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

Proto-oncogene c-Fos (Cellular oncogene fos)

 FOS_RAT                 Reviewed;         380 AA.
P12841; Q4FDN1;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
22-NOV-2017, entry version 154.
RecName: Full=Proto-oncogene c-Fos;
AltName: Full=Cellular oncogene fos;
Name=Fos;
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].
PubMed=3325886;
Curran T., Gordon M.B., Rubino K.L., Sambucetti L.C.;
"Isolation and characterization of the c-fos(rat) cDNA and analysis of
post-translational modification in vitro.";
Oncogene 2:79-84(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
Weiler E.;
"cFOS expression in rat.";
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
DNA-BINDING.
PubMed=2105492; DOI=10.1073/pnas.87.3.1032;
Abate C., Luk D., Gentz R., Rauscher F.J. III, Curran T.;
"Expression and purification of the leucine zipper and DNA-binding
domains of Fos and Jun: both Fos and Jun contact DNA directly.";
Proc. Natl. Acad. Sci. U.S.A. 87:1032-1036(1990).
[4]
INTERACTION WITH MAFB.
PubMed=9571165; DOI=10.1006/bbrc.1998.8447;
Matsushima-Hibiya Y., Nishi S., Sakai M.;
"Rat maf-related factors: the specificities of DNA binding and
heterodimer formation.";
Biochem. Biophys. Res. Commun. 245:412-418(1998).
[5]
PHOSPHORYLATION AT THR-232, FUNCTION, AND MUTAGENESIS OF THR-232.
PubMed=7816602; DOI=10.1093/nar/22.24.5173;
Bannister A.J., Brown H.J., Sutherland J.A., Kouzarides T.;
"Phosphorylation of the c-Fos and c-Jun HOB1 motif stimulates its
activation capacity.";
Nucleic Acids Res. 22:5173-5176(1994).
[6]
PHOSPHORYLATION AT THR-325; THR-331; SER-362 AND SER-374, FUNCTION,
AND MUTAGENESIS OF THR-325; THR-331; 343-PHE--TYR-345; SER-362 AND
SER-374.
PubMed=17223854; DOI=10.1111/j.1471-4159.2006.04250.x;
Pellegrino M.J., Stork P.J.;
"Sustained activation of extracellular signal-regulated kinase by
nerve growth factor regulates c-fos protein stabilization and
transactivation in PC12 cells.";
J. Neurochem. 99:1480-1493(2006).
-!- FUNCTION: Nuclear phosphoprotein which forms a tight but non-
covalently linked complex with the JUN/AP-1 transcription factor.
On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS
complex, at the AP1/SMAD-binding site to regulate TGF-beta-
mediated signaling (By similarity). Has a critical function in
regulating the development of cells destined to form and maintain
the skeleton. It is thought to have an important role in signal
transduction, cell proliferation and differentiation. In growing
cells, activates phospholipid synthesis, possibly by activating
CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and
association with the endoplasmic reticulum (By similarity).
{ECO:0000250, ECO:0000269|PubMed:17223854,
ECO:0000269|PubMed:7816602}.
-!- SUBUNIT: Heterodimer; with JUN (By similarity). Component of the
SMAD3/SMAD4/JUN/FOS complex required for synergistic TGF-beta-
mediated transcription at the AP1 promoter site. Interacts with
SMAD3; the interaction is weak even on TGF-beta activation.
Interacts with DSIPI; this interaction inhibits the binding of
active AP1 to its target DNA (By similarity). Interacts with MAFB.
Interacts with CDS1 and PI4K2A (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm,
cytosol {ECO:0000250}. Note=In quiescent cells, present in very
small amounts in the cytosol. Following induction of cell growth,
first localizes to the endoplasmic reticulum and only later to the
nucleus. Localization at the endoplasmic reticulum requires
dephosphorylation at Tyr-10 and Tyr-30 (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated in the C-terminal upon stimulation by nerve
growth factor (NGF) and epidermal growth factor (EGF) (By
similarity). Phosphorylated, in vitro, by MAPK and RSK1.
Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2
leads to protein stabilization with phosphorylation on Ser-374
being the major site for protein stabilization on NGF stimulation.
Phosphorylation on Ser-362 and Ser-374 primes further
phosphorylations on Thr-325 and Thr-331 through promoting docking
of MAPK to the DEF domain. Phosphorylation on Thr-232, induced by
HA-RAS, activates the transcriptional activity and antagonizes
sumoylation. Phosphorylation on Ser-362 by RSK2 in osteoblasts
contributes to osteoblast transformation. {ECO:0000250,
ECO:0000269|PubMed:17223854, ECO:0000269|PubMed:7816602}.
-!- PTM: Constitutively sumoylated with SUMO1, SUMO2 and SUMO3.
Desumoylated by SENP2. Sumoylation requires heterodimerization
with JUN and is enhanced by mitogen stimulation. Sumoylation
inhibits the AP-1 transcriptional activity and is, itself,
inhibited by Ras-activated phosphorylation on Thr-232 (By
similarity). {ECO:0000250}.
-!- PTM: In quiescent cells, the small amount of FOS present is
phosphorylated at Tyr-10 and Tyr-30 by SRC. This Tyr-
phosphorylated form is cytosolic. In growing cells,
dephosphorylated by PTPN2. Dephosphorylation leads to the
association with endoplasmic reticulum membranes and activation of
phospholipid synthesis (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. Fos subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X06769; CAA29937.1; -; mRNA.
EMBL; DQ089699; AAZ13764.1; -; Genomic_DNA.
PIR; A28263; TVRTFS.
RefSeq; NP_071533.1; NM_022197.2.
UniGene; Rn.103750; -.
ProteinModelPortal; P12841; -.
SMR; P12841; -.
BioGrid; 260681; 1.
CORUM; P12841; -.
DIP; DIP-6001N; -.
IntAct; P12841; 1.
MINT; MINT-220035; -.
STRING; 10116.ENSRNOP00000010712; -.
iPTMnet; P12841; -.
PhosphoSitePlus; P12841; -.
PaxDb; P12841; -.
PRIDE; P12841; -.
Ensembl; ENSRNOT00000010712; ENSRNOP00000010712; ENSRNOG00000008015.
GeneID; 314322; -.
KEGG; rno:314322; -.
UCSC; RGD:2626; rat.
CTD; 2353; -.
RGD; 2626; Fos.
eggNOG; KOG1414; Eukaryota.
eggNOG; ENOG4111CH5; LUCA.
GeneTree; ENSGT00730000110541; -.
HOGENOM; HOG000234334; -.
HOVERGEN; HBG005743; -.
InParanoid; P12841; -.
KO; K04379; -.
OMA; HRPACKM; -.
OrthoDB; EOG091G0GGW; -.
PhylomeDB; P12841; -.
TreeFam; TF326301; -.
Reactome; R-RNO-2559580; Oxidative Stress Induced Senescence.
Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
Reactome; R-RNO-450341; Activation of the AP-1 family of transcription factors.
PRO; PR:P12841; -.
Proteomes; UP000002494; Chromosome 6.
Bgee; ENSRNOG00000008015; -.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
GO; GO:0035976; C:transcription factor AP-1 complex; ISO:RGD.
GO; GO:0005667; C:transcription factor complex; ISO:RGD.
GO; GO:0003682; F:chromatin binding; ISO:RGD.
GO; GO:0003677; F:DNA binding; IDA:RGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0070412; F:R-SMAD binding; ISO:RGD.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:RGD.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:RGD.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:RGD.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IMP:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:RGD.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:RGD.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; ISO:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:RGD.
GO; GO:0071277; P:cellular response to calcium ion; ISO:RGD.
GO; GO:0031668; P:cellular response to extracellular stimulus; ISO:RGD.
GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
GO; GO:0001661; P:conditioned taste aversion; IEP:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0007399; P:nervous system development; ISO:RGD.
GO; GO:1901216; P:positive regulation of neuron death; IGI:ARUK-UCL.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:RGD.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0009409; P:response to cold; IEP:RGD.
GO; GO:0051412; P:response to corticosterone; IEP:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0009629; P:response to gravity; IEP:RGD.
GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
GO; GO:0009416; P:response to light stimulus; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0035994; P:response to muscle stretch; ISO:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0032570; P:response to progesterone; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
GO; GO:0030431; P:sleep; IEP:RGD.
GO; GO:0060395; P:SMAD protein signal transduction; ISO:RGD.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
Gene3D; 1.10.880.10; -; 1.
InterPro; IPR000837; AP-1.
InterPro; IPR004827; bZIP.
InterPro; IPR029816; c-Fos/v-Fos.
InterPro; IPR008917; TF_DNA-bd_sf.
PANTHER; PTHR23351; PTHR23351; 1.
PANTHER; PTHR23351:SF4; PTHR23351:SF4; 1.
Pfam; PF00170; bZIP_1; 1.
PRINTS; PR00042; LEUZIPPRFOS.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; DNA-binding; Endoplasmic reticulum;
Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Ubl conjugation.
CHAIN 1 380 Proto-oncogene c-Fos.
/FTId=PRO_0000076469.
DOMAIN 137 200 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 139 159 Basic motif; required for the activation
of phospholipid synthesis, but not for
CDS1-binding. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 165 193 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 10 10 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P01100}.
MOD_RES 30 30 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P01100}.
MOD_RES 232 232 Phosphothreonine.
{ECO:0000269|PubMed:7816602}.
MOD_RES 325 325 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:17223854}.
MOD_RES 331 331 Phosphothreonine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:17223854}.
MOD_RES 362 362 Phosphoserine; by MAPK1, MAPK3 and
RPS6KA3. {ECO:0000269|PubMed:17223854}.
MOD_RES 374 374 Phosphoserine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:17223854}.
CROSSLNK 113 113 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P01100}.
CROSSLNK 128 128 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P01100}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P01100}.
MUTAGEN 232 232 T->A: Abolishes HA-RAS-mediated
activation. Loss of in vitro ERK2-
mediated phosphorylation. No change in
sumoylation levels.
{ECO:0000269|PubMed:7816602}.
MUTAGEN 325 325 T->A: Loss of NGF-mediated
phosphorylation; when associated with A-
331. {ECO:0000269|PubMed:17223854}.
MUTAGEN 331 331 T->A: Loss of NGF-mediated
phosphorylation; when associated with A-
325. {ECO:0000269|PubMed:17223854}.
MUTAGEN 343 345 FTY->ATA: Decreased phosphorylation
levels. Reduced NGF-mediated enhanced
transactivation.
{ECO:0000269|PubMed:17223854}.
MUTAGEN 362 362 S->A: Some loss of protein stabilization
on NGF-treatment; when associated with D-
374. {ECO:0000269|PubMed:17223854}.
MUTAGEN 362 362 S->D: Increased protein stabilization on
NGF-treatment, but no increase when
treated with MAPK-inhibitor; when
associated with D-374.
{ECO:0000269|PubMed:17223854}.
MUTAGEN 374 374 S->A: Greatly reduced protein
stabilization on NGF stimulation.
{ECO:0000269|PubMed:17223854}.
MUTAGEN 374 374 S->D: Increased protein stabilization on
NGF-treatment, but no increase when
treated with MAPK-inhibitor; when
associated with D-362. Some loss of
protein stablization on NGF-treatment;
wnen associated with A-362.
{ECO:0000269|PubMed:17223854}.
