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

cGMP-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) (Cyclic GMP-stimulated phosphodiesterase) (CGS-PDE) (cGSPDE)

 PDE2A_RAT               Reviewed;         928 AA.
Q01062;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
20-DEC-2017, entry version 139.
RecName: Full=cGMP-dependent 3',5'-cyclic phosphodiesterase;
EC=3.1.4.17;
AltName: Full=Cyclic GMP-stimulated phosphodiesterase;
Short=CGS-PDE;
Short=cGSPDE;
Name=Pde2a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=7811274; DOI=10.1006/bbrc.1994.2886;
Yang Q., Paskind M., Bolger G., Thompson W.J., Repaske D.R.,
Cutler L.S., Epstein P.M.;
"A novel cyclic GMP stimulated phosphodiesterase from rat brain.";
Biochem. Biophys. Res. Commun. 205:1850-1858(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 643-759.
PubMed=1326532;
Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.;
"A polymerase chain reaction strategy to identify and clone cyclic
nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA
encoding the 63-kDa calmodulin-dependent phosphodiesterase.";
J. Biol. Chem. 267:18683-18688(1992).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=28463107; DOI=10.7554/eLife.21374;
Monterisi S., Lobo M.J., Livie C., Castle J.C., Weinberger M.,
Baillie G., Surdo N.C., Musheshe N., Stangherlin A., Gottlieb E.,
Maizels R., Bortolozzi M., Micaroni M., Zaccolo M.;
"PDE2A2 regulates mitochondria morphology and apoptotic cell death via
local modulation of cAMP/PKA signalling.";
Elife 6:0-0(2017).
-!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-
specificity for the second messengers cAMP and cGMP, which are key
regulators of many important physiological processes.
{ECO:0000250}.
-!- FUNCTION: Isoform PDE2A2: Regulates mitochondrial cAMP levels and
respiration. Involved in the regulation of mitochondria
morphology/dynamics and apoptotic cell death via local modulation
of cAMP/PKA signaling in the mitochondrion, including the
monitoring of local cAMP levels at the outer mitochondrial
membrane and of PKA-dependent phosphorylation of Dnm1l.
{ECO:0000269|PubMed:28463107}.
-!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
nucleoside 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=Binds 2 divalent metal cations per subunit. Site 1 may
preferentially bind zinc ions, while site 2 has a preference for
magnesium and/or manganese ions. {ECO:0000250};
-!- ENZYME REGULATION: Specifically inhibited by Bay 60-7550. When
repressed, protected from ionomycin- but not staurosporin-induced
cell death. {ECO:0000269|PubMed:28463107}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- INTERACTION:
Q5FWY5:Aip; NbExp=2; IntAct=EBI-1786062, EBI-1786045;
-!- SUBCELLULAR LOCATION: Isoform PDE2A3: Cell membrane
{ECO:0000269|PubMed:28463107}; Peripheral membrane protein
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform PDE2A1: Cytoplasm
{ECO:0000269|PubMed:28463107}.
-!- SUBCELLULAR LOCATION: Isoform PDE2A2: Mitochondrion
{ECO:0000269|PubMed:28463107}. Mitochondrion inner membrane
{ECO:0000269|PubMed:28463107}. Mitochondrion outer membrane
{ECO:0000269|PubMed:28463107}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist. Experimental
confirmation may be lacking for some isoforms.;
Name=PDE2A3;
IsoId=Q01062-1; Sequence=Displayed;
Name=PDE2A1;
IsoId=Q01062-2; Sequence=Not described;
Name=PDE2A2;
IsoId=Q01062-3; Sequence=Not described;
-!- TISSUE SPECIFICITY: Brain.
-!- DOMAIN: GAF 1 functions as a dimerization domain, whereas GAF 2
binds cGMP, which causes activation of the catalytic activity of
the enzyme. {ECO:0000250}.
-!- MISCELLANEOUS: cGMP binds at an allosteric activator site.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE2 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U21101; AAA63683.1; -; mRNA.
EMBL; M94540; AAA40922.1; -; mRNA.
