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

Linoleate 9S-lipoxygenase 1 (EC 1.13.11.58) (Lipoxygenase 1) (AtLOX1)

 LOX1_ARATH              Reviewed;         859 AA.
Q06327; Q9FZ30;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
07-JUN-2017, entry version 145.
RecName: Full=Linoleate 9S-lipoxygenase 1;
EC=1.13.11.58;
AltName: Full=Lipoxygenase 1;
Short=AtLOX1;
Name=LOX1; OrderedLocusNames=At1g55020;
ORFNames=F14C21.3, F14C21.54, T24C10.13;
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], INDUCTION BY ABA; JA AND PATHOGEN, AND
TISSUE SPECIFICITY.
STRAIN=cv. Columbia; TISSUE=Root;
PubMed=7506426; DOI=10.1104/pp.101.2.441;
Melan M.A., Dong X., Endara M.E., Davis K.R., Ausubel F.M.,
Peterman T.K.;
"An Arabidopsis thaliana lipoxygenase gene can be induced by
pathogens, abscisic acid, and methyl jasmonate.";
Plant Physiol. 101:441-450(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
PubMed=8305494; DOI=10.1016/0005-2760(94)90244-5;
Melan M.A., Nemhauser J.M., Peterman T.K.;
"Structure and sequence of the Arabidopsis thaliana lipoxygenase 1
gene.";
Biochim. Biophys. Acta 1210:377-380(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[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].
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).
[6]
TISSUE SPECIFICITY, INDUCTION BY LIGHT, AND DEVELOPMENTAL STAGE.
PubMed=12232208; DOI=10.1104/pp.105.1.385;
Melan M.A., Enriquez A.L.D., Peterman T.K.;
"The LOX1 gene of Arabidopsis is temporally and spatially regulated in
germinating seedlings.";
Plant Physiol. 105:385-393(1994).
[7]
TISSUE SPECIFICITY.
Peterman T.K., Rattigan E.M., Enriquez A., Melan M.A.;
"Immunological characterization of Arabidopsis thaliana lipoxygenase:
Expression of the LOX1 gene product in Escherichia coli and polyclonal
antibody production.";
Plant Physiol. Biochem. 32:443-450(1994).
[8]
DEVELOPMENTAL STAGE.
PubMed=11891244; DOI=10.1104/pp.010843;
He Y., Fukushige H., Hildebrand D.F., Gan S.;
"Evidence supporting a role of jasmonic acid in Arabidopsis leaf
senescence.";
Plant Physiol. 128:876-884(2002).
[9]
FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=17369372; DOI=10.1105/tpc.106.046052;
Vellosillo T., Martinez M., Lopez M.A., Vicente J., Cascon T.,
Dolan L., Hamberg M., Castresana C.;
"Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis
regulate lateral root development and defense responses through a
specific signaling cascade.";
Plant Cell 19:831-846(2007).
[10]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18949503; DOI=10.1007/s11745-008-3245-7;
Bannenberg G., Martinez M., Hamberg M., Castresana C.;
"Diversity of the enzymatic activity in the lipoxygenase gene family
of Arabidopsis thaliana.";
Lipids 44:85-95(2009).
-!- FUNCTION: 9S-lipoxygenase that can use linoleic acid or linolenic
acid as substrates. Plant lipoxygenases may be involved in a
number of diverse aspects of plant physiology including growth and
development, pest resistance, and senescence or responses to
wounding. Catalyzes the hydroperoxidation of lipids containing a
cis,cis-1,4-pentadiene structure. Function as regulators of root
development by controlling the emergence of lateral roots.
{ECO:0000269|PubMed:17369372, ECO:0000269|PubMed:18949503}.
-!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9S,10E,12Z)-9-hydroperoxy-
10,12-octadecadienoate. {ECO:0000269|PubMed:17369372,
ECO:0000269|PubMed:18949503}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00726};
Note=Binds 1 Fe cation per subunit. Iron is tightly bound.
{ECO:0000255|PROSITE-ProRule:PRU00726};
-!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
{ECO:0000255|PROSITE-ProRule:PRU00726}.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Seedlings, roots, leaves, and flowers (at
protein level). {ECO:0000269|PubMed:12232208,
ECO:0000269|PubMed:17369372, ECO:0000269|PubMed:7506426,
ECO:0000269|Ref.7}.
-!- DEVELOPMENTAL STAGE: Transiently expressed during germination,
within 1 day after imbibition, especially in the epidermis and the
aleurone layer. Later present in the epidermis of the radicle and
the adaxial side of the cotyledons. In roots, confined to the
pericycle cells and in the lateral root primordia (LRP), and
declined at the time of lateral root emergence. Expression is
greatly increased in leaves during leaf senescence.
