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

FAS-associated death domain protein (FAS-associating death domain-containing protein) (Mediator of receptor induced toxicity) (Protein FADD)

 FADD_MOUSE              Reviewed;         205 AA.
Q61160; Q3TC37; Q61082;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
23-MAY-2018, entry version 160.
RecName: Full=FAS-associated death domain protein;
AltName: Full=FAS-associating death domain-containing protein;
AltName: Full=Mediator of receptor induced toxicity;
AltName: Full=Protein FADD;
Name=Fadd; Synonyms=Mort1;
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].
PubMed=8649383; DOI=10.1128/MCB.16.6.2756;
Zhang J., Winoto A.;
"A mouse Fas-associated protein with homology to the human Mort1/FADD
protein is essential for Fas-induced apoptosis.";
Mol. Cell. Biol. 16:2756-2763(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8565075; DOI=10.1016/S0092-8674(00)80984-8;
Hsu H., Shu H.-B., Pan M.G., Goeddel D.V.;
"TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF
receptor 1 signal transduction pathways.";
Cell 84:299-308(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary gland, and Salivary gland;
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).
[5]
INTERACTION WITH NOL3.
PubMed=15383280; DOI=10.1016/j.molcel.2004.08.020;
Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B.,
Hayakawa Y., Lee P., Korsmeyer S.J., Kitsis R.N.;
"Inhibition of both the extrinsic and intrinsic death pathways through
nonhomotypic death-fold interactions.";
Mol. Cell 15:901-912(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
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).
[7]
STRUCTURE BY NMR OF 89-183.
PubMed=10347191; DOI=10.1074/jbc.274.23.16337;
Jeong E.-J., Bang S., Lee T.H., Park Y.-I., Sim W.-S., Kim K.-S.;
"The solution structure of FADD death domain. Structural basis of
death domain interactions of Fas and FADD.";
J. Biol. Chem. 274:16337-16342(1999).
-!- FUNCTION: Apoptotic adaptor molecule that recruits caspase-8 or
caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The
resulting aggregate called the death-inducing signaling complex
(DISC) performs caspase-8 proteolytic activation. Active caspase-8
initiates the subsequent cascade of caspases mediating apoptosis
(By similarity). Involved in interferon-mediated antiviral immune
response, playing a role in the positive regulation of interferon
signaling (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with CFLAR, PEA15 and MBD4. When
phosphorylated, part of a complex containing HIPK3 and FAS. May
interact with MAVS/IPS1. Interacts with PIDD1 (By similarity).
Interacts with FAS (By similarity). Interacts directly (via DED
domain) with NOL3 (via CARD domain); inhibits death-inducing
signaling complex (DISC) assembly by inhibiting the increase in
FAS-FADD binding induced by FAS activation. {ECO:0000250,
ECO:0000269|PubMed:15383280}.
-!- INTERACTION:
O89110:Casp8; NbExp=6; IntAct=EBI-524415, EBI-851690;
P25446:Fas; NbExp=3; IntAct=EBI-524415, EBI-296206;
Q60855:Ripk1; NbExp=9; IntAct=EBI-524415, EBI-529119;
Q9QZL0:Ripk3; NbExp=6; IntAct=EBI-524415, EBI-2367423;
-!- DOMAIN: Contains a death domain involved in the binding of the
corresponding domain within Fas receptor.
-!- PTM: Phosphorylated.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U50406; AAB07789.1; -; mRNA.
EMBL; U43184; AAA97876.1; -; mRNA.
EMBL; AK084808; BAC39283.1; -; mRNA.
EMBL; AK169798; BAE41374.1; -; mRNA.
EMBL; AK170927; BAE42120.1; -; mRNA.
EMBL; BC004584; AAH04584.1; -; mRNA.
EMBL; BC021400; AAH21400.1; -; mRNA.
CCDS; CCDS22050.1; -.
RefSeq; NP_034305.1; NM_010175.5.
UniGene; Mm.5126; -.
PDB; 1FAD; NMR; -; A=89-183.
PDBsum; 1FAD; -.
ProteinModelPortal; Q61160; -.
SMR; Q61160; -.
BioGrid; 199586; 13.
DIP; DIP-34771N; -.
IntAct; Q61160; 15.
MINT; Q61160; -.
STRING; 10090.ENSMUSP00000033394; -.
iPTMnet; Q61160; -.
PhosphoSitePlus; Q61160; -.
EPD; Q61160; -.
MaxQB; Q61160; -.
PaxDb; Q61160; -.
PeptideAtlas; Q61160; -.
PRIDE; Q61160; -.
Ensembl; ENSMUST00000033394; ENSMUSP00000033394; ENSMUSG00000031077.
GeneID; 14082; -.
KEGG; mmu:14082; -.
UCSC; uc009kql.1; mouse.
CTD; 8772; -.
