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

L-ascorbate peroxidase 1, cytosolic (AP) (AtAPx01) (EC 1.11.1.11)

 APX1_ARATH              Reviewed;         250 AA.
Q05431; Q0WLU2; Q2V4P8; Q2V4P9;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
18-JUL-2018, entry version 157.
RecName: Full=L-ascorbate peroxidase 1, cytosolic;
Short=AP;
Short=AtAPx01;
EC=1.11.1.11;
Name=APX1; OrderedLocusNames=At1g07890; ORFNames=F24B9.2;
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], AND PROTEIN SEQUENCE OF 2-17.
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=1558944; DOI=10.1007/BF00020011;
Kubo A., Saji H., Tanaka K., Tanaka K., Kondo N.;
"Cloning and sequencing of a cDNA encoding ascorbate peroxidase from
Arabidopsis thaliana.";
Plant Mol. Biol. 18:691-701(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=8422923; DOI=10.1016/0014-5793(93)81185-3;
Kubo A., Saji H., Tanaka K., Kondo N.;
"Genomic DNA structure of a gene encoding cytosolic ascorbate
peroxidase from Arabidopsis thaliana.";
FEBS Lett. 315:313-317(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Tremousaygue D., Bardet C., Dabos P., Regad F., Pelese F., Lescure B.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
INDUCTION.
PubMed=8534847; DOI=10.1007/BF00020979;
Kubo A., Saji H., Tanaka K., Kondo N.;
"Expression of Arabidopsis cytosolic ascorbate peroxidase gene in
response to ozone or sulfur dioxide.";
Plant Mol. Biol. 29:479-489(1995).
[10]
INDUCTION.
PubMed=9144965; DOI=10.1105/tpc.9.4.627;
Karpinski S., Escobar C., Karpinski B., Creissen G.P.,
Mullineaux P.M.;
"Photosynthetic electron transport regulates the expression of
cytosolic ascorbate peroxidase genes in Arabidopsis during excess
light stress.";
Plant Cell 9:627-640(1997).
[11]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=9808745; DOI=10.1104/pp.118.3.1005;
Storozhenko S., De Pauw P., Van Montagu M., Inze D., Kushnir S.;
"The heat-shock element is a functional component of the Arabidopsis
APX1 gene promoter.";
Plant Physiol. 118:1005-1014(1998).
[12]
INDUCTION.
PubMed=14739345; DOI=10.1104/pp.103.029876;
Fourcroy P., Vansuyt G., Kushnir S., Inze D., Briat J.-F.;
"Iron-regulated expression of a cytosolic ascorbate peroxidase encoded
by the APX1 gene in Arabidopsis seedlings.";
Plant Physiol. 134:605-613(2004).
[13]
FUNCTION.
PubMed=15608336; DOI=10.1105/tpc.104.026971;
Davletova S., Rizhsky L., Liang H., Shengqiang Z., Oliver D.J.,
Coutu J., Shulaev V., Schlauch K., Mittler R.;
"Cytosolic ascorbate peroxidase 1 is a central component of the
reactive oxygen gene network of Arabidopsis.";
Plant Cell 17:268-281(2005).
[14]
INDUCTION BY CADMIUM.
STRAIN=cv. Columbia;
PubMed=16502469; DOI=10.1002/pmic.200500543;
Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B.,
Moulin C., Ezan E., Garin J., Bourguignon J.;
"The early responses of Arabidopsis thaliana cells to cadmium exposure
explored by protein and metabolite profiling analyses.";
Proteomics 6:2180-2198(2006).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
-!- FUNCTION: Plays a key role in hydrogen peroxide removal.
Constitutes a central component of the reactive oxygen gene
network. {ECO:0000269|PubMed:15608336}.
-!- CATALYTIC ACTIVITY: 2 L-ascorbate + H(2)O(2) + 2 H(+) = L-
ascorbate + L-dehydroascorbate + 2 H(2)O.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit.;
-!- INTERACTION:
Q42403:TRX3; NbExp=2; IntAct=EBI-449365, EBI-449157;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q05431-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Predominantly expressed in flowers.
{ECO:0000269|PubMed:9808745}.
-!- INDUCTION: By ethylene, ozone, sulfur dioxide, Fe exposure,
oxidative and heat-shock stresses, and by excess light treatment.
Induced by cadmium (PubMed:16502469).
{ECO:0000269|PubMed:14739345, ECO:0000269|PubMed:16502469,
ECO:0000269|PubMed:8534847, ECO:0000269|PubMed:9144965,
ECO:0000269|PubMed:9808745}.
-!- MISCELLANEOUS: Binds one cation per subunit; probably K(+), but
might also be Ca(2+). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X59600; CAA42168.1; -; mRNA.
EMBL; D14442; BAA03334.1; -; Genomic_DNA.
EMBL; U63815; AAB07880.1; -; Genomic_DNA.
EMBL; AC007583; AAF75066.1; -; Genomic_DNA.
