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

Aquaporin Z (Bacterial nodulin-like intrinsic protein)

 AQPZ_ECOLI              Reviewed;         231 AA.
P60844; P48838; P75827; Q47159;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 1.
25-OCT-2017, entry version 130.
RecName: Full=Aquaporin Z;
AltName: Full=Bacterial nodulin-like intrinsic protein;
Name=aqpZ; Synonyms=bniP; OrderedLocusNames=b0875, JW0859;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / DH5-alpha;
PubMed=7493926; DOI=10.1074/jbc.270.49.29063;
Calamita G., Bishai W.R., Preston G.M., Guggino W.B., Agre P.;
"Molecular cloning and characterization of AqpZ, a water channel from
Escherichia coli.";
J. Biol. Chem. 270:29063-29066(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=LE392;
Fushimi K.;
"Cloning and expression of a new member of aquaporin water channel
family of E. coli.";
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9137831;
Fushimi K., Bai L., Marumo F., Sasaki S.;
"Isolation of a gene encoding nodulin-like intrinsic protein of
Escherichia coli.";
Biochem. Mol. Biol. Int. 41:995-1003(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[7]
FUNCTION.
STRAIN=K12 / DH5-alpha;
PubMed=10400575;
Delamarche C., Thomas D., Rolland J.-P., Froger A., Gouranton J.,
Svelto M., Agre P., Calamita G.;
"Visualization of AqpZ-mediated water permeability in Escherichia coli
by cryoelectron microscopy.";
J. Bacteriol. 181:4193-4197(1999).
[8]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-9;
CYS-20; THR-183 AND ARG-189.
STRAIN=K12 / DH5-alpha;
PubMed=10518952; DOI=10.1006/jmbi.1999.3032;
Borgnia M.J., Kozono D., Calamita G., Maloney P.C., Agre P.;
"Functional reconstitution and characterization of AqpZ, the E. coli
water channel protein.";
J. Mol. Biol. 291:1169-1179(1999).
[9]
FUNCTION, AND CHARACTERIZATION OF MEMBRANE SELECTIVITY.
STRAIN=K12 / DH5-alpha;
PubMed=11493683; DOI=10.1073/pnas.161299398;
Pohl P., Saparov S.M., Borgnia M.J., Agre P.;
"Highly selective water channel activity measured by voltage clamp:
Analysis of planar lipid bilayers reconstituted with purified AqpZ.";
Proc. Natl. Acad. Sci. U.S.A. 98:9624-9629(2001).
[10]
CRYSTALLIZATION, AND SUBUNIT.
PubMed=10518953; DOI=10.1006/jmbi.1999.3031;
Ringler P., Borgnia M.J., Stahlberg H., Maloney P.C., Agre P.,
Engel A.;
"Structure of the water channel AqpZ from Escherichia coli revealed by
electron crystallography.";
J. Mol. Biol. 291:1181-1190(1999).
[11]
SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=10487750; DOI=10.1093/emboj/18.18.4981;
Scheuring S., Ringler P., Borgnia M.J., Stahlberg H., Mueller D.J.,
Agre P., Engel A.;
"High resolution AFM topographs of the Escherichia coli water channel
aquaporin Z.";
EMBO J. 18:4981-4987(1999).
[12]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=14691544; DOI=10.1371/journal.pbio.0000072;
Savage D.F., Egea P.F., Robles-Colmenares Y., O'Connell J.D. III,
Stroud R.M.;
"Architecture and selectivity in aquaporins: 2.5 A X-ray structure of
aquaporin Z.";
PLoS Biol. 1:334-340(2003).
[14]
REVIEW.
PubMed=10931322; DOI=10.1046/j.1365-2958.2000.02016.x;
Calamita G.;
"The Escherichia coli aquaporin-Z water channel.";
Mol. Microbiol. 37:254-262(2000).
-!- FUNCTION: Channel that permits osmotically driven movement of
water in both directions. It is involved in the osmoregulation and
in the maintenance of cell turgor during volume expansion in
rapidly growing cells. It mediates rapid entry or exit of water in
response to abrupt changes in osmolarity.
