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

Vacuolar protein-sorting-associated protein 25 (ESCRT-II complex subunit VPS25) (Vacuolar protein sorting 25)

 VPS25_DROME             Reviewed;         174 AA.
Q7JXV9;
13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 1.
20-DEC-2017, entry version 96.
RecName: Full=Vacuolar protein-sorting-associated protein 25;
AltName: Full=ESCRT-II complex subunit VPS25;
AltName: Full=Vacuolar protein sorting 25;
Name=Vps25; Synonyms=l(2)44Db; ORFNames=CG14750;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4]
INTERACTION WITH LSN/SNF8/VPS22.
PubMed=14605208; DOI=10.1126/science.1090289;
Giot L., Bader J.S., Brouwer C., Chaudhuri A., Kuang B., Li Y.,
Hao Y.L., Ooi C.E., Godwin B., Vitols E., Vijayadamodar G.,
Pochart P., Machineni H., Welsh M., Kong Y., Zerhusen B., Malcolm R.,
Varrone Z., Collis A., Minto M., Burgess S., McDaniel L., Stimpson E.,
Spriggs F., Williams J., Neurath K., Ioime N., Agee M., Voss E.,
Furtak K., Renzulli R., Aanensen N., Carrolla S., Bickelhaupt E.,
Lazovatsky Y., DaSilva A., Zhong J., Stanyon C.A., Finley R.L. Jr.,
White K.P., Braverman M., Jarvie T., Gold S., Leach M., Knight J.,
Shimkets R.A., McKenna M.P., Chant J., Rothberg J.M.;
"A protein interaction map of Drosophila melanogaster.";
Science 302:1727-1736(2003).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16256743; DOI=10.1016/j.devcel.2005.09.019;
Vaccari T., Bilder D.;
"The Drosophila tumor suppressor vps25 prevents nonautonomous
overproliferation by regulating notch trafficking.";
Dev. Cell 9:687-698(2005).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16256745; DOI=10.1016/j.devcel.2005.09.020;
Thompson B.J., Mathieu J., Sung H.H., Loeser E., Rorth P., Cohen S.M.;
"Tumor suppressor properties of the ESCRT-II complex component Vps25
in Drosophila.";
Dev. Cell 9:711-720(2005).
[7]
DISRUPTION PHENOTYPE.
PubMed=17088062; DOI=10.1016/j.cub.2006.09.031;
Childress J.L., Acar M., Tao C., Halder G.;
"Lethal giant discs, a novel C2-domain protein, restricts notch
activation during endocytosis.";
Curr. Biol. 16:2228-2233(2006).
[8]
DISRUPTION PHENOTYPE.
PubMed=16611691; DOI=10.1242/dev.02356;
Herz H.M., Chen Z., Scherr H., Lackey M., Bolduc C., Bergmann A.;
"vps25 mosaics display non-autonomous cell survival and overgrowth,
and autonomous apoptosis.";
Development 133:1871-1880(2006).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17935992; DOI=10.1016/j.cub.2007.09.032;
Rusten T.E., Vaccari T., Lindmo K., Rodahl L.M., Nezis I.P.,
Sem-Jacobsen C., Wendler F., Vincent J.P., Brech A., Bilder D.,
Stenmark H.;
"ESCRTs and Fab1 regulate distinct steps of autophagy.";
Curr. Biol. 17:1817-1825(2007).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17268469; DOI=10.1038/nature05503;
Irion U., St Johnston D.;
"bicoid RNA localization requires specific binding of an endosomal
sorting complex.";
Nature 445:554-558(2007).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19132102; DOI=10.1371/journal.pone.0004165;
Herz H.M., Woodfield S.E., Chen Z., Bolduc C., Bergmann A.;
"Common and distinct genetic properties of ESCRT-II components in
Drosophila.";
PLoS ONE 4:E4165-E4165(2009).
-!- FUNCTION: Component of the ESCRT-II complex (ensodomal sorting
complex required for transport II), which is required for
multivesicular body (MVB) formation and sorting of endosomal cargo
proteins into MVBs. The MVB pathway mediates delivery of
transmembrane proteins into the lumen of the lysosome for
degradation. The ESCRT-II complex is probably involved in the
recruitment of the ESCRT-III complex (By similarity). Seems to
function as a tumor suppressor by regulating Notch trafficking,
hence preventing non-autonomous overproliferation. May be involved
in the regulation of autophagy. ESCRT-II interacts with bicoid
mRNA, which is required for the anterior localization of bicoid
mRNA in the developing egg. {ECO:0000250,
ECO:0000269|PubMed:16256743, ECO:0000269|PubMed:16256745,
ECO:0000269|PubMed:17268469, ECO:0000269|PubMed:17935992,
ECO:0000269|PubMed:19132102}.