EMBL; CP002684; AEE28200.1; -; Genomic_DNA.
EMBL; CP002684; AEE28201.1; -; Genomic_DNA.
EMBL; CP002684; AEE28202.1; -; Genomic_DNA.
EMBL; CP002684; AEE28203.1; -; Genomic_DNA.
EMBL; CP002684; AEE28204.1; -; Genomic_DNA.
EMBL; CP002684; AEE28206.1; -; Genomic_DNA.
EMBL; CP002684; AEE28207.1; -; Genomic_DNA.
EMBL; AY039879; AAK63983.1; -; mRNA.
EMBL; AY056395; AAL08251.1; -; mRNA.
EMBL; AY094002; AAM16263.1; -; mRNA.
EMBL; AK230096; BAF01915.1; -; mRNA.
EMBL; AY086425; AAM63427.1; -; mRNA.
PIR; D86214; D86214.
PIR; S20866; S20866.
RefSeq; NP_001030991.2; NM_001035914.2. [Q05431-1]
RefSeq; NP_001077482.1; NM_001084013.1. [Q05431-1]
RefSeq; NP_001117244.1; NM_001123772.2. [Q05431-1]
RefSeq; NP_001318949.1; NM_001331739.1. [Q05431-1]
RefSeq; NP_172267.1; NM_100663.4. [Q05431-1]
RefSeq; NP_849607.1; NM_179276.2. [Q05431-1]
RefSeq; NP_973786.1; NM_202057.2. [Q05431-1]
UniGene; At.47584; -.
UniGene; At.67008; -.
ProteinModelPortal; Q05431; -.
SMR; Q05431; -.
BioGrid; 22545; 4.
IntAct; Q05431; 4.
MINT; Q05431; -.
STRING; 3702.AT1G07890.1; -.
PeroxiBase; 1890; AtAPx01.
iPTMnet; Q05431; -.
SWISS-2DPAGE; Q05431; -.
PaxDb; Q05431; -.
PRIDE; Q05431; -.
EnsemblPlants; AT1G07890.1; AT1G07890.1; AT1G07890. [Q05431-1]
EnsemblPlants; AT1G07890.2; AT1G07890.2; AT1G07890. [Q05431-1]
EnsemblPlants; AT1G07890.3; AT1G07890.3; AT1G07890. [Q05431-1]
EnsemblPlants; AT1G07890.4; AT1G07890.4; AT1G07890. [Q05431-1]
EnsemblPlants; AT1G07890.5; AT1G07890.5; AT1G07890. [Q05431-1]
EnsemblPlants; AT1G07890.7; AT1G07890.7; AT1G07890. [Q05431-1]
EnsemblPlants; AT1G07890.8; AT1G07890.8; AT1G07890. [Q05431-1]
GeneID; 837304; -.
Gramene; AT1G07890.1; AT1G07890.1; AT1G07890. [Q05431-1]
Gramene; AT1G07890.2; AT1G07890.2; AT1G07890. [Q05431-1]
Gramene; AT1G07890.3; AT1G07890.3; AT1G07890. [Q05431-1]
Gramene; AT1G07890.4; AT1G07890.4; AT1G07890. [Q05431-1]
Gramene; AT1G07890.5; AT1G07890.5; AT1G07890. [Q05431-1]
Gramene; AT1G07890.7; AT1G07890.7; AT1G07890. [Q05431-1]
Gramene; AT1G07890.8; AT1G07890.8; AT1G07890. [Q05431-1]
KEGG; ath:AT1G07890; -.
Araport; AT1G07890; -.
TAIR; locus:2026616; AT1G07890.
eggNOG; ENOG410IF5T; Eukaryota.
eggNOG; COG0376; LUCA.
HOGENOM; HOG000189824; -.
InParanoid; Q05431; -.
KO; K00434; -.
OMA; TEDYQNA; -.
OrthoDB; EOG09360KYY; -.
PhylomeDB; Q05431; -.
BioCyc; ARA:GQT-2090-MONOMER; -.
BRENDA; 1.11.1.11; 399.
PRO; PR:Q05431; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q05431; baseline and differential.
Genevisible; Q05431; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0004130; F:cytochrome-c peroxidase activity; IBA:GO_Central.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0016688; F:L-ascorbate peroxidase activity; IMP:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
GO; GO:0009408; P:response to heat; IEP:TAIR.
GO; GO:0000302; P:response to reactive oxygen species; IMP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
InterPro; IPR002207; Peroxidase_I.
InterPro; IPR019794; Peroxidases_AS.
InterPro; IPR019793; Peroxidases_heam-ligand_BS.
Pfam; PF00141; peroxidase; 1.
PRINTS; PR00459; ASPEROXIDASE.
PRINTS; PR00458; PEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS00436; PEROXIDASE_2; 1.
PROSITE; PS50873; PEROXIDASE_4; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome; Cytoplasm;
Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
Metal-binding; Oxidoreductase; Peroxidase; Phosphoprotein; Potassium;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1558944}.
