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

Glutathione hydrolase 1 proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase 1) (Gamma-glutamyltranspeptidase 1) (GGT 1) (EC 2.3.2.2) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) (CD antigen CD224) [Cleaved into: Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain]

 GGT1_MOUSE              Reviewed;         568 AA.
Q60928;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-DEC-2018, entry version 159.
RecName: Full=Glutathione hydrolase 1 proenzyme;
EC=3.4.19.13 {ECO:0000250|UniProtKB:P19440};
AltName: Full=Gamma-glutamyltransferase 1;
AltName: Full=Gamma-glutamyltranspeptidase 1;
Short=GGT 1;
EC=2.3.2.2 {ECO:0000250|UniProtKB:P19440};
AltName: Full=Leukotriene-C4 hydrolase;
EC=3.4.19.14 {ECO:0000250|UniProtKB:P07314};
AltName: CD_antigen=CD224;
Contains:
RecName: Full=Glutathione hydrolase 1 heavy chain;
Contains:
RecName: Full=Glutathione hydrolase 1 light chain;
Flags: Precursor;
Name=Ggt1; Synonyms=Ggt, Ggtp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=8566783; DOI=10.1016/0378-1119(95)00618-4;
Shi Z.Z., Habib G.M., Lebovitz R.M., Lieberman M.W.;
"Cloning of cDNA and genomic structure of the mouse gamma-glutamyl
transpeptidase-encoding gene.";
Gene 167:233-237(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
GENE ORGANIZATION, AND ALTERNATIVE PROMOTER USAGE.
PubMed=10392451; DOI=10.1016/S0305-0491(99)00013-9;
Chikhi N., Holic N., Guellaen G., Laperche Y.;
"Gamma-glutamyl transpeptidase gene organization and expression: a
comparative analysis in rat, mouse, pig and human species.";
Comp. Biochem. Physiol. 122B:367-380(1999).
[4]
DISEASE.
PubMed=9139708; DOI=10.1074/jbc.272.19.12560;
Harding C.O., Williams P., Wagner E., Chang D.S., Wild K.,
Colwell R.E., Wolff J.A.;
"Mice with genetic gamma-glutamyl transpeptidase deficiency exhibit
glutathionuria, severe growth failure, reduced life spans, and
infertility.";
J. Biol. Chem. 272:12560-12567(1997).
[5]
DISEASE, AND FUNCTION.
PubMed=12810527; DOI=10.1210/en.2002-0071;
Levasseur R., Barrios R., Elefteriou F., Glass D.A. II,
Lieberman M.W., Karsenty G.;
"Reversible skeletal abnormalities in gamma-glutamyl transpeptidase-
deficient mice.";
Endocrinology 144:2761-2764(2003).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-114; ASN-229 AND ASN-510.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, and Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Cleaves the gamma-glutamyl bond of extracellular
glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other
gamma-glutamyl compounds. The metabolism of glutathione releases
free glutamate and the dipeptide cysteinyl-glycine, which is
hydrolyzed to cysteine and glycine by dipeptidases. In the
presence of high concentrations of dipeptides and some amino
acids, can also catalyze a transpeptidation reaction, transferring
the gamma-glutamyl moiety to an acceptor amino acid to form a new
gamma-glutamyl compound. Initiates extracellular glutathione (GSH)
breakdown, provides cells with a local cysteine supply and
contributes to maintain intracellular GSH level. It is part of the
cell antioxidant defense mechanism. Indirectly regulates multiple
aspects of skeletal biology. {ECO:0000269|PubMed:12810527}.
-!- CATALYTIC ACTIVITY:
Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-
[peptide] = 5-L-glutamyl amino acid + a [peptide] N-terminus;
Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
ChEBI:CHEBI:78608; EC=2.3.2.2;
Evidence={ECO:0000250|UniProtKB:P19440};
-!- CATALYTIC ACTIVITY:
Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
Evidence={ECO:0000250|UniProtKB:P19440};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + leukotriene C4 = L-glutamate + leukotriene D4;
Xref=Rhea:RHEA:31563, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
ChEBI:CHEBI:57973, ChEBI:CHEBI:63166; EC=3.4.19.14;
Evidence={ECO:0000250|UniProtKB:P07314};
-!- ACTIVITY REGULATION: Activated by autocatalytic cleavage.