{ECO:0000269|PubMed:11891244, ECO:0000269|PubMed:12232208,
ECO:0000269|PubMed:17369372}.
-!- INDUCTION: By pathogens (e.g. Pseudomonas syringae), wounding,
abscisic acid (ABA) and methyl jasmonate (MeJA). Higher levels in
light than in dark conditions. {ECO:0000269|PubMed:12232208,
ECO:0000269|PubMed:7506426}.
-!- DISRUPTION PHENOTYPE: Increment in the number of lateral roots,
and moderate increase in the length of the primary root.
{ECO:0000269|PubMed:17369372}.
-!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L04637; AAA32827.1; -; mRNA.
EMBL; U01843; AAA17036.1; -; Genomic_DNA.
EMBL; AC064840; AAG00881.1; -; Genomic_DNA.
EMBL; AC069144; AAG51123.1; -; Genomic_DNA.
EMBL; CP002684; AEE33175.1; -; Genomic_DNA.
EMBL; AY093104; AAM13103.1; -; mRNA.
EMBL; BT010358; AAQ56801.1; -; mRNA.
PIR; JQ2267; JQ2267.
RefSeq; NP_175900.1; NM_104376.3.
UniGene; At.19984; -.
UniGene; At.67309; -.
ProteinModelPortal; Q06327; -.
SMR; Q06327; -.
BioGrid; 27169; 1.
MINT; MINT-8068008; -.
STRING; 3702.AT1G55020.1; -.
PaxDb; Q06327; -.
PRIDE; Q06327; -.
EnsemblPlants; AT1G55020.1; AT1G55020.1; AT1G55020.
GeneID; 841944; -.
Gramene; AT1G55020.1; AT1G55020.1; AT1G55020.
KEGG; ath:AT1G55020; -.
Araport; AT1G55020; -.
TAIR; locus:2011030; AT1G55020.
eggNOG; ENOG410IH0D; Eukaryota.
eggNOG; ENOG410YN4N; LUCA.
HOGENOM; HOG000230469; -.
InParanoid; Q06327; -.
KO; K15718; -.
OMA; LEIWHAI; -.
OrthoDB; EOG093601GX; -.
PhylomeDB; Q06327; -.
BRENDA; 1.13.11.58; 399.
Reactome; R-ATH-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-ATH-2142696; Synthesis of Hepoxilins (HX) and Trioxilins (TrX).
Reactome; R-ATH-2142700; Synthesis of Lipoxins (LX).
Reactome; R-ATH-2142712; Synthesis of 12-eicosatetraenoic acid derivatives.
Reactome; R-ATH-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
Reactome; R-ATH-6798695; Neutrophil degranulation.
UniPathway; UPA00382; -.
PRO; PR:Q06327; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; Q06327; AT.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
GO; GO:0034440; P:lipid oxidation; IDA:TAIR.
GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
GO; GO:0048364; P:root development; IMP:TAIR.
Gene3D; 2.60.60.20; -; 1.
Gene3D; 4.10.372.10; -; 1.
InterPro; IPR000907; LipOase.
InterPro; IPR013819; LipOase_C.
InterPro; IPR020834; LipOase_CS.
InterPro; IPR020833; LipOase_Fe_BS.
InterPro; IPR001246; LipOase_plant.
InterPro; IPR027433; Lipoxygenase_domain_3.
InterPro; IPR001024; PLAT/LH2_dom.
PANTHER; PTHR11771; PTHR11771; 1.
Pfam; PF00305; Lipoxygenase; 1.
Pfam; PF01477; PLAT; 1.
PRINTS; PR00087; LIPOXYGENASE.
PRINTS; PR00468; PLTLPOXGNASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF48484; SSF48484; 1.
SUPFAM; SSF49723; SSF49723; 1.
PROSITE; PS00711; LIPOXYGENASE_1; 1.
PROSITE; PS00081; LIPOXYGENASE_2; 1.
PROSITE; PS51393; LIPOXYGENASE_3; 1.
PROSITE; PS50095; PLAT; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Dioxygenase; Fatty acid biosynthesis;
Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism;
Metal-binding; Oxidoreductase; Oxylipin biosynthesis;
Reference proteome.
CHAIN 1 859 Linoleate 9S-lipoxygenase 1.
/FTId=PRO_0000220703.
DOMAIN 21 161 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
DOMAIN 164 859 Lipoxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 519 519 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 524 524 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 711 711 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 715 715 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00726}.
METAL 859 859 Iron; via carboxylate; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00726}.
