GNTCLYGATG GQIFARGKAG ERFAVRNSLA EAVVEGTGDH
CCEYMTGGCV VVLGKVGRNV AAGMTGGLAY LLDEDDTLLP KINREIVKIQ RVTAPAGELQ
LKSLIEAHVE KTGSSKGATI LNEWEKYLPL FWQLVPPSEE DTPEASAAYV RTSTGEVTFQ
SA


Related products :

Catalog number Product name Quantity
AS11 1757 Antibody: Fd | ferredoxin 1 (chloroplastic), Immunogen: KLH-conjugated synthetic peptide derived from known C-terminal part of Chlamydomonas reinhardtii chloroplastic ferredoxin P07839, Host: rabbit, 200
AS07 242 Glutamate Synthase (GOGAT) 0.2 ml
AS07242 Glutamate Synthase (GOGAT) 0.2 ml
AS07 242 Glutamate Synthase (GOGAT) 0.2 ml
'AS07 242 Glutamate Synthase (GOGAT) antibody Ab host: Rabbit 0.2 ml
'AS07 242 Glutamate Synthase (GOGAT) antibody Host rabbit 0.2 mg
20312449-1 Fd | ferredoxin 1 (chloroplastic) (rabbi 200 uL
AS11 1757 rabbit polyclonal Fd | ferredoxin 1 (chloroplastic) 200
AS07 242 Antibody: GOGAT | glutamine oxoglutarate aminotransferase, Immunogen: KLH-conjugated synthetic peptide well conserved in known GOGAT sequences from different species including Arabidopsis thaliana Fd- 200
30-375 ATP5B is a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosph 0.1 mg
30-374 ATP5B is a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosph 0.1 mg
26-294 ATP5F1 is a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosp 0.05 mg
20312203-1 FeSOD | chloroplastic Fe-dependent super 200 uL
AS09 579 ATP synthase subunit III_c, chloroplastic 100 ul
AS06 125 rabbit polyclonal FeSOD | chloroplastic Fe-dependent superoxide dismutase 200
abx109165 Polyclonal Rabbit ATP synthase subunit beta, chloroplastic Antibody (HRP) 100 μg
CSB-RP139994Pl Recombinant Lemna minor ATP synthase subunit beta, chloroplastic 500ug
15-288-22653 Hydroxymethylglutaryl-CoA synthase. mitochondrial - EC 2.3.3.10; HMG-CoA synthase; 3-hydroxy-3-methylglutaryl coenzyme A synthase Polyclonal 0.1 mg
18-003-44261 Hydroxymethylglutaryl-CoA synthase. mitochondrial - EC 2.3.3.10; HMG-CoA synthase; 3-hydroxy-3-methylglutaryl coenzyme A synthase Polyclonal 0.1 mg Protein A
15-288-22653 Hydroxymethylglutaryl-CoA synthase. mitochondrial - EC 2.3.3.10; HMG-CoA synthase; 3-hydroxy-3-methylglutaryl coenzyme A synthase Polyclonal 0.05 mg
abx106334 Polyclonal Rabbit ATP synthase subunit beta, chloroplastic Antibody (Biotin) 100 μg
abx107747 Polyclonal Rabbit ATP synthase subunit beta, chloroplastic Antibody (FITC) 100 μg
AS14 2782 rabbit polyclonal EPSP synthase | 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic 50
CSB-RP139994Pl Recombinant Lemna minor ATP synthase subunit beta, chloroplastic Source: E.coli 1mg
CSB-EL027234PL Plant solanesyl diphosphate synthase 2, chloroplastic(SPS2_SPPS)ELISA kit , Species , Sample Type 96T


 

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