{ECO:0000250|UniProtKB:P19440}.
-!- PATHWAY: Sulfur metabolism; glutathione metabolism.
-!- SUBUNIT: Heterodimer composed of the light and heavy chains. The
active site is located in the light chain.
{ECO:0000250|UniProtKB:P19440}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:P19440}.
-!- PTM: N-glycosylated on both chains.
{ECO:0000250|UniProtKB:P19440}.
-!- PTM: Cleaved by autocatalysis into a large and a small subunit and
the autocatalytic cleavage is essential to the functional
activation of the enzyme. {ECO:0000250|UniProtKB:P19440}.
-!- DISEASE: Note=Defects in Ggt1 are a cause of glutathionuria,
severe growth failure, reduced life spans and infertility. Ggt1-
deficient mice have multiple metabolic abnormalities and are
dwarf. Some abnormalities can be ameliorated by N-acetylcysteine
treatment. {ECO:0000269|PubMed:12810527,
ECO:0000269|PubMed:9139708}.
-!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
{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; U30509; AAA97395.1; -; mRNA.
EMBL; BC012969; AAH12969.1; -; mRNA.
CCDS; CCDS23927.1; -.
PIR; JC4570; JC4570.
RefSeq; NP_001292921.1; NM_001305992.1.
RefSeq; NP_032142.1; NM_008116.3.
RefSeq; XP_006513293.1; XM_006513230.3.
RefSeq; XP_006513294.1; XM_006513231.3.
UniGene; Mm.4559; -.
UniGene; Mm.486584; -.
ProteinModelPortal; Q60928; -.
SMR; Q60928; -.
IntAct; Q60928; 2.
MINT; Q60928; -.
STRING; 10090.ENSMUSP00000006508; -.
iPTMnet; Q60928; -.
PhosphoSitePlus; Q60928; -.
MaxQB; Q60928; -.
PaxDb; Q60928; -.
PRIDE; Q60928; -.
TopDownProteomics; Q60928; -.
Ensembl; ENSMUST00000006508; ENSMUSP00000006508; ENSMUSG00000006345.
Ensembl; ENSMUST00000134503; ENSMUSP00000121312; ENSMUSG00000006345.
GeneID; 14598; -.
KEGG; mmu:14598; -.
UCSC; uc007fqo.2; mouse.
CTD; 2678; -.
MGI; MGI:95706; Ggt1.
eggNOG; KOG2410; Eukaryota.
eggNOG; COG0405; LUCA.
GeneTree; ENSGT00940000154601; -.
HOGENOM; HOG000175620; -.
HOVERGEN; HBG005835; -.
InParanoid; Q60928; -.
KO; K18592; -.
OMA; TKNMFLD; -.
OrthoDB; EOG091G03Y3; -.
PhylomeDB; Q60928; -.
TreeFam; TF313608; -.
Reactome; R-MMU-174403; Glutathione synthesis and recycling.
Reactome; R-MMU-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
UniPathway; UPA00204; -.
ChiTaRS; Ggt1; mouse.
PRO; PR:Q60928; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000006345; Expressed in 126 organ(s), highest expression level in jejunum.
CleanEx; MM_GGT1; -.
ExpressionAtlas; Q60928; baseline and differential.
Genevisible; Q60928; MM.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:MGI.
GO; GO:0036374; F:glutathione hydrolase activity; ISS:UniProtKB.
GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
GO; GO:0002951; F:leukotriene-C(4) hydrolase; ISO:MGI.
GO; GO:0000048; F:peptidyltransferase activity; ISO:MGI.
GO; GO:0016755; F:transferase activity, transferring amino-acyl groups; ISO:MGI.
GO; GO:0006520; P:cellular amino acid metabolic process; ISO:MGI.
