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

Peroxiredoxin PRX1, mitochondrial (Prx) (EC 1.11.1.15) (1-Cys PRX) (Mitochondrial thiol peroxidase) (mTPx) (Thioredoxin peroxidase)

 PRX1_YEAST              Reviewed;         261 AA.
P34227; D6VPT6;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
12-SEP-2018, entry version 158.
RecName: Full=Peroxiredoxin PRX1, mitochondrial {ECO:0000305};
Short=Prx;
EC=1.11.1.15 {ECO:0000269|PubMed:10821871};
AltName: Full=1-Cys PRX;
AltName: Full=Mitochondrial thiol peroxidase {ECO:0000303|PubMed:10681558};
Short=mTPx {ECO:0000303|PubMed:10681558};
AltName: Full=Thioredoxin peroxidase;
Flags: Precursor;
Name=PRX1 {ECO:0000303|PubMed:10821871}; OrderedLocusNames=YBL064C;
ORFNames=YBL0503, YBL0524;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8154187; DOI=10.1002/yea.320091210;
Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
"Sequencing and functional analysis of a 32,560 bp segment on the left
arm of yeast chromosome II. Identification of 26 open reading frames,
including the KIP1 and SEC17 genes.";
Yeast 9:1355-1371(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
CHARACTERIZATION, AND MUTAGENESIS OF CYS-91.
PubMed=10681558; DOI=10.1074/jbc.275.8.5723;
Park S.G., Cha M.-K., Jeong W., Kim I.-H.;
"Distinct physiological functions of thiol peroxidase isoenzymes in
Saccharomyces cerevisiae.";
J. Biol. Chem. 275:5723-5732(2000).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-38.
PubMed=10821871; DOI=10.1074/jbc.275.21.16296;
Pedrajas J.R., Miranda-Vizuete A., Javanmardy N., Gustafsson J.A.,
Spyrou G.;
"Mitochondria of Saccharomyces cerevisiae contain one-conserved
cysteine type peroxiredoxin with thioredoxin peroxidase activity.";
J. Biol. Chem. 275:16296-16301(2000).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=17761666; DOI=10.1074/mcp.M700098-MCP200;
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
"Profiling phosphoproteins of yeast mitochondria reveals a role of
phosphorylation in assembly of the ATP synthase.";
Mol. Cell. Proteomics 6:1896-1906(2007).
[9]
FUNCTION.
PubMed=19332553; DOI=10.1128/MCB.01918-08;
Greetham D., Grant C.M.;
"Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin
is dependent on thioredoxin reductase and glutathione in vivo.";
Mol. Cell. Biol. 29:3229-3240(2009).
[10]
FUNCTION, AND SUBUNIT.
PubMed=20059400; DOI=10.1089/ars.2009.2950;
Pedrajas J.R., Padilla C.A., McDonagh B., Barcena J.A.;
"Glutaredoxin participates in the reduction of peroxides by the
mitochondrial 1-CYS peroxiredoxin in Saccharomyces cerevisiae.";
Antioxid. Redox Signal. 13:249-258(2010).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides and as sensor of
hydrogen peroxide-mediated signaling events. Involved in
mitochondrial protection of cadmium-induced oxidative stress.
{ECO:0000269|PubMed:10821871, ECO:0000269|PubMed:19332553,
ECO:0000269|PubMed:20059400}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:10821871}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.2 uM for H(2)O(2) {ECO:0000269|PubMed:10821871};
KM=10.9 uM for tert-butyl hydroperoxide
{ECO:0000269|PubMed:10821871};
KM=8.1 uM for TRX3 {ECO:0000269|PubMed:10821871};
Vmax=8.5 umol/min/mg enzyme for H(2)O(2)
{ECO:0000269|PubMed:10821871};
Vmax=7.4 umol/min/mg enzyme for tert-butyl hydroperoxide
{ECO:0000269|PubMed:10821871};
Vmax=9.5 umol/min/mg enzyme for TRX3
{ECO:0000269|PubMed:10821871};
pH dependence:
Optimum pH is 7.0 (PubMed:10821871). Optimum pH is 8.5 (using
glutaredoxin as electron donor) (PubMed:20059400).