{ECO:0000269|PubMed:10400575, ECO:0000269|PubMed:10518952,
ECO:0000269|PubMed:11493683}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10487750,
ECO:0000269|PubMed:10518952, ECO:0000269|PubMed:10518953}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-957663, EBI-957663;
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:10487750, ECO:0000269|PubMed:10518952}; Multi-
pass membrane protein {ECO:0000269|PubMed:10487750,
ECO:0000269|PubMed:10518952}.
-!- INDUCTION: By extracellular hypoosmotic conditions, especially
during the mid-logarithmic phase of growth.
-!- DOMAIN: Aquaporins contain two tandem repeats each containing
three membrane-spanning domains and a pore-forming loop with the
signature motif Asn-Pro-Ala (NPA).
-!- MISCELLANEOUS: It is a remarkably rigid tetramer that does not
dissociate even when solubilized in SDS.
{ECO:0000305|PubMed:10518952}.
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U38664; AAC43518.1; -; Genomic_DNA.
EMBL; D49469; BAA08441.1; -; Genomic_DNA.
EMBL; U00096; AAC73962.1; -; Genomic_DNA.
EMBL; AP009048; BAA35589.1; -; Genomic_DNA.
PIR; C64826; C64826.
RefSeq; NP_415396.1; NC_000913.3.
RefSeq; WP_001298299.1; NZ_LN832404.1.
PDB; 1RC2; X-ray; 2.50 A; A/B=1-231.
PDB; 2ABM; X-ray; 3.20 A; A/B/C/D/E/F/G/H=1-231.
PDB; 2O9D; X-ray; 2.30 A; A/B=1-231.
PDB; 2O9E; X-ray; 2.20 A; A=1-231.
PDB; 2O9F; X-ray; 2.55 A; A/B=1-231.
PDB; 2O9G; X-ray; 1.90 A; A=1-231.
PDB; 3NK5; X-ray; 2.40 A; A/B=1-231.
PDB; 3NKA; X-ray; 2.50 A; A/B=1-231.
PDB; 3NKC; X-ray; 3.10 A; A/B=1-231.
PDBsum; 1RC2; -.
PDBsum; 2ABM; -.
PDBsum; 2O9D; -.
PDBsum; 2O9E; -.
PDBsum; 2O9F; -.
PDBsum; 2O9G; -.
PDBsum; 3NK5; -.
PDBsum; 3NKA; -.
PDBsum; 3NKC; -.
ProteinModelPortal; P60844; -.
SMR; P60844; -.
BioGrid; 4260000; 107.
DIP; DIP-35499N; -.
STRING; 316385.ECDH10B_0945; -.
DrugBank; DB03152; B-2-Octylglucoside.
DrugBank; DB07923; octyl alpha-L-altropyranoside.
DrugBank; DB07924; octyl beta-D-galactopyranoside.
TCDB; 1.A.8.3.1; the major intrinsic protein (mip) family.
PaxDb; P60844; -.
PRIDE; P60844; -.
EnsemblBacteria; AAC73962; AAC73962; b0875.
EnsemblBacteria; BAA35589; BAA35589; BAA35589.
GeneID; 945497; -.
KEGG; ecj:JW0859; -.
KEGG; eco:b0875; -.
PATRIC; fig|1411691.4.peg.1402; -.
EchoBASE; EB1283; -.
EcoGene; EG13270; aqpZ.
eggNOG; ENOG4105D8C; Bacteria.
eggNOG; COG0580; LUCA.
HOGENOM; HOG000288286; -.
InParanoid; P60844; -.
KO; K06188; -.
PhylomeDB; P60844; -.
BioCyc; EcoCyc:AQPZ-MONOMER; -.
BioCyc; MetaCyc:AQPZ-MONOMER; -.
EvolutionaryTrace; P60844; -.
PRO; PR:P60844; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0015250; F:water channel activity; IDA:EcoCyc.
GO; GO:0009992; P:cellular water homeostasis; IMP:EcoCyc.
GO; GO:0006970; P:response to osmotic stress; IMP:EcoCyc.
GO; GO:0006833; P:water transport; IDA:EcoCyc.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
HAMAP; MF_01146; Aquaporin_Z; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR023743; Aquaporin_Z.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
TIGRFAMs; TIGR00861; MIP; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Membrane; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 231 Aquaporin Z.