PIR; JC2486; JC2486.
RefSeq; NP_001137319.1; NM_001143847.1.
RefSeq; NP_112341.1; NM_031079.1. [Q01062-1]
UniGene; Rn.10044; -.
ProteinModelPortal; Q01062; -.
SMR; Q01062; -.
IntAct; Q01062; 1.
STRING; 10116.ENSRNOP00000026586; -.
BindingDB; Q01062; -.
ChEMBL; CHEMBL4650; -.
iPTMnet; Q01062; -.
PhosphoSitePlus; Q01062; -.
SwissPalm; Q01062; -.
PaxDb; Q01062; -.
PRIDE; Q01062; -.
GeneID; 81743; -.
KEGG; rno:81743; -.
UCSC; RGD:620965; rat. [Q01062-1]
CTD; 5138; -.
RGD; 620965; Pde2a.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
HOGENOM; HOG000007068; -.
HOVERGEN; HBG053540; -.
InParanoid; Q01062; -.
KO; K18283; -.
PhylomeDB; Q01062; -.
BRENDA; 3.1.4.17; 5301.
SABIO-RK; Q01062; -.
PRO; PR:Q01062; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; ISO:RGD.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISO:RGD.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0097457; C:hippocampal mossy fiber; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0030552; F:cAMP binding; IDA:RGD.
GO; GO:0030553; F:cGMP binding; IDA:RGD.
GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IDA:RGD.
GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; ISS:UniProtKB.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0036004; F:GAF domain binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0030911; F:TPR domain binding; ISO:RGD.
GO; GO:0035904; P:aorta development; ISO:RGD.
GO; GO:0006198; P:cAMP catabolic process; IDA:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:UniProtKB.
GO; GO:0003279; P:cardiac septum development; ISO:RGD.
GO; GO:0071321; P:cellular response to cGMP; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
GO; GO:0046069; P:cGMP catabolic process; IDA:RGD.
GO; GO:0019934; P:cGMP-mediated signaling; ISS:UniProtKB.
GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
GO; GO:0061028; P:establishment of endothelial barrier; IDA:UniProtKB.
GO; GO:0007507; P:heart development; ISO:RGD.
GO; GO:0003170; P:heart valve development; ISO:RGD.
GO; GO:0030224; P:monocyte differentiation; ISO:RGD.
GO; GO:0030818; P:negative regulation of cAMP biosynthetic process; IMP:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
GO; GO:0033159; P:negative regulation of protein import into nucleus, translocation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0043116; P:negative regulation of vascular permeability; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0043117; P:positive regulation of vascular permeability; ISS:UniProtKB.
GO; GO:0006626; P:protein targeting to mitochondrion; IMP:UniProtKB.
GO; GO:0030823; P:regulation of cGMP metabolic process; ISO:RGD.
GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB.
GO; GO:1904880; P:response to hydrogen sulfide; IEP:RGD.
GO; GO:0003281; P:ventricular septum development; ISO:RGD.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
Gene3D; 3.30.450.40; -; 3.
InterPro; IPR003018; GAF.
InterPro; IPR029016; GAF-like_dom_sf.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
Pfam; PF01590; GAF; 1.
Pfam; PF13185; GAF_2; 1.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00065; GAF; 3.
SMART; SM00471; HDc; 1.
SUPFAM; SSF55781; SSF55781; 3.
PROSITE; PS00126; PDEASE_I_1; 1.
PROSITE; PS51845; PDEASE_I_2; 1.
1: Evidence at protein level;
Alternative splicing; cAMP; Cell membrane; cGMP; cGMP-binding;
Complete proteome; Cytoplasm; Hydrolase; Membrane; Metal-binding;
Mitochondrion; Mitochondrion inner membrane;
Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 928 cGMP-dependent 3',5'-cyclic
phosphodiesterase.
/FTId=PRO_0000198798.
DOMAIN 228 365 GAF 1. {ECO:0000255}.
DOMAIN 397 536 GAF 2. {ECO:0000255}.
DOMAIN 566 890 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
REGION 644 648 Substrate binding. {ECO:0000250}.