{ECO:0000269|PubMed:10821871, ECO:0000269|PubMed:20059400};
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000269|PubMed:10821871, ECO:0000305|PubMed:20059400}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10821871,
ECO:0000269|PubMed:14576278}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P)
instead forms a disulfide with a cysteine from another protein or
with a small thiol molecule. C(P) is reactivated by
glutathionylation and subsequent reduction by either glutaredoxin
GRX2 or thioredoxin reductase TRR2, coupled with reduced
glutathione (GSH). {ECO:0000305|PubMed:19332553,
ECO:0000305|PubMed:20059400}.
-!- MISCELLANEOUS: Present with 4510 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 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; Z23261; CAA80784.1; -; Genomic_DNA.
EMBL; Z35825; CAA84884.1; -; Genomic_DNA.
EMBL; BK006936; DAA07056.1; -; Genomic_DNA.
PIR; S39825; S39825.
RefSeq; NP_009489.1; NM_001178304.1.
ProteinModelPortal; P34227; -.
SMR; P34227; -.
BioGrid; 32635; 76.
DIP; DIP-6412N; -.
IntAct; P34227; 12.
MINT; P34227; -.
STRING; 4932.YBL064C; -.
iPTMnet; P34227; -.
UCD-2DPAGE; P34227; -.
MaxQB; P34227; -.
PaxDb; P34227; -.
PRIDE; P34227; -.
TopDownProteomics; P34227; -.
EnsemblFungi; YBL064C; YBL064C; YBL064C.
GeneID; 852215; -.
KEGG; sce:YBL064C; -.
EuPathDB; FungiDB:YBL064C; -.
SGD; S000000160; PRX1.
GeneTree; ENSGT00550000074794; -.
HOGENOM; HOG000022346; -.
InParanoid; P34227; -.
KO; K03386; -.
OMA; MSAGRNF; -.
OrthoDB; EOG092C3W08; -.
BioCyc; YEAST:G3O-28961-MONOMER; -.
Reactome; R-SCE-6798695; Neutrophil degranulation.
PRO; PR:P34227; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:SGD.
GO; GO:0045454; P:cell redox homeostasis; IDA:SGD.
GO; GO:0034599; P:cellular response to oxidative stress; IGI:SGD.
GO; GO:0046686; P:response to cadmium ion; IMP:SGD.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Antioxidant; Complete proteome; Disulfide bond; Mitochondrion;
Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center;
Reference proteome; Transit peptide.
TRANSIT 1 13 Mitochondrion. {ECO:0000255}.
CHAIN 14 261 Peroxiredoxin PRX1, mitochondrial.
/FTId=PRO_0000135151.
DOMAIN 49 212 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 91 91 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000305|PubMed:10681558}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:17761666}.
DISULFID 38 38 Interchain.
{ECO:0000305|PubMed:10821871}.
MUTAGEN 38 38 C->S: Impairs dimer formation.
{ECO:0000269|PubMed:10821871}.
MUTAGEN 91 91 C->S: No activity.
{ECO:0000269|PubMed:10681558}.
