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

Peroxygenase 1 (AtPXG1) (EC 1.11.2.3) (Caleosin-1) (Embryo-specific protein 1 (ATS1))

 PXG1_ARATH              Reviewed;         245 AA.
O81270; Q8VZS4;
22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
27-SEP-2017, entry version 98.
RecName: Full=Peroxygenase 1;
Short=AtPXG1;
EC=1.11.2.3;
AltName: Full=Caleosin-1;
AltName: Full=Embryo-specific protein 1 (ATS1);
Name=PXG1; Synonyms=ATS1, CLO1; OrderedLocusNames=At4g26740;
ORFNames=F10M23.80;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=cv. Landsberg erecta;
PubMed=10380802; DOI=10.1023/A:1006101404867;
Nuccio M.L., Thomas T.L.;
"ATS1 and ATS3: two novel embryo-specific genes in Arabidopsis
thaliana.";
Plant Mol. Biol. 39:1153-1163(1999).
[2]
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).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
PROTEIN SEQUENCE OF N-TERMINUS, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT GLY-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=21751352; DOI=10.1002/pmic.201000603;
Vermachova M., Purkrtova Z., Santrucek J., Jolivet P., Chardot T.,
Kodicek M.;
"New protein isoforms identified within Arabidopsis thaliana seed oil
bodies combining chymotrypsin/trypsin digestion and peptide
fragmentation analysis.";
Proteomics 11:3430-3434(2011).
[6]
GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=11197322; DOI=10.1023/A:1026564411918;
Naested H., Frandsen G.I., Jauh G.Y., Hernandez-Pinzon I.,
Nielsen H.B., Murphy D.J., Rogers J.C., Mundy J.;
"Caleosins: Ca2+-binding proteins associated with lipid bodies.";
Plant Mol. Biol. 44:463-476(2000).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16961733; DOI=10.1111/j.1365-313X.2006.02845.x;
Poxleitner M., Rogers S.W., Lacey Samuels A., Browse J., Rogers J.C.;
"A role for caleosin in degradation of oil-body storage lipid during
seed germination.";
Plant J. 47:917-933(2006).
[8]
CATALYTIC ACTIVITY, MUTAGENESIS OF THR-15; HIS-52; HIS-59; HIS-70;
ASP-75; ASN-109; THR-116; HIS-131; HIS-134; HIS-138; LYS-196; CYS-221
AND CYS-230, CALCIUM-BINDING, ENZYME REGULATION, AND SUBUNIT.
PubMed=16956885; DOI=10.1074/jbc.M605395200;
Hanano A., Burcklen M., Flenet M., Ivancich A., Louwagie M., Garin J.,
Blee E.;
"Plant seed peroxygenase is an original heme-oxygenase with an EF-hand
calcium binding motif.";
J. Biol. Chem. 281:33140-33151(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-225,
DISULFIDE BOND, AND SUBUNIT.
PubMed=17582382; DOI=10.1016/j.abb.2007.04.041;
Purkrtova Z., d'Andrea S., Jolivet P., Lipovova P., Kralova B.,
Kodicek M., Chardot T.;
"Structural properties of caleosin: a MS and CD study.";
Arch. Biochem. Biophys. 464:335-343(2007).
[10]
CALCIUM-BINDING.
PubMed=19012406; DOI=10.1021/jf802305b;
Purkrtova Z., Le Bon C., Kralova B., Ropers M.H., Anton M.,
Chardot T.;
"Caleosin of Arabidopsis thaliana: effect of calcium on functional and
structural properties.";
J. Agric. Food Chem. 56:11217-11224(2008).
-!- FUNCTION: Calcium-binding peroxygenase involved in the degradation
of storage lipid in oil bodies. May be involved in the interaction
between oil bodies and vacuoles during seed germination and in the
oxylipin signaling pathways and plant defense responses. Can
catalyze sulfoxidation of thiobenzamide, hydroxylation of aniline,
epoxidation of oleic acid or intramolecular oxygen transfer.
{ECO:0000269|PubMed:16961733}.
-!- CATALYTIC ACTIVITY: RH + ROOH = ROH + ROH.
{ECO:0000269|PubMed:16956885}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group.;
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
-!- ENZYME REGULATION: Inhibited by beta-mercaptoethanol and the
organophosphorothioate terbufos. {ECO:0000269|PubMed:16956885}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16956885,
ECO:0000269|PubMed:17582382}.
-!- SUBCELLULAR LOCATION: Microsome membrane
{ECO:0000269|PubMed:11197322}. Lipid droplet
{ECO:0000269|PubMed:11197322}.
-!- TISSUE SPECIFICITY: Expressed in seeds. Expression restricted to
the developing embryo with enhanced expression in both the
protoderm and vasculature. Detected in root tip cells throughout
development. {ECO:0000269|PubMed:10380802,
ECO:0000269|PubMed:11197322}.
-!- DEVELOPMENTAL STAGE: Expressed during the early-to-late cotyledon
stage of seed maturation. {ECO:0000269|PubMed:10380802,
ECO:0000269|PubMed:11197322}.
-!- INDUCTION: Not induced by abscisic acid or osmotic stress.
{ECO:0000269|PubMed:11197322}.
-!- DOMAIN: The proline-knot motif (118-127) may be involved in
targeting to lipid bodies.