ACT_SITE 644 644 Proton donor. {ECO:0000250}.
METAL 648 648 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
METAL 684 684 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
METAL 685 685 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
METAL 685 685 Divalent metal cation 2.
{ECO:0000250|UniProtKB:O00408}.
METAL 796 796 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O00408}.
BINDING 419 419 cGMP. {ECO:0000250|UniProtKB:Q922S4}.
BINDING 434 434 cGMP. {ECO:0000250|UniProtKB:Q922S4}.
BINDING 487 487 cGMP. {ECO:0000250|UniProtKB:Q922S4}.
BINDING 685 685 Substrate. {ECO:0000250}.
BINDING 796 796 Substrate. {ECO:0000250}.
MOD_RES 109 109 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CONFLICT 646 646 W -> R (in Ref. 2; AAA40922).
{ECO:0000305}.
CONFLICT 758 758 L -> M (in Ref. 2). {ECO:0000305}.
SEQUENCE 928 AA; 104664 MW; EF0B8C1E266EAB18 CRC64;
MVLVLHHILI AVVQFLRRGQ QVFLKPDEPP PQPCADSLQD ALLSLGAVID IAGLRQAAKD
ALSAVLPKVE TVYTYLVDGE SRLVCEDPPH ELPQEGKIRE AVISRKRLSC DGLGPSDLLG
KPLARLVAPL APDTQVLVIP LLDKETGTVA AVILVHCGQL SDSEEQSLQV VEKHALVALQ
RVQALQQRRP EAVQNTSADP SEDQKDEKGY TAHDRKILQL CGELYDLDAT SLQLKVLRYL
QQETQATHCC LLLVSEDNLQ LSCKVIGEKV LGEEVSFPLT MGRLGQVVED KQCIQLKDLT
SDDVQQLQNM LGCELRAMLC VPVISRATDQ VVALACAFNK LGGDFFTDED ERAIQHCFHY
TGTVLTSTLA FQKEQKLKCE CQALLQVAKN LFTHLDDVSV LLQEIITEAR NLSNAEICSV
FLLDQNELVA KVFDGGVVDD ESYEIRIPAD QGIAGHVATT GQILNIPDAY AHPLFYRGVD
DSTGFRTRNI LCFPIKNENQ EVIGVAELVN KINGPWFSKF DEDLATAFSI YCGISIAHSL
LYKKVNEAQY RSHLANEMMM YHMKVSDDEY TKLLHDGIQP VAAIDSNFAN FTYTPRSLPE
DDTSMAILSM LQDMNFINNY KIDCPTLARF CLMVKKGYRD PPYHNWMHAF SVSHFCYLLY
KNLELSNYLE DIEIFALFIS CMCHDLDHRG TNNSFQVASK SVLAALYSSE GSVMERHHFA
QAIAILNTHG CNIFDHFSRK DYQRMLDLMR DIILATDLAH HLRIFKDLQK MAEVGYDRNN
KQHHRLLLCL LMTSCDLSDQ TKGWKTTRKI AELIYKEFFS QGDLEKAMGN RPMEMMDREK
AYIPELQISF MEHIAMPIYK LLQDLFPKAA ELYERVASNR EHWTKVSHKF TIRGLPSNNS
LDFLDEEYEV PDLDVTRAPV NGCCSLEG


Related products :

Catalog number Product name Quantity
EIAAB30305 cGMP-dependent 3',5'-cyclic phosphodiesterase,cGSPDE,CGS-PDE,Cyclic GMP-stimulated phosphodiesterase,Homo sapiens,Human,PDE2A
EIAAB30304 cGMP-dependent 3',5'-cyclic phosphodiesterase,cGSPDE,CGS-PDE,Cyclic GMP-stimulated phosphodiesterase,Mouse,Mus musculus,Pde2a
EIAAB30303 cGMP-dependent 3',5'-cyclic phosphodiesterase,cGSPDE,CGS-PDE,Cyclic GMP-stimulated phosphodiesterase,Pde2a,Rat,Rattus norvegicus
EIAAB30306 Bos taurus,Bovine,cGMP-dependent 3',5'-cyclic phosphodiesterase,cGSPDE,CGS-PDE,Cyclic GMP-stimulated phosphodiesterase,PDE2A
18-783-75530 RABBIT ANTI HUMAN PHOSPHODIESTERASE 2A (N-TERMINAL) - PDE2A; EC 3.1.4.17; Cyclic GMP-stimulated phosphodiesterase; CGS-PDE; cGSPDE Polyclonal 0.05 mg
