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

ATP-binding cassette transporter abc2 (ABC transporter abc2) (EC 3.6.3.-) (ATP-energized glutathione S-conjugate pump abc2) (Glutathione S-conjugate-transporting ATPase abc2)

 ABC2_SCHPO              Reviewed;        1478 AA.
Q10185; P78928;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
22-NOV-2017, entry version 140.
RecName: Full=ATP-binding cassette transporter abc2;
Short=ABC transporter abc2;
EC=3.6.3.-;
AltName: Full=ATP-energized glutathione S-conjugate pump abc2;
AltName: Full=Glutathione S-conjugate-transporting ATPase abc2;
Name=abc2; ORFNames=SPAC3F10.11c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
REVISION OF GENE MODEL.
PubMed=21511999; DOI=10.1126/science.1203357;
Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K.,
Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.,
Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L.,
FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D.,
Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M.,
Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M.,
Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D.,
Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H.,
Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
"Comparative functional genomics of the fission yeasts.";
Science 332:930-936(2011).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1043-1478.
STRAIN=PR745;
PubMed=9501991; DOI=10.1093/dnares/4.6.363;
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
"Identification of open reading frames in Schizosaccharomyces pombe
cDNAs.";
DNA Res. 4:363-369(1997).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=16849797; DOI=10.1099/mic.0.28952-0;
Iwaki T., Giga-Hama Y., Takegawa K.;
"A survey of all 11 ABC transporters in fission yeast: two novel ABC
transporters are required for red pigment accumulation in a
Schizosaccharomyces pombe adenine biosynthetic mutant.";
Microbiology 152:2309-2321(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-839; SER-843 AND
SER-863, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: Involved in vacuolar sequestration of glutathione S-
conjugates. Together with abc4, required for accumulation of a red
pigment (ade pigment) in the vacuole of a mutant affected in the
adenine biosynthetic pathway. {ECO:0000269|PubMed:16849797}.
-!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
-!- DISRUPTION PHENOTYPE: Cells lacking both abc2 and abc4 show
sensitivity to cycloheximide (CHX) and 4-nitroquinoline oxide (4-
NQO), and decreased accumulation of monochlorobimane-glutathione
(MCIB-GS). {ECO:0000269|PubMed:16849797}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. Conjugate transporter (TC 3.A.1.208) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CU329670; CAA93309.3; -; Genomic_DNA.
EMBL; D89231; BAA13892.1; -; mRNA.
PIR; T38712; T38712.
RefSeq; NP_593943.3; NM_001019371.3.
ProteinModelPortal; Q10185; -.
SMR; Q10185; -.
BioGrid; 279622; 20.
MINT; MINT-4697599; -.
STRING; 4896.SPAC3F10.11c.1; -.
TCDB; 3.A.1.208.16; the atp-binding cassette (abc) superfamily.
iPTMnet; Q10185; -.
MaxQB; Q10185; -.
PRIDE; Q10185; -.
EnsemblFungi; SPAC3F10.11c.1; SPAC3F10.11c.1:pep; SPAC3F10.11c.
GeneID; 2543193; -.
KEGG; spo:SPAC3F10.11c; -.
EuPathDB; FungiDB:SPAC3F10.11c; -.
PomBase; SPAC3F10.11c; abc2.
InParanoid; Q10185; -.
OMA; ENEWRVD; -.
OrthoDB; EOG092C0QQU; -.
PhylomeDB; Q10185; -.
Reactome; R-SPO-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
Reactome; R-SPO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-SPO-382556; ABC-family proteins mediated transport.
PRO; PR:Q10185; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0044604; F:phytochelatin transmembrane transporter ATPase activity; IMP:PomBase.
GO; GO:0098849; P:cellular detoxification of cadmium ion; IMP:PomBase.
GO; GO:0071996; P:glutathione transmembrane import into vacuole; IMP:PomBase.
GO; GO:0036246; P:phytochelatin 2 import into vacuole; IMP:PomBase.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
ATP-binding; Complete proteome; Detoxification; Glycoprotein;
Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Vacuole.
CHAIN 1 1478 ATP-binding cassette transporter abc2.
/FTId=PRO_0000093468.
TOPO_DOM 1 25 Vacuolar. {ECO:0000250}.
TRANSMEM 26 46 Helical; Name=1. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 47 65 Cytoplasmic. {ECO:0000250}.