GO; GO:0019344; P:cysteine biosynthetic process; IMP:UniProtKB.
GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
GO; GO:0006750; P:glutathione biosynthetic process; IMP:UniProtKB.
GO; GO:0006751; P:glutathione catabolic process; ISS:UniProtKB.
GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
GO; GO:1901750; P:leukotriene D4 biosynthetic process; ISO:MGI.
GO; GO:0031179; P:peptide modification; ISO:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0002682; P:regulation of immune system process; IMP:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
GO; GO:0032355; P:response to estradiol; IBA:GO_Central.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0034612; P:response to tumor necrosis factor; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
InterPro; IPR000101; GGT_peptidase.
InterPro; IPR029055; Ntn_hydrolases_N.
PANTHER; PTHR11686; PTHR11686; 1.
SUPFAM; SSF56235; SSF56235; 1.
TIGRFAMs; TIGR00066; g_glut_trans; 1.
PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
1: Evidence at protein level;
Acyltransferase; Cell membrane; Complete proteome; Disulfide bond;
Glutathione biosynthesis; Glycoprotein; Hydrolase; Membrane; Protease;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix; Zymogen.
CHAIN 1 379 Glutathione hydrolase 1 heavy chain.
/FTId=PRO_0000011060.
CHAIN 380 568 Glutathione hydrolase 1 light chain.
/FTId=PRO_0000011061.
TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.
TRANSMEM 5 26 Helical; Signal-anchor for type II
membrane protein. {ECO:0000305}.
TOPO_DOM 27 568 Extracellular. {ECO:0000255}.
REGION 450 451 Glutamate binding. {ECO:0000250}.
ACT_SITE 380 380 Nucleophile. {ECO:0000250}.
BINDING 106 106 Glutamate. {ECO:0000250}.
BINDING 398 398 Glutamate. {ECO:0000250}.
BINDING 419 419 Glutamate. {ECO:0000250}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 343 343 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 510 510 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 49 73 {ECO:0000250}.
DISULFID 191 195 {ECO:0000250}.
SEQUENCE 568 AA; 61563 MW; 293C6E224FDC0766 CRC64;
MKNRFLVLGL VAVVLVFVII GLCIWLPYTS GKPDHVYSRA AVATDAKRCS EIGRDILQEG
GSVVDAAIAS LLCMGLMNAH SMGIGGGLFF TIYNSTTGKV EVINAREVAP RLANTTMFNN
SKDSEEGGLS VAVPGEIRGY ELAHQRHGRL PWARLFQPSI QLARHGFPVG KGLAIALDKK
RDVIEKTPAL CEVFCRQGKV LQEGETVTMP KLADTLQILA QEGAKAFYNG SLTAQIVKDI
QEAGGIMTVE DLNNYRAELI EHPMSIGLGD ATLYVPSAPL SGPVLILILN ILKGYNFSPK
SVATPEQKAL TYHRIVEAFR FAYAKRTMLG DPKFVDVSQV IRNMSSEFYA TQLRARITDE
TTHPAAYYEP EFYLQDDGGT AHLSAVSEDG SAVAATSTIN LYFGSKVLSR VSGILFNDEM
DDFSSPNFIN QFRVAPSPAN FIKPGKQPLS SMCPSIILDK DGQVRMVVGA SGGTQITTSV
ALAIINSLWF GYDVKRAVEE PRLHNQLLPN TTTVEKDIDQ VVTAGLKIRH HHTEVTPTFI
AVVQAVVRAS GGWAAASDSR KGGEPAGY


Related products :

Catalog number Product name Quantity
E1384077 gamma-Glutamyl Hydrolase (Conjugase, Folylpolygammaglutamyl Hydrolase) (GGH) ELISA Kit
GGNBP2 GGH Gene gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase)
E1381751 gamma-Glutamyl Hydrolase (Conjugase, Folylpolygammaglutamyl Hydrolase) (GGH) ELISA Kit 1