-!- DOMAIN: Transmembrane regions are predicted by sequence analysis
tools, but these regions probably constitute hydrophobic domains
associated to phospholipids.
-!- PTM: Phosphorylated. Partially phosphorylated at Ser-225, but not
phosphorylated at Ser-72, Tyr-145, Thr-166 or Ser-172.
Phosphorylation is not required for catalytic activity.
{ECO:0000269|PubMed:17582382}.
-!- DISRUPTION PHENOTYPE: No visible phenotype, but retarded growth
during the first 48 hours after germination.
{ECO:0000269|PubMed:16961733}.
-!- SIMILARITY: Belongs to the caleosin family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF067857; AAC27072.1; -; Genomic_DNA.
EMBL; AL035440; CAB36520.1; -; Genomic_DNA.
EMBL; AL161565; CAB79529.1; -; Genomic_DNA.
EMBL; CP002687; AEE85247.1; -; Genomic_DNA.
EMBL; AY063885; AAL36241.1; -; mRNA.
PIR; T04797; T04797.
RefSeq; NP_194404.1; NM_118808.5.
UniGene; At.27433; -.
ProteinModelPortal; O81270; -.
SMR; O81270; -.
BioGrid; 14068; 1.
STRING; 3702.AT4G26740.1; -.
iPTMnet; O81270; -.
PaxDb; O81270; -.
PRIDE; O81270; -.
EnsemblPlants; AT4G26740.1; AT4G26740.1; AT4G26740.
GeneID; 828781; -.
Gramene; AT4G26740.1; AT4G26740.1; AT4G26740.
KEGG; ath:AT4G26740; -.
Araport; AT4G26740; -.
TAIR; locus:2116427; AT4G26740.
eggNOG; ENOG410IVG5; Eukaryota.
eggNOG; ENOG4111R51; LUCA.
HOGENOM; HOG000217500; -.
InParanoid; O81270; -.
KO; K17991; -.
OMA; ILLWPED; -.
OrthoDB; EOG09360L7L; -.
PhylomeDB; O81270; -.
BioCyc; MetaCyc:MONOMER-15999; -.
PRO; PR:O81270; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; O81270; baseline and differential.
Genevisible; O81270; AT.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IDA:TAIR.
GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:TAIR.
GO; GO:0071614; F:linoleic acid epoxygenase activity; IDA:TAIR.
GO; GO:0004497; F:monooxygenase activity; IDA:TAIR.
GO; GO:1990137; F:plant seed peroxidase activity; IEA:UniProtKB-EC.
GO; GO:0006952; P:defense response; TAS:TAIR.
GO; GO:0009793; P:embryo development ending in seed dormancy; TAS:TAIR.
GO; GO:0034389; P:lipid particle organization; IDA:TAIR.
GO; GO:0031408; P:oxylipin biosynthetic process; IDA:TAIR.
InterPro; IPR007736; Caleosin-related.
PANTHER; PTHR31495; PTHR31495; 1.
Pfam; PF05042; Caleosin; 1.
1: Evidence at protein level;
Acetylation; Calcium; Complete proteome; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Heme; Iron; Lipid droplet;
Membrane; Metal-binding; Microsome; Oxidoreductase; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:21751352}.
CHAIN 2 245 Peroxygenase 1.
/FTId=PRO_0000415552.
DOMAIN 62 97 EF-hand.
CA_BIND 75 86 {ECO:0000255}.
MOTIF 118 127 Proline-knot.
METAL 70 70 Iron (heme axial ligand).
MOD_RES 2 2 N-acetylglycine.
{ECO:0000269|PubMed:21751352}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000269|PubMed:17582382}.
DISULFID 221 230 {ECO:0000269|PubMed:17582382}.
MUTAGEN 15 15 T->V: No effect on molecular weight; when
associated with V-109 and V-116.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 52 52 H->V: No effect on activity.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 59 59 H->V: No effect on activity.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 70 70 H->V: Total loss of activity.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 75 75 D->V: No effect on activity.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 109 109 N->V: No effect on molecular weight; when
associated with V-15 and V-116.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 116 116 T->V: No effect on molecular weight; when
associated with V-15 and V-109.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 131 131 H->V: No effect on activity.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 134 134 H->V: No effect on activity.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 138 138 H->V: Decreased heme binding and total
loss of activity.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 196 196 K->V: No effect on molecular weight.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 221 221 C->G: No effect on activity.
{ECO:0000269|PubMed:16956885}.
MUTAGEN 230 230 C->G: No effect on activity.
{ECO:0000269|PubMed:16956885}.
CONFLICT 145 145 Y -> H (in Ref. 4; AAL36241).
{ECO:0000305}.
SEQUENCE 245 AA; 28038 MW; A30BF01D51F54346 CRC64;
MGSKTEMMER DAMATVAPYA PVTYHRRARV DLDDRLPKPY MPRALQAPDR EHPYGTPGHK
NYGLSVLQQH VSFFDIDDNG IIYPWETYSG LRMLGFNIIG SLIIAAVINL TLSYATLPGW
LPSPFFPIYI HNIHKSKHGS DSKTYDNEGR FMPVNLELIF SKYAKTLPDK LSLGELWEMT
EGNRDAWDIF GWIAGKIEWG LLYLLARDEE GFLSKEAIRR CFDGSLFEYC AKIYAGISED
KTAYY