TRANSMEM 66 85 Helical; Name=2. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 86 90 Vacuolar. {ECO:0000250}.
TRANSMEM 91 104 Helical; Name=3. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 105 116 Cytoplasmic. {ECO:0000250}.
TRANSMEM 117 137 Helical; Name=4. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 138 154 Vacuolar. {ECO:0000250}.
TRANSMEM 155 175 Helical; Name=5. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 176 259 Cytoplasmic. {ECO:0000250}.
TRANSMEM 260 280 Helical; Name=6. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 281 310 Vacuolar. {ECO:0000250}.
TRANSMEM 311 331 Helical; Name=7. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 332 387 Cytoplasmic. {ECO:0000250}.
TRANSMEM 388 408 Helical; Name=8. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 409 411 Vacuolar. {ECO:0000250}.
TRANSMEM 412 432 Helical; Name=9. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 433 495 Cytoplasmic. {ECO:0000250}.
TRANSMEM 496 516 Helical; Name=10. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 517 539 Vacuolar. {ECO:0000250}.
TRANSMEM 540 560 Helical; Name=11. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 561 910 Cytoplasmic. {ECO:0000250}.
TRANSMEM 911 931 Helical; Name=12. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 932 968 Vacuolar. {ECO:0000250}.
TRANSMEM 969 990 Helical; Name=13. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 991 1033 Cytoplasmic. {ECO:0000250}.
TRANSMEM 1034 1054 Helical; Name=14. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1055 1055 Vacuolar. {ECO:0000250}.
TRANSMEM 1056 1076 Helical; Name=15. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1077 1147 Cytoplasmic. {ECO:0000250}.
TRANSMEM 1148 1168 Helical; Name=16. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1169 1172 Vacuolar. {ECO:0000250}.
TRANSMEM 1173 1193 Helical; Name=17. {ECO:0000255|PROSITE-
ProRule:PRU00441}.
TOPO_DOM 1194 1478 Cytoplasmic. {ECO:0000250}.
DOMAIN 268 557 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 593 821 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 918 1202 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1239 1473 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 631 638 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1273 1280 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
MOD_RES 839 839 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 843 843 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 863 863 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 1287 1287 F -> L (in Ref. 3; BAA13892).
{ECO:0000305}.
CONFLICT 1301 1303 DIN -> YIH (in Ref. 3; BAA13892).
{ECO:0000305}.
CONFLICT 1311 1311 D -> H (in Ref. 3; BAA13892).
{ECO:0000305}.
CONFLICT 1467 1467 L -> V (in Ref. 3; BAA13892).
{ECO:0000305}.
SEQUENCE 1478 AA; 166938 MW; 6C59F43105EB7187 CRC64;
MVLEQDLDPF VGGNWMNSAY KGFTFLSATW LAPNIYLLIS GCLQYFYEVR KRSHYFHFRR
FWTIWLKSLV IMVLLFTHIY DCYKTNESVW NVLSIITYFL ALFLHVVEQP TLRIPMASLL
MFWLFKFLAS ALVLLLRPNY TMFPMLNVVP SITFFCSLVC LLAEIYVPPA NRVWYPDDAA
ELEETGLRPS RFTYANIFSR ISFGWLSPLM KFGYRNYLTE SDAWSLPPAE RSSNLTIVFE
KNWISHAKKK KSSLYMWGVL FLNHWKLTVV IIVLKLVQDV VAFIQPNLIR KIVIFVSSYS
SEHPQPPQVG FSLAIAMFLT NVVQTALLQQ YFQLGMVLGM RWRSELITAI YRKSLRLSSA
ARQSRSVGDI VNYMSVDTQK VCDLTMFLFV IVSGPFQIVL ALTNLYHLVG YGALSGAFVT
FLLFPCNVVI ASIFKRFQNR QMKNKDARSQ FMTEIINNIR SIKLYAWENI FLQKLLQLRN
TRELRMLKKI GIVNTIGNFT WLFAPILVSA ATFGTFIVLY GKTRVLSVDI VFACLSLFNL
LQFPLTMLPI VVSSVLEASV AISRIYGFLT AGELDSNAVQ RYPANKEPSG VCLEIKKGTF
SWSGPGQNAA EPTLRDIDFV ARRGELCCIV GKVGMGKSSL LEACLGNMQK HSGSVFRCGS
IAYAAQQPWI LNATIQENIL FGLELDPEFY EKTIRACCLL RDFEILADGD QTEVGEKGIS
LSGGQKARIS LARAVYSRSD IYLLDDILSA VDQHVNRDLV RNLLGSKGLL RSRCVILSTN
SLTVLKEASM IYMLRNGKII ESGSFTQLSS SPDSQLFQLL SEFSKKDTAS STGADTPLSR
SQSVITSSTD VTSSASRSSD TVSNYPKATI KGTGRIRKRL TDEDNVKATG QAAEKMERGK
VKWKVYWTYF KACSLFLIFL YFLFIIGGIG MNVGTNVWLK HWSEVNTQLG YNPKPYFYLG
IYTLFGLLSC ALISLSSLTI TVFCAIKSCR YLHDSMVKAV LRAPMSFFET TPTGRILNRF
SSDVYRVDEV ISRVFMFFFR NLFQIVFVLA VICYSSPMFM ILIVPLFFLY RYNQVYYTQT
SRELKRLDSV TRSPLYAHFQ ESLGGLSTIR AYDMEDTFIS ENDIRVDTNH RIWFLYFSSN
RWQAIRVEAI GALVVFSSAF FGVLSAVRGN PNSGLVGLSL SYAVQITQSL TFVVRQSVDV
ETNIVSVERM LEYIGLPSEA PSIIPDHRPP EGWPSHGAIK FDHYSVRYRE NLPLVLNDIS
VNIKPQEKIG IVGRTGAGKS TLTLALFRLI EPTSGDIQLD DINITSIGLH DLRSRLAIIP
QENQAFEGTI RENLDPNANA TDEEIWHALE AASLKQFIQT LDGGLYSRVT EGGANLSSGQ
RQLMCLTRAL LTPTRVLLLD EATAAVDVET DAIVQRTIRE RFNDRTILTI AHRINTVMDS
NRILVLDHGK VVEFDSTKKL LENKASLFYS LAKESGLI