SEQUENCE 261 AA; 29496 MW; F611A9ED85E4681A CRC64;
MFSRICSAQL KRTAWTLPKQ AHLQSQTIKT FATAPILCKQ FKQSDQPRLR INSDAPNFDA
DTTVGKINFY DYLGDSWGVL FSHPADFTPV CTTEVSAFAK LKPEFDKRNV KLIGLSVEDV
ESHEKWIQDI KEIAKVKNVG FPIIGDTFRN VAFLYDMVDA EGFKNINDGS LKTVRSVFVI
DPKKKIRLIF TYPSTVGRNT SEVLRVIDAL QLTDKEGVVT PINWQPADDV IIPPSVSNDE
AKAKFGQFNE IKPYLRFTKS K


Related products :

Catalog number Product name Quantity
U0703r CLIA Antioxidant enzyme B166,AOEB166,Peroxiredoxin V,Peroxiredoxin-5, mitochondrial,Peroxisomal antioxidant enzyme,PLP,Prdx5,Prx-V,Rat,Rattus norvegicus,Thioredoxin peroxidase PMP20,Thioredoxin reduct 96T
E0703r ELISA Antioxidant enzyme B166,AOEB166,Peroxiredoxin V,Peroxiredoxin-5, mitochondrial,Peroxisomal antioxidant enzyme,PLP,Prdx5,Prx-V,Rat,Rattus norvegicus,Thioredoxin peroxidase PMP20,Thioredoxin reduc 96T
E0703r ELISA kit Antioxidant enzyme B166,AOEB166,Peroxiredoxin V,Peroxiredoxin-5, mitochondrial,Peroxisomal antioxidant enzyme,PLP,Prdx5,Prx-V,Rat,Rattus norvegicus,Thioredoxin peroxidase PMP20,Thioredoxin 96T
E1123p ELISA Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
U1123p CLIA Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123p ELISA kit Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123r ELISA kit Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123m ELISA kit Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,TSA 96T
U1123m CLIA Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,TSA 96T
U1123r CLIA Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123r ELISA Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123m ELISA Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,TSA 96T
15-288-21018 Peroxiredoxin-2 - EC 1.11.1.15; Thioredoxin peroxidase 1; Thioredoxin-dependent peroxide reductase 1; Thiol-specific antioxidant protein; TSA; PRP; Natural killer cell-enhancing factor B; NKEF-B Polyc 0.05 mg
15-288-21018 Peroxiredoxin-2 - EC 1.11.1.15; Thioredoxin peroxidase 1; Thioredoxin-dependent peroxide reductase 1; Thiol-specific antioxidant protein; TSA; PRP; Natural killer cell-enhancing factor B; NKEF-B Polyc 0.1 mg
E1123h ELISA Homo sapiens,Human,Natural killer cell-enhancing factor B,NKEFB,NKEF-B,Peroxiredoxin-2,PRDX2,PRP,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide 96T
U1123h CLIA Homo sapiens,Human,Natural killer cell-enhancing factor B,NKEFB,NKEF-B,Peroxiredoxin-2,PRDX2,PRP,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide r 96T
E1123h ELISA kit Homo sapiens,Human,Natural killer cell-enhancing factor B,NKEFB,NKEF-B,Peroxiredoxin-2,PRDX2,PRP,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent pero 96T
EIAAB32327 Antioxidant enzyme AOE372,Mouse,Mus musculus,Peroxiredoxin IV,Peroxiredoxin-4,Prdx4,Prx-IV,Thioredoxin peroxidase AO372,Thioredoxin-dependent peroxide reductase A0372
EIAAB32326 Antioxidant enzyme AOE372,Peroxiredoxin IV,Peroxiredoxin-4,Prdx4,Prx-IV,Rat,Rattus norvegicus,Rno2CysPrx04,Thioredoxin peroxidase AO372,Thioredoxin-dependent peroxide reductase A0372
EIAAB32329 Antioxidant enzyme AOE372,AOE37-2,Homo sapiens,Human,Peroxiredoxin IV,Peroxiredoxin-4,PRDX4,Prx-IV,Thioredoxin peroxidase AO372,Thioredoxin-dependent peroxide reductase A0372
E2222r HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2
E0703b ELISA Bos taurus,Bovine,Peroxiredoxin V,Peroxiredoxin-5, mitochondrial,PRDX5,Prx-V,Thioredoxin reductase 96T
E0703b ELISA kit Bos taurus,Bovine,Peroxiredoxin V,Peroxiredoxin-5, mitochondrial,PRDX5,Prx-V,Thioredoxin reductase 96T
U0703b CLIA Bos taurus,Bovine,Peroxiredoxin V,Peroxiredoxin-5, mitochondrial,PRDX5,Prx-V,Thioredoxin reductase 96T
U2222r CLIA kit HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 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