MGI; MGI:109324; Fadd.
eggNOG; ENOG410J0KM; Eukaryota.
eggNOG; ENOG41122TX; LUCA.
GeneTree; ENSGT00390000002105; -.
HOGENOM; HOG000112490; -.
HOVERGEN; HBG000853; -.
InParanoid; Q61160; -.
KO; K02373; -.
OMA; CQMNLVA; -.
OrthoDB; EOG091G0SHT; -.
PhylomeDB; Q61160; -.
TreeFam; TF102046; -.
Reactome; R-MMU-140534; Ligand-dependent caspase activation.
Reactome; R-MMU-2562578; TRIF-mediated programmed cell death.
Reactome; R-MMU-3371378; Regulation by c-FLIP.
Reactome; R-MMU-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-MMU-5218900; CASP8 activity is inhibited.
Reactome; R-MMU-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-MMU-69416; Dimerization of procaspase-8.
Reactome; R-MMU-75157; FasL/ CD95L signaling.
Reactome; R-MMU-75158; TRAIL signaling.
EvolutionaryTrace; Q61160; -.
PRO; PR:Q61160; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000031077; -.
CleanEx; MM_FADD; -.
Genevisible; Q61160; MM.
GO; GO:0031265; C:CD95 death-inducing signaling complex; ISO:MGI.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031264; C:death-inducing signaling complex; ISO:MGI.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0097342; C:ripoptosome; ISS:UniProtKB.
GO; GO:0089720; F:caspase binding; ISO:MGI.
GO; GO:0035877; F:death effector domain binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; ISO:MGI.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI.
GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
GO; GO:0048738; P:cardiac muscle tissue development; TAS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; ISO:MGI.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0048535; P:lymph node development; IGI:UniProtKB.
GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI.
GO; GO:0097527; P:necroptotic signaling pathway; ISO:MGI.
GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; IMP:UniProtKB.
GO; GO:0060546; P:negative regulation of necroptotic process; IGI:MGI.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IMP:UniProtKB.
GO; GO:0002821; P:positive regulation of adaptive immune response; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:2000454; P:positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation; IMP:UniProtKB.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IGI:MGI.
GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IGI:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
GO; GO:0045651; P:positive regulation of macrophage differentiation; ISO:MGI.
GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISO:MGI.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:0048536; P:spleen development; IGI:UniProtKB.
GO; GO:0030217; P:T cell differentiation; TAS:UniProtKB.
GO; GO:0033077; P:T cell differentiation in thymus; IMP:UniProtKB.
GO; GO:0043029; P:T cell homeostasis; IMP:UniProtKB.
GO; GO:0048538; P:thymus development; IGI:UniProtKB.
GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; ISO:MGI.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR001875; DED_dom.
InterPro; IPR016729; FADD.
Pfam; PF00531; Death; 1.
Pfam; PF01335; DED; 1.
PIRSF; PIRSF018586; FADD; 1.
SMART; SM00005; DEATH; 1.
SMART; SM00031; DED; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS50168; DED; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Immunity; Innate immunity;
Phosphoprotein; Reference proteome.
CHAIN 1 205 FAS-associated death domain protein.
/FTId=PRO_0000191280.
DOMAIN 3 81 DED. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
DOMAIN 97 181 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
MOD_RES 191 191 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 168 168 C -> F (in Ref. 2; AAA97876).
{ECO:0000305}.
HELIX 94 118 {ECO:0000244|PDB:1FAD}.
HELIX 123 132 {ECO:0000244|PDB:1FAD}.
HELIX 137 152 {ECO:0000244|PDB:1FAD}.
HELIX 153 156 {ECO:0000244|PDB:1FAD}.
HELIX 158 168 {ECO:0000244|PDB:1FAD}.
HELIX 171 181 {ECO:0000244|PDB:1FAD}.
SEQUENCE 205 AA; 22960 MW; 4BC8D86B33A58783 CRC64;
MDPFLVLLHS LSGSLSGNDL MELKFLCRER VSKRKLERVQ SGLDLFTVLL EQNDLERGHT
GLLRELLASL RRHDLLQRLD DFEAGTATAA PPGEADLQVA FDIVCDNVGR DWKRLARELK
VSEAKMDGIE EKYPRSLSER VRESLKVWKN AEKKNASVAG LVKALRTCRL NLVADLVEEA
QESVSKSENM SPVLRDSTVS SSETP