CHAIN 2 250 L-ascorbate peroxidase 1, cytosolic.
/FTId=PRO_0000055592.
ACT_SITE 42 42 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00297, ECO:0000255|PROSITE-
ProRule:PRU10012}.
METAL 163 163 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00297}.
METAL 164 164 Potassium or calcium. {ECO:0000250}.
METAL 180 180 Potassium or calcium. {ECO:0000250}.
METAL 182 182 Potassium or calcium. {ECO:0000250}.
METAL 185 185 Potassium or calcium; via carbonyl
oxygen. {ECO:0000250}.
METAL 187 187 Potassium or calcium. {ECO:0000250}.
SITE 38 38 Transition state stabilizer.
{ECO:0000255|PROSITE-ProRule:PRU00297}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000244|PubMed:22092075}.
SEQUENCE 250 AA; 27561 MW; 33A536D85B2CAA6C CRC64;
MTKNYPTVSE DYKKAVEKCR RKLRGLIAEK NCAPIMVRLA WHSAGTFDCQ SRTGGPFGTM
RFDAEQAHGA NSGIHIALRL LDPIREQFPT ISFADFHQLA GVVAVEVTGG PDIPFHPGRE
DKPQPPPEGR LPDATKGCDH LRDVFAKQMG LSDKDIVALS GAHTLGRCHK DRSGFEGAWT
SNPLIFDNSY FKELLSGEKE GLLQLVSDKA LLDDPVFRPL VEKYAADEDA FFADYAEAHM
KLSELGFADA


Related products :

Catalog number Product name Quantity
AS06 180 Antibody: cAPX | cytosolic ascorbate peroxidase, Immunogen: KLH-conjugated peptide derived from N-terminal of Zea mays cytosolic APX Q41772, Host: rabbit, polyclonal, Confirmed reactivity: Arabidopsis 200
AS06 180 cAPX | cytosolic ascorbate peroxidase 200 ul
AS06180 cAPX | cytosolic ascorbate peroxidase 200 ul
20312234-1 cAPX | cytosolic ascorbate peroxidase (r 200 uL
AS06 180 rabbit polyclonal cAPX | cytosolic ascorbate peroxidase 200
abx109049 Polyclonal Rabbit L-ascorbate peroxidase 2, cytosolic Antibody (HRP) 100 μg
CSB-EL027227PL Plant L-ascorbate peroxidase 2,cytosolic(APX2)ELISA kit SpeciesPlant 96T
abx106217 Polyclonal Rabbit L-ascorbate peroxidase 2, cytosolic Antibody (Biotin) 100 μg
abx107631 Polyclonal Rabbit L-ascorbate peroxidase 2, cytosolic Antibody (FITC) 100 μg
CSB-RP144194PI Recombinant Pl(Arabidopsis thaliana (Mouse-ear cress)) L-ascorbate peroxidase 2, cytosolic 500ug
CSB-RP134794Pl Recombinant Pl(Arabidopsis thaliana (Mouse-ear cress)) L-ascorbate peroxidase 1, cytosolic 500ug
CSB-EL027227PL Plant L-ascorbate peroxidase 2,cytosolic(APX2)ELISA kit , Species , Sample Type 96T
CSB-EL027226PL Plant L-ascorbate peroxidase 1,cytosolic(APX1)ELISA kit , Species , Sample Type 96T
CSB-RP144194PI Recombinant Pl(Arabidopsis thaliana (Mouse-ear cress)) L-ascorbate peroxidase 2, cytosolic Source: E.coli 1mg
CSB-RP134794Pl Recombinant Pl(Arabidopsis thaliana (Mouse-ear cress)) L-ascorbate peroxidase 1, cytosolic Source: E.coli 1mg
CSB-EL027226PL Plant L-ascorbate peroxidase 1,cytosolic(APX1)ELISA kit, Species Plant, Sample Type serum, plasma 96T
CSB-EL027227PL Plant L-ascorbate peroxidase 2,cytosolic(APX2)ELISA kit, Species Plant, Sample Type serum, plasma 96T
20312346-1 APX | L-ascorbate peroxidase (rabbit) 200 uL
AS08 368 rabbit polyclonal APX | L-ascorbate peroxidase 200
'AS08 368 L-ascorbate peroxidase 1 antibody Host rabbit 1 mg
'AS08 368 L-ascorbate peroxidase 1 antibody Ab host: Rabbit 0.2 ml
Y052238 Anti-Ascorbate Oxidase Peroxidase Conjugated antibody 250ug
Y052238 Anti-Ascorbate Oxidase Peroxidase Conjugated Antibody 100 μg
CSB-EL027228PL Plant L-ascorbate peroxidase 3, peroxisomal(APX3)ELISA kit SpeciesPlant 96T
CSB-EL027228PL Plant L-ascorbate peroxidase 3, peroxisomal(APX3)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