SEQUENCE 859 AA; 98045 MW; 49378EBACD5FF579 CRC64;
MFGELRDLLT GGGNETTTKK VKGTVVLMKK NVLDFNDFNA SFLDRLHEFL GNKITLRLVS
SDVTDSENGS KGKLGKAAHL EDWITTITSL TAGESAFKVT FDYETDFGYP GAFLIRNSHF
SEFLLKSLTL EDVPGHGRVH YICNSWIYPA KHYTTDRVFF SNKTYLPHET PATLLKYREE
ELVSLRGTGE GELKEWDRVY DYAYYNDLGV PPKNPRPVLG GTQEYPYPRR GRTGRKPTKE
DPQTESRLPI TSSLDIYVPR DERFGHLKMS DFLAYALKAI AQFIQPALEA VFDDTPKEFD
SFEDVLKIYE EGIDLPNQAL IDSIVKNIPL EMLKEIFRTD GQKFLKFPVP QVIKEDKTAW
RTDEEFAREM LAGLNPVVIQ LLKEFPPKSK LDSESYGNQN STITKSHIEH NLDGLTVEEA
LEKERLFILD HHDTLMPYLG RVNTTTTKTY ASRTLLFLKD DGTLKPLVIE LSLPHPNGDK
FGAVSEVYTP GEGVYDSLWQ LAKAFVGVND SGNHQLISHW MQTHASIEPF VIATNRQLSV
LHPVFKLLEP HFRDTMNINA LARQILINGG GIFEITVFPS KYAMEMSSFI YKNHWTFPDQ
ALPAELKKRG MAVEDPEAPH GLRLRIKDYP YAVDGLEVWY AIESWVRDYI FLFYKIEEDI
QTDTELQAWW KEVREEGHGD KKSEPWWPKM QTREELVESC TIIIWVASAL HAAVNFGQYP
VAGYLPNRPT ISRQYMPKEN TPEFEELEKN PDKVFLKTIT AQLQTLLGIS LIEILSTHSS
DEVYLGQRDS KEWAAEKEAL EAFEKFGEKV KEIEKNIDER NDDETLKNRT GLVKMPYTLL
FPSSEGGVTG RGIPNSVSI


Related products :

Catalog number Product name Quantity
U1356m CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,8S-lipoxygenase,8S-LOX,Alox15b,Alox8,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Mouse,Mus musculus 96T
E1356m ELISA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,8S-lipoxygenase,8S-LOX,Alox15b,Alox8,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Mouse,Mus musculus 96T
E1356m ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,8S-lipoxygenase,8S-LOX,Alox15b,Alox8,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Mouse,Mus musculus 96T
U0891Rb CLIA 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Erythroid cell-specific 15-lipoxygenase,Omega-6 lipoxygenase,Oryctolagus cuniculus,Rabbit 96T
E0891Rb ELISA 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Erythroid cell-specific 15-lipoxygenase,Omega-6 lipoxygenase,Oryctolagus cuniculus,Rabbit 96T
E0891Rb ELISA kit 15-LOX,ALOX15,Arachidonate 15-lipoxygenase,Erythroid cell-specific 15-lipoxygenase,Omega-6 lipoxygenase,Oryctolagus cuniculus,Rabbit 96T
E1965h ELISA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
U1965h CLIA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
E1965h ELISA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
U1965h CLIA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Homo sapiens,Human,LOG12,Platelet-type lipoxygenase 12 96T
U1965m CLIA kit 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
E1965m ELISA 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
E1965m ELISA kit 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
U1965m CLIA 12S-lipoxygenase,12S-LOX,Alox12,Alox12p,Arachidonate 12-lipoxygenase, 12S-type,Mouse,Mus musculus,Platelet-type lipoxygenase 12 96T
U1356h CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human 96T
E1356h ELISA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human 96T
E1356h ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,ALOX15B,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Homo sapiens,Human 96T
E1356r ELISA kit 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus 96T
E1356r ELISA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus 96T
U1356r CLIA 15-lipoxygenase 2,15-LOX-2,15-LOX-B,Alox15b,Arachidonate 15-lipoxygenase B,Arachidonate 15-lipoxygenase type II,Rat,Rattus norvegicus 96T
U1965b CLIA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
U1965b CLIA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
E1965b ELISA 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
E1965b ELISA kit 12S-lipoxygenase,12S-LOX,ALOX12,Arachidonate 12-lipoxygenase, 12S-type,Bos taurus,Bovine 96T
U1355m CLIA 5-lipoxygenase,5-LO,Alox5,Arachidonate 5-lipoxygenase,Mouse,Mus musculus 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