GGH-1399H Protein: Recombinant Human Gamma-Glutamyl Hydrolase (conjugase, folylpolygammaglutamyl hydrolase), His-tagged 0.5mg
GGH-1399H Protein Recombinant Human Gamma-Glutamyl Hydrolase (conjugase, folylpolygammaglutamyl hydrolase), His-tagged 0.5mg
CSB-EL009389RA Rat gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase) (GGH) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL009389HU Human gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase) (GGH) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL009389MO Mouse gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase) (GGH) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL009389BO Bovine gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase) (GGH) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
E0752m ELISA ADP-ribosyl cyclase 1,cADPr hydrolase 1,Cd38,Cyclic ADP-ribose hydrolase 1,I-19,Mouse,Mus musculus,NIM-R5 antigen 96T
U0752m CLIA ADP-ribosyl cyclase 1,cADPr hydrolase 1,Cd38,Cyclic ADP-ribose hydrolase 1,I-19,Mouse,Mus musculus,NIM-R5 antigen 96T
E0752m ELISA kit ADP-ribosyl cyclase 1,cADPr hydrolase 1,Cd38,Cyclic ADP-ribose hydrolase 1,I-19,Mouse,Mus musculus,NIM-R5 antigen 96T
LF-PA40672 anti-Leukotriene A4 Hydrolase (LTA4H) , Rabbit polyclonal to Leukotriene A4 Hydrolase (LTA4H) , Isotype IgG, Host Rabbit 50 ug
20-783-70012 MOUSE ANTI HUMAN CD38 - EC 3.2.2.5; Cyclic ADP-ribose hydrolase 1; cADPr hydrolase 1; T10; CD38 antigen Monoclonal 0.2 mg
20-783-70016 MOUSE ANTI HUMAN CD38 - EC 3.2.2.5; Cyclic ADP-ribose hydrolase 1; cADPr hydrolase 1; T10; CD38 antigen Monoclonal 0.02 mg
20-783-70596 RAT ANTI MOUSE CD38 FITC - EC 3.2.2.5; Cyclic ADP-ribose hydrolase 1; cADPr hydrolase 1; T10; CD38 antigen Monoclonal 0.1 mg
20-783-70015 MOUSE ANTI HUMAN CD38 RPE - EC 3.2.2.5; Cyclic ADP-ribose hydrolase 1; cADPr hydrolase 1; T10; CD38 antigen Monoclonal 100 TESTS
20-783-70845 MOUSE ANTI HUMAN CD38 RPE-Cy5 - EC 3.2.2.5; Cyclic ADP-ribose hydrolase 1; cADPr hydrolase 1; T10; CD38 antigen Monoclonal 100 TESTS
20-783-70014 MOUSE ANTI HUMAN CD38 FITC - EC 3.2.2.5; Cyclic ADP-ribose hydrolase 1; cADPr hydrolase 1; T10; CD38 antigen Monoclonal 0.1 mg
20-783-70013 MOUSE ANTI HUMAN CD38 Biotin - EC 3.2.2.5; Cyclic ADP-ribose hydrolase 1; cADPr hydrolase 1; T10; CD38 antigen Monoclonal 0.1 mg
20-783-70597 RAT ANTI MOUSE CD38 RPE - EC 3.2.2.5; Cyclic ADP-ribose hydrolase 1; cADPr hydrolase 1; T10; CD38 antigen Monoclonal 0.1 mg
20-783-70598 RAT ANTI MOUSE CD38 - EC 3.2.2.5; Cyclic ADP-ribose hydrolase 1; cADPr hydrolase 1; T10; CD38 antigen Monoclonal 0.2 mg
20-783-70017 MOUSE ANTI HUMAN CD38 Azide Free - EC 3.2.2.5; Cyclic ADP-ribose hydrolase 1; cADPr hydrolase 1; T10; CD38 antigen Monoclonal 1 mg
abx111230 Polyclonal Rabbit Biphenyl Hydrolase-Like (Serine Hydrolase) Antibody 50 μl
BPIL1 BPHL Gene biphenyl hydrolase-like (serine hydrolase)


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | 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 | 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 | 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 | Gentaur