Related products :

Catalog number Product name Quantity
ARP57129_P050 ABC2 50 µg
NB100-74598 ABC2 0.1 mg
orb101114 ABC2 antibody 100 ug
NB100-74598 ABC2 0.1 mg
orb101114 ABC2 antibody 200 ug
orb101999 ABC2 antibody (FITC) 100 ug
BP301-471 ABC2 Blocking Peptide 50 ug
bs-6515R Rabbit Anti-ABC2 Polyclonal Antibody 100ul
'AP45776PU-N ABC2 SMG8 antibody Ab host: Rabbit 0.1 mg
bs-6515R-Cy5.5 Rabbit Anti-ABC2 Polyclonal Antibody, Cy5.5 Conjugated 100ul
bs-6515R-Cy7 Rabbit Anti-ABC2 Polyclonal Antibody, Cy7 Conjugated 100ul
bs-6515R-Cy5 Rabbit Anti-ABC2 Polyclonal Antibody, Cy5 Conjugated 100ul
bs-6515R-Cy3 Rabbit Anti-ABC2 Polyclonal Antibody, Cy3 Conjugated 100ul
bs-6515R-A350 Rabbit Anti-ABC2 Polyclonal Antibody, ALEXA FLUOR 350 Conjugated 100ul
bs-6515R-A555 Rabbit Anti-ABC2 Polyclonal Antibody, ALEXA FLUOR 555 Conjugated 100ul
bs-6515R-A488 Rabbit Anti-ABC2 Polyclonal Antibody, ALEXA FLUOR 488 Conjugated 100ul
bs-6515R-A647 Rabbit Anti-ABC2 Polyclonal Antibody, ALEXA FLUOR 647 Conjugated 100ul
bs-6515R-Biotin Rabbit Anti-ABC2 Polyclonal Antibody, Biotin Conjugated 100ul
bs-6515R-FITC Rabbit Anti-ABC2 Polyclonal Antibody, FITC Conjugated 100ul
orb101999 ABC2 antibody (FITC) Polyclonal Antibody Host: Rabbit 100ug
orb101999 ABC2 antibody (FITC) Polyclonal Antibodies Primary antibodies 100
orb101114 ABC2 antibody Polyclonal Antibody Host: Rabbit 100ug
orb101114 ABC2 antibody Polyclonal Antibody Host: Rabbit 200ug
orb101114 ABC2 antibody Polyclonal Antibodies Primary antibodies 100
EIAAB38808 ABC2,Amplified in breast cancer gene 2 protein,C17orf71,Homo sapiens,Human,Protein SMG8,Protein smg-8 homolog,SMG8


 

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