Related products :

Catalog number Product name Quantity
EIAAB27875 Mouse,Mus musculus,Nck-interacting kinase-like embryo specific kinase,NESK,Nesk,NIK-like embryo-specific kinase,Nik-related protein kinase,Nrk
EIAAB26416 EBS,Embryo brain-specific protein,Homo sapiens,Human,N-acetyltransferase 9,NAT9
EIAAB28855 C6orf156,hOEP19,Homo sapiens,Human,KH homology domain-containing protein 2,KHDC2,OEP19,Oocyte- and embryo-specific protein 19,Oocyte-expressed protein homolog,OOEP
EIAAB44932 HMG-box preimplantation embryo-specific protein,HMGPI,Hmgpi,Mouse,Mus musculus,Ubtfl1,Upstream-binding factor 1-like protein 1
EIAAB28856 Factor located in oocytes permitting embryonic development,Floped,mOEP19,Mouse,Mus musculus,Oep19,Oocyte- and embryo-specific protein 19,Oocyte-expressed protein homolog,Ooep,Sddr,STAT3 downstream gen
EIAAB26356 Early embryo specific expression NK-type homeobox protein,Ecat4,Enk,ES cell-associated protein 4,Homeobox protein NANOG,Homeobox transcription factor Nanog,Mouse,Mus musculus,Nanog
EIAAB28857 Canis familiaris,Canis lupus familiaris,dOEP19,Dog,OEP19,Oocyte- and embryo-specific protein 19,Oocyte-expressed protein,OOEP
EIAAB37769 Homeobox OG-9,Homeobox protein SEBOX,Og9x,Rat,Rattus norvegicus,Sebox,Skin-, embryo-, brain- and oocyte-specific homeobox
EIAAB37771 Homeobox OG-9,Homeobox protein SEBOX,Mouse,Mus musculus,Og9x,Sebox,Skin-, embryo-, brain- and oocyte-specific homeobox
EIAAB37770 Homeobox OG-9,Homeobox protein SEBOX,Homo sapiens,Human,OG9X,SEBOX,Skin-, embryo-, brain- and oocyte-specific homeobox
EIAAB12951 Endou,Mouse,Mus musculus,Placental protein 11-related protein,Poly(U)-specific endoribonuclease,Pp11r,PP11-related protein,Protein endoU,T-cell-specific protein 30,Tcl-30,Uridylate-specific endoribonu
KMH003 Model of human embryo, development process of embryo, 13 parts, expansion
KMH003 Model of human embryo, development process of embryo, 13 parts Set
MT-104-009 Mouse Embryo Total Protein Set of all 9 embryo Total Protein, 0.1mg each 9x0.1mg
MT-104-005 Mouse Embryo Total Protein Set of 5 embryo Total Protein, 0.1mg each 5x0.1mg
18-003-44001 10 days embryo whole body cDNA. RIKEN full-length enriched library. clone 2610510L15 product poly(A)-specific ribonuclease (dead - N_A Polyclonal 0.1 mg Protein A
Embryo-E20 Rat Whole Embryo cDNA Embryo_E20 30 reactions
Embryo-E19  Rat Whole Embryo cDNA Embryo_E19  30 reactions
Embryo-E13   Rat Whole Embryo cDNA Embryo_E13   30 reactions
Embryo-E12   Rat Whole Embryo cDNA Embryo_E12   30 reactions
Embryo-E18 Rat Whole Embryo cDNA Embryo_E18 30 reactions
Embryo-E15 Rat Whole Embryo cDNA Embryo_E15 30 reactions
Embryo-E17  Rat Whole Embryo cDNA Embryo_E17  30 reactions
Embryo-E14  Rat Whole Embryo cDNA Embryo_E14  30 reactions
Embryo-E16   Rat Whole Embryo cDNA Embryo_E16   30 reactions


 

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