/FTId=PRO_0000063989.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 30 33 Periplasmic. {ECO:0000255}.
TRANSMEM 34 54 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 55 81 Cytoplasmic. {ECO:0000255}.
TRANSMEM 82 102 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 103 130 Periplasmic. {ECO:0000255}.
TRANSMEM 131 151 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 152 155 Cytoplasmic. {ECO:0000255}.
TRANSMEM 156 176 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 177 201 Periplasmic. {ECO:0000255}.
TRANSMEM 202 222 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 223 231 Cytoplasmic. {ECO:0000255}.
MOTIF 63 65 NPA 1.
MOTIF 186 188 NPA 2.
SITE 20 20 Involved in tetramerization or stability
of the tetramer.
SITE 43 43 Selectivity filter.
SITE 174 174 Selectivity filter.
SITE 183 183 Selectivity filter.
SITE 189 189 Selectivity filter.
MUTAGEN 9 9 C->S: No effect.
{ECO:0000269|PubMed:10518952}.
MUTAGEN 20 20 C->S: Loss of oligomerization; no
alteration of water permeability.
{ECO:0000269|PubMed:10518952}.
MUTAGEN 183 183 T->C: No effect.
{ECO:0000269|PubMed:10518952}.
MUTAGEN 189 189 R->V,S: Loss of function.
{ECO:0000269|PubMed:10518952}.
CONFLICT 14 14 W -> C (in Ref. 2; BAA08441).
{ECO:0000305}.
CONFLICT 26 26 A -> P (in Ref. 2; BAA08441).
{ECO:0000305}.
CONFLICT 99 99 L -> V (in Ref. 1; AAC43518).
{ECO:0000305}.
HELIX 1 25 {ECO:0000244|PDB:2O9G}.
TURN 26 28 {ECO:0000244|PDB:2O9G}.
TURN 30 32 {ECO:0000244|PDB:2O9G}.
HELIX 35 58 {ECO:0000244|PDB:2O9G}.
HELIX 64 72 {ECO:0000244|PDB:2O9G}.
HELIX 78 80 {ECO:0000244|PDB:2O9G}.
HELIX 81 103 {ECO:0000244|PDB:2O9G}.
HELIX 111 114 {ECO:0000244|PDB:2O9G}.
HELIX 115 117 {ECO:0000244|PDB:2O9F}.
HELIX 122 124 {ECO:0000244|PDB:2O9G}.
STRAND 125 127 {ECO:0000244|PDB:2O9F}.
HELIX 131 152 {ECO:0000244|PDB:2O9G}.
HELIX 162 181 {ECO:0000244|PDB:2O9G}.
HELIX 187 197 {ECO:0000244|PDB:2O9G}.
HELIX 200 203 {ECO:0000244|PDB:2O9G}.
HELIX 205 226 {ECO:0000244|PDB:2O9G}.
SEQUENCE 231 AA; 23703 MW; 3BDE1A932D45CF14 CRC64;
MFRKLAAECF GTFWLVFGGC GSAVLAAGFP ELGIGFAGVA LAFGLTVLTM AFAVGHISGG
HFNPAVTIGL WAGGRFPAKE VVGYVIAQVV GGIVAAALLY LIASGKTGFD AAASGFASNG
YGEHSPGGYS MLSALVVELV LSAGFLLVIH GATDKFAPAG FAPIAIGLAL TLIHLISIPV
TNTSVNPARS TAVAIFQGGW ALEQLWFFWV VPIVGGIIGG LIYRTLLEKR D


Related products :

Catalog number Product name Quantity
27-715 Aquaporins_major intrinsic protein (MIP) are a family of water-selective membrane channels. Aquaporin 7 has greater sequence similarity with AQP3 and AQP9 and they may be a subfamily. Aquaporin 7 and 0.05 mg
EIAAB24799 Aquaporin-0,Lens fiber major intrinsic protein,MIP,Oryctolagus cuniculus,Rabbit
EIAAB24802 Aquaporin-0,Bos taurus,Bovine,Lens fiber major intrinsic protein,MIP,MIP26,MP26
EIAAB24798 Aquaporin-0,Lens fiber major intrinsic protein,Mip,MIP26,MP26,Rat,Rattus norvegicus
EIAAB24800 Aquaporin-0,Lens fiber major intrinsic protein,Mip,MIP26,Mouse,MP26,Mus musculus,Palm
EIAAB24801 AQP0,Aquaporin-0,Homo sapiens,Human,Lens fiber major intrinsic protein,MIP,MIP26,MP26