Related products :

Catalog number Product name Quantity
EIAAB14324 Fadd,FAS-associated death domain protein,FAS-associating death domain-containing protein,Mediator of receptor induced toxicity,Mort1,Mouse,Mus musculus,Protein FADD
EIAAB14326 FADD,FAS-associated death domain protein,FAS-associating death domain-containing protein,GIG3,Growth-inhibiting gene 3 protein,Homo sapiens,Human,Mediator of receptor induced toxicity,MORT1,Protein FA
18-003-43791 Protein FADD - FAS-associated death domain protein; FAS-associating death domain-containing protein; Mediator of receptor induced toxicity Polyclonal 0.05 mg Aff Pur
20-272-190237 FADD - Mouse monoclonal [FD19] to FADD; FAS-associated death domain protein; FAS-associating death domain-containing protein; Mediator of receptor induced toxicity Monoclonal 0.1 ml
18-272-196807 FADD - Rabbit polyclonal to FADD; FAS-associated death domain protein; FAS-associating death domain-containing protein; Mediator of receptor induced toxicity Polyclonal 0.25 mg
18-003-42868 FADD protein - FAS-associating death domain-containing protein; Mediator of receptor induced toxicity Polyclonal 0.05 mg Aff Pur
EIAAB14325 Bos taurus,Bovine,FADD,FAS-associated death domain protein,FAS-associating death domain-containing protein,Protein FADD
EIAAB43761 Homo sapiens,Human,TNFR1-associated DEATH domain protein,TNFRSF1A-associated via death domain,TRADD,Tumor necrosis factor receptor type 1-associated DEATH domain protein
EIAAB43759 Mouse,Mus musculus,TNFR1-associated DEATH domain protein,TNFRSF1A-associated via death domain,Tradd,Tumor necrosis factor receptor type 1-associated DEATH domain protein
EIAAB43760 Bos taurus,Bovine,TNFR1-associated DEATH domain protein,TNFRSF1A-associated via death domain,TRADD,Tumor necrosis factor receptor type 1-associated DEATH domain protein
EIAAB31046 Homo sapiens,Human,Leucine-rich repeat and death domain-containing protein,LRDD,p53-induced protein with a death domain,PIDD
EIAAB31045 Leucine-rich repeat and death domain-containing protein,Lrdd,Mouse,Mus musculus,p53-induced protein with a death domain,Pidd
18-661-15008 Death domain-containing protein CRADD - Caspase and RIP adapter with death domain; RIP-associated protein with a death domain Polyclonal 0.1 mg
18-661-15009 Death domain-containing protein CRADD - Caspase and RIP adapter with death domain; RIP-associated protein with a death domain Polyclonal 0.1 mg
EIAAB09252 Caspase and RIP adapter with death domain,CRADD,Death domain-containing protein CRADD,Homo sapiens,Human,RAIDD,RIP-associated protein with a death domain
EIAAB09251 Caspase and RIP adapter with death domain,Cradd,Death domain-containing protein CRADD,Mouse,Mus musculus,Raidd,RIP-associated protein with a death domain
EIAAB10423 BING2,DAP6,Daxx,DAXX,Death domain-associated protein 6,EAP1,ETS1-associated protein 1,Fas death domain-associated protein,hDaxx,Homo sapiens,Human
bs-0511P Peptides: FADD (Fas-associated protein with death domain) Protein Length:12-25 amino acids. 200ug lyophilized
orb81113 Human Fas-Associated Death Domain protein FADD produced in E.coli is a single, non-glycosylated polypeptide chain containing 244 amino acids (1-208 a.a.) and having a molecular mass of 27.4 kDa.FADD i 2
BPA1052 Fas-Associated protein with Death Domain, FADD Polyclonal Antibodie 100 μg
EIAAB10849 DED-containing protein FLAME-3,Dedd2,DNA-binding death effector domain-containing protein 2,FADD-like anti-apoptotic molecule 3,Flame3,Mouse,Mus musculus
BPA1052 Fas-Associated protein with Death Domain, FADD, Polyclonal primary Antibodies 100 μg
FADD-381H Protein: Recombinant Human Fas (TNFRSF6)-associated Via Death Domain, GST tagged 20ug
FADD-381H Protein Recombinant Human Fas (TNFRSF6)-associated Via Death Domain, GST tagged 20ug
EIAAB10848 DED-containing protein FLAME-3,DEDD2,DNA-binding death effector domain-containing protein 2,FADD-like anti-apoptotic molecule 3,FLAME3,Homo sapiens,Human,PSEC0004


 

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