EIAAB30312 CGIP1,CGI-PDE B,CGIPDE1,cGMP-inhibited 3',5'-cyclic phosphodiesterase B,Cyclic GMP-inhibited phosphodiesterase B,Homo sapiens,Human,PDE3B
EIAAB30309 CGI-PDE A,cGMP-inhibited 3',5'-cyclic phosphodiesterase A,Cyclic GMP-inhibited phosphodiesterase A,Homo sapiens,Human,PDE3A
EIAAB30311 CGI-PDE B,CGIPDE1,cGMP-inhibited 3',5'-cyclic phosphodiesterase B,Cyclic GMP-inhibited phosphodiesterase B,Pde3b,Rat,Rattus norvegicus
EIAAB30310 CGI-PDE B,CGIPDE1,cGMP-inhibited 3',5'-cyclic phosphodiesterase B,Cyclic GMP-inhibited phosphodiesterase B,Mouse,Mus musculus,Pde3b
EIAAB30339 cGMP phosphodiesterase 6C,Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha',Mouse,Mus musculus,Pde6c
EIAAB30340 Bos taurus,Bovine,cGMP phosphodiesterase 6C,Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha',PDE V-C1,PDE6C,PDEA2
EIAAB30308 CGI-PDE A,cGMP-inhibited 3',5'-cyclic phosphodiesterase A,Cyclic GMP-inhibited phosphodiesterase A,Pde3a,Rat,Rattus norvegicus
EIAAB30307 CGI-PDE A,cGMP-inhibited 3',5'-cyclic phosphodiesterase A,Cyclic GMP-inhibited phosphodiesterase A,Mouse,Mus musculus,Pde3a
EIAAB30338 cGMP phosphodiesterase 6C,Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha',Homo sapiens,Human,PDE6C,PDEA2
EIAAB30328 CGB-PDE,cGMP-binding cGMP-specific phosphodiesterase,cGMP-specific 3',5'-cyclic phosphodiesterase,Homo sapiens,Human,PDE5,PDE5A
EIAAB30327 CGB-PDE,cGMP-binding cGMP-specific phosphodiesterase,cGMP-specific 3',5'-cyclic phosphodiesterase,Pde5,Pde5a,Rat,Rattus norvegicus
EIAAB30326 CGB-PDE,cGMP-binding cGMP-specific phosphodiesterase,cGMP-specific 3',5'-cyclic phosphodiesterase,Mouse,Mus musculus,Pde5,Pde5a
EIAAB30325 Bos taurus,Bovine,CGB-PDE,cGMP-binding cGMP-specific phosphodiesterase,cGMP-specific 3',5'-cyclic phosphodiesterase,PDE5,PDE5A
E0379h Bovine ELISA Kit FOR cGMP-dependent 3',5'-cyclic phosphodiesterase 96T
CCDC9_MOUSE Bovine ELISA Kit FOR cGMP-dependent 3',5'-cyclic phosphodiesterase 96T
MET20_RAT Bovine ELISA Kit FOR cGMP-dependent 3',5'-cyclic phosphodiesterase 96T
EIAAB30287 cAMP and cGMP phosphodiesterase 11A,Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A,Pde11a,Rat,Rattus norvegicus
EIAAB30288 cAMP and cGMP phosphodiesterase 11A,Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A,Mouse,Mus musculus,Pde11a
EIAAB30286 cAMP and cGMP phosphodiesterase 11A,Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A,Homo sapiens,Human,PDE11A
EIAAB30337 cGMP phosphodiesterase 6C,Chicken,Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha',Gallus gallus,PDE6C


 

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