orb81171 Human Intrinsic Factor protein Intrinsic Facor Human Recombinant produced in baculovirus is glycosylated, polypeptide chain containing having a molecular mass of 55,000 Dalton. The Intrinsic Facor is 2
EIAAB24803 AQP0,Aquaporin-0,Chicken,Gallus gallus,Lens fiber major intrinsic protein,MIP,MIP26,MP26
EIAAB24797 AQP0,Aquaporin-0,Canis familiaris,Canis lupus familiaris,Dog,Lens fiber major intrinsic protein,MIP
orb81883 Intrinsic Factor, Pig protein Intrinsic Factor is a purified protein_bioactive peptide. For research use only. 100
5390-0004 NATIVE PIG INTRINSIC FACTOR, Product Type Purified Protein, Specificity INTRINSIC FACTOR, Target Species Pig, Host N_A, Format Purified, Isotypes , Applications FN, Clone 1 KU
SCH-5390-0004 NATIVE PIG INTRINSIC FACTOR, Product Type Purified Protein, Specificity INTRINSIC FACTOR, Target Species Pig, Host N_A, Format Purified, Isotypes , Applications FN, Clone 1 KU
EIAAB09968 460 kDa receptor,Cubilin,CUBN,Homo sapiens,Human,IFCR,Intestinal intrinsic factor receptor,Intrinsic factor-cobalamin receptor,Intrinsic factor-vitamin B12 receptor
27-570 RuvB-Like 2 (48-kDa TATA box-binding protein-interacting protein, Reptin 52, RUVBL2) is the second human homologue of the bacterial RuvB gene. Bacterial RuvB protein is a DNA helicase essential for ho 0.1 mg
E0579m ELISA Aqp1,AQP-1,Aquaporin-1,Aquaporin-CHIP,Delayed early response protein 2,DER2,Mouse,Mus musculus,Water channel protein for red blood cells and kidney proximal tubule 96T
U0579m CLIA Aqp1,AQP-1,Aquaporin-1,Aquaporin-CHIP,Delayed early response protein 2,DER2,Mouse,Mus musculus,Water channel protein for red blood cells and kidney proximal tubule 96T
E0579m ELISA kit Aqp1,AQP-1,Aquaporin-1,Aquaporin-CHIP,Delayed early response protein 2,DER2,Mouse,Mus musculus,Water channel protein for red blood cells and kidney proximal tubule 96T
E0579p ELISA AQP1,AQP-1,Aquaporin-1,Aquaporin-CHIP,Pig,Sus scrofa,Water channel protein for red blood cells and kidney proximal tubule 96T
U0579p CLIA AQP1,AQP-1,Aquaporin-1,Aquaporin-CHIP,Pig,Sus scrofa,Water channel protein for red blood cells and kidney proximal tubule 96T
E0579p ELISA kit AQP1,AQP-1,Aquaporin-1,Aquaporin-CHIP,Pig,Sus scrofa,Water channel protein for red blood cells and kidney proximal tubule 96T
E0579r ELISA kit Aqp1,AQP-1,Aquaporin-1,Aquaporin-CHIP,Chip28,Rat,Rattus norvegicus,Water channel protein for red blood cells and kidney proximal tubule 96T
U0579r CLIA Aqp1,AQP-1,Aquaporin-1,Aquaporin-CHIP,Chip28,Rat,Rattus norvegicus,Water channel protein for red blood cells and kidney proximal tubule 96T
E0579r ELISA Aqp1,AQP-1,Aquaporin-1,Aquaporin-CHIP,Chip28,Rat,Rattus norvegicus,Water channel protein for red blood cells and kidney proximal tubule 96T
20-783-73410 MOUSE ANTI PORCINE INTRINSIC FACTOR - Intrinsic factor; IF; INF Monoclonal 0.2 mg
18-003-42293 Aquaporin-7 - AQP-7; Aquaporin-7-like; Aquaporin adipose; AQPap Polyclonal 0.05 mg Aff Pur


 

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