-!- SUBUNIT: Component of the endosomal sorting complex required for
transport II (ESCRT-II) (By similarity). Interacts with
Lsn/Snf8/Vps22 (Probable). {ECO:0000250, ECO:0000305}.
-!- INTERACTION:
Q9VD72:lsn; NbExp=3; IntAct=EBI-98834, EBI-104459;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Vps25 mutant cells exhibit multivesicular
body sorting defects, with large amounts of ubiquitinated proteins
detected on endosomes. This leads to activation of signals
(through Notch and Dpp receptors) that drive cell proliferation,
non-autonomous overgrowth, loss of epithelial organization, and
render cells sensitive to apoptosis. Vps25 mutant cells display
accumulation of autophagosomes. Bicoid mRNA is mislocalized in
developing eggs. {ECO:0000269|PubMed:16256743,
ECO:0000269|PubMed:16256745, ECO:0000269|PubMed:16611691,
ECO:0000269|PubMed:17088062, ECO:0000269|PubMed:17268469,
ECO:0000269|PubMed:17935992, ECO:0000269|PubMed:19132102}.
-!- SIMILARITY: Belongs to the VPS25 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AE013599; AAF59066.1; -; Genomic_DNA.
EMBL; AY089657; AAL90395.1; -; mRNA.
RefSeq; NP_610398.1; NM_136554.3.
UniGene; Dm.4897; -.
ProteinModelPortal; Q7JXV9; -.
SMR; Q7JXV9; -.
BioGrid; 61697; 17.
IntAct; Q7JXV9; 5.
STRING; 7227.FBpp0087774; -.
MoonProt; Q7JXV9; -.
PaxDb; Q7JXV9; -.
PRIDE; Q7JXV9; -.
EnsemblMetazoa; FBtr0088694; FBpp0087774; FBgn0022027.
GeneID; 35847; -.
KEGG; dme:Dmel_CG14750; -.
UCSC; CG14750-RA; d. melanogaster.
CTD; 84313; -.
FlyBase; FBgn0022027; Vps25.
eggNOG; KOG4068; Eukaryota.
eggNOG; ENOG4111F6Y; LUCA.
GeneTree; ENSGT00390000014892; -.
InParanoid; Q7JXV9; -.
KO; K12189; -.
OMA; PPFFTIQ; -.
OrthoDB; EOG091G0PIU; -.
PhylomeDB; Q7JXV9; -.
Reactome; R-DME-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
GenomeRNAi; 35847; -.
PRO; PR:Q7JXV9; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0022027; -.
Genevisible; Q7JXV9; DM.
GO; GO:0000814; C:ESCRT II complex; ISS:FlyBase.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0005198; F:structural molecule activity; ISS:FlyBase.
GO; GO:0097352; P:autophagosome maturation; IMP:FlyBase.
GO; GO:0045450; P:bicoid mRNA localization; IMP:UniProtKB.
GO; GO:0030154; P:cell differentiation; IMP:FlyBase.
GO; GO:0008283; P:cell proliferation; IMP:FlyBase.
GO; GO:0016197; P:endosomal transport; IMP:FlyBase.
GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IMP:FlyBase.
GO; GO:0010669; P:epithelial structure maintenance; IMP:FlyBase.
GO; GO:0060429; P:epithelium development; IMP:FlyBase.
GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:FlyBase.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:FlyBase.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:FlyBase.
GO; GO:0030713; P:ovarian follicle cell stalk formation; IMP:FlyBase.
GO; GO:0008104; P:protein localization; IMP:UniProtKB.
GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
GO; GO:0042981; P:regulation of apoptotic process; IMP:FlyBase.
GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:FlyBase.
GO; GO:0070086; P:ubiquitin-dependent endocytosis; IMP:FlyBase.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:FlyBase.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 1.10.10.570; -; 1.
InterPro; IPR008570; ESCRT-II_cplx_vps25-sub.
InterPro; IPR014041; ESCRT-II_cplx_Vps25-sub_N.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR13149; PTHR13149; 1.
Pfam; PF05871; ESCRT-II; 1.
SUPFAM; SSF46785; SSF46785; 2.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Endosome; Membrane; Protein transport;
Reference proteome; Transport.
CHAIN 1 174 Vacuolar protein-sorting-associated
protein 25.
/FTId=PRO_0000386527.
SEQUENCE 174 AA; 20608 MW; 0711584CC2727233 CRC64;
MAEFQWPWEY TFPPFFTLQP HEETRQQQLK VWTDLFLKYL RHTNRFTLSI GDQNSPLFHN
EALKRRLSPE LVLAILGELE RSGHANPLDK RRQEWQVYWF TLEEYGNMVY DWVQETGQTN
TICTLYEIAS GENTSHLDFY GVDEAVLLSA LRLLEEKGRC ELIEMDGSHG VKFF


Related products :

Catalog number Product name Quantity
EIAAB45931 Eap20,ELL-associated protein of 20 kDa,ESCRT-II complex subunit VPS25,Rat,Rattus norvegicus,Vacuolar protein-sorting-associated protein 25,Vps25
EIAAB45929 Dermal papilla-derived protein 9,DERP9,EAP20,ELL-associated protein of 20 kDa,ESCRT-II complex subunit VPS25,Homo sapiens,Human,hVps25,Vacuolar protein-sorting-associated protein 25,VPS25
EIAAB45928 D11Wsu68e,ESCRT-II complex subunit VPS25,Mouse,Mus musculus,Vacuolar protein-sorting-associated protein 25,Vps25
EIAAB45930 Bos taurus,Bovine,ESCRT-II complex subunit VPS25,Vacuolar protein-sorting-associated protein 25,VPS25
orb41401 VPS37C antibody Polyclonal Rabbit polyclonal to VPS37C. VPS37C is a subunit of ESCRT-I (endosomal sorting complex required for transport I), a complex in the class E vacuolar protein sorting (VPS) pat 100
EIAAB45946 C13orf9,CGI-145,EAP45,ELL-associated protein of 45 kDa,ESCRT-II complex subunit VPS36,Homo sapiens,Human,Vacuolar protein-sorting-associated protein 36,VPS36
EIAAB45944 Eap45,ELL-associated protein of 45 kDa,ESCRT-II complex subunit VPS36,Rat,Rattus norvegicus,Vacuolar protein-sorting-associated protein 36,Vps36
EIAAB45896 ESCRT-I complex subunit VPS37A,HCRP1,Hepatocellular carcinoma-related protein 1,Homo sapiens,Human,hVps37A,Vacuolar protein sorting-associated protein 37A,VPS37A
EIAAB45902 ESCRT-I complex subunit VPS37D,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 37D,Vps37d,Wbscr24,Williams-Beuren syndrome region protein 24 homolog
EIAAB45901 ESCRT-I complex subunit VPS37D,Homo sapiens,Human,Vacuolar protein sorting-associated protein 37D,VPS37D,WBSCR24,Williams-Beuren syndrome chromosomal region 24 protein
EIAAB45932 Bos taurus,Bovine,ESCRT-I complex subunit VPS28,Vacuolar protein sorting-associated protein 28 homolog,VPS28
EIAAB38953 Eap30,ELL-associated protein of 30 kDa,ESCRT-II complex subunit VPS22,Rat,Rattus norvegicus,Snf8,Vacuolar-sorting protein SNF8
EIAAB45898 ESCRT-I complex subunit VPS37B,Homo sapiens,Human,hVps37B,Vacuolar protein sorting-associated protein 37B,VPS37B
EIAAB45899 ESCRT-I complex subunit VPS37C,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 37C,Vps37c
EIAAB45945 Bos taurus,Bovine,ESCRT-II complex subunit VPS36,Vacuolar protein-sorting-associated protein 36,VPS36
EIAAB45947 ESCRT-II complex subunit VPS36,Mouse,Mus musculus,Vacuolar protein-sorting-associated protein 36,Vps36
EIAAB45900 ESCRT-I complex subunit VPS37C,Homo sapiens,Human,hVps37C,PML39,Vacuolar protein sorting-associated protein 37C,VPS37C
EIAAB38954 EAP30,ELL-associated protein of 30 kDa,ESCRT-II complex subunit VPS22,Homo sapiens,Human,hVps22,SNF8,Vacuolar-sorting protein SNF8
EIAAB45933 Caspase-activated DNase inhibitor that interacts with ASK1,CIIA,ESCRT-I complex subunit VPS28,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 28 homolog,Vps28
EIAAB38952 D11Moh34,ESCRT-II complex subunit VPS22,Mouse,Mus musculus,Snf8,Vacuolar-sorting protein SNF8
EIAAB45934 ESCRT-I complex subunit VPS28,Homo sapiens,Human,H-Vps28,Vacuolar protein sorting-associated protein 28 homolog,VPS28
EIAAB45897 ESCRT-I complex subunit VPS37B,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 37B,Vps37B,Vps37b
EIAAB45895 ESCRT-I complex subunit VPS37A,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 37A,Vps37A,Vps37a
VPS25 VPS25 Gene vacuolar protein sorting 25 homolog (S. cerevisiae)
CSB-EL025897HU Human Vacuolar protein-sorting-associated protein 25(VPS25) ELISA kit SpeciesHuman 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