SEQUENCE 380 AA; 40927 MW; E62D16A88CB2BEE9 CRC64;
MMFSGFNADY EASSSRCSSA SPAGDSLSYY HSPADSFSSM GSPVNTQDFC ADLSVSSANF
IPTVTAISTS PDLQWLVQPT LVSSVAPSQT RAPHPYGLPT PSTGAYARAG VVKTMSGGRA
QSIGRRGKVE QLSPEEEEKR RIRRERNKMA AAKCRNRRRE LTDTLQAETD QLEDEKSALQ
TEIANLLKEK EKLEFILAAH RPACKIPNDL GFPEEMSVTS LDLTGGLPEA TTPESEEAFT
LPLLNDPEPK PSLEPVKNIS NMELKAEPFD DFLFPASSRP SGSETARSVP DVDLSGSFYA
ADWEPLHSSS LGMGPMVTEL EPLCTPVVTC TPSCTTYTSS FVFTYPEADS FPSCAAAHRK
GSSSNEPSSD SLSSPTLLAL


Related products :

Catalog number Product name Quantity
U1291r CLIA Cellular oncogene fos,Fos,Proto-oncogene c-Fos,Rat,Rattus norvegicus 96T
U1291m CLIA Cellular oncogene fos,Fos,Mouse,Mus musculus,Proto-oncogene c-Fos 96T
U1291b CLIA Bos taurus,Bovine,Cellular oncogene fos,FOS,Proto-oncogene c-Fos 96T
E1291b ELISA Bos taurus,Bovine,Cellular oncogene fos,FOS,Proto-oncogene c-Fos 96T
E1291r ELISA kit Cellular oncogene fos,Fos,Proto-oncogene c-Fos,Rat,Rattus norvegicus 96T
E1291m ELISA kit Cellular oncogene fos,Fos,Mouse,Mus musculus,Proto-oncogene c-Fos 96T
E1291b ELISA kit Bos taurus,Bovine,Cellular oncogene fos,FOS,Proto-oncogene c-Fos 96T
E1291m ELISA Cellular oncogene fos,Fos,Mouse,Mus musculus,Proto-oncogene c-Fos 96T
E1291r ELISA Cellular oncogene fos,Fos,Proto-oncogene c-Fos,Rat,Rattus norvegicus 96T
PR-771 c-fosHis Proto-oncogene, Cellular oncogene fos, G0 per G1 switch regulatory protein 7 human, recombinant, Baculovirus 5
PR-771 c-fos Proto-oncogene, Cellular oncogene fos, G0_G1 switch regulatory protein 7human, recombinant, Baculovirus 5
E1291p ELISA Cellular oncogene fos,FOS,Pig,Proto-oncogene c-Fos,Sus scrofa 96T
U1291p CLIA Cellular oncogene fos,FOS,Pig,Proto-oncogene c-Fos,Sus scrofa 96T
E1291p ELISA kit Cellular oncogene fos,FOS,Pig,Proto-oncogene c-Fos,Sus scrofa 96T
PR-771 Proteins: c-fosHis Proto-oncogene, Cellular oncogene fos, G0_G1 switch regulatory protein 7human, recombinant, Baculovirus 5
31-234 The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex 0.1 mg
28-798 The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex 0.05 mg
28-797 The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex 0.1 mg
31-233 The c-Jun proto-oncogene was first identified as the cellular homolog of the avian sarcoma virus v-Jun oncogene. The c-Jun protein, along with c-Fos, is a component of the AP-1 transcriptional complex 0.1 mg
EIAAB14724 Feline sarcoma_Fujinami avian sarcoma oncogene homolog,FES,FPS,Homo sapiens,Human,p93c-fes,Proto-oncogene c-Fes,Proto-oncogene c-Fps,Tyrosine-protein kinase Fes_Fps
E1291h ELISA kit Cellular oncogene fos,FOS,G0_G1 switch regulatory protein 7,G0S7,Homo sapiens,Human,Proto-oncogene c-Fos 96T
E1291h ELISA Cellular oncogene fos,FOS,G0_G1 switch regulatory protein 7,G0S7,Homo sapiens,Human,Proto-oncogene c-Fos 96T
U1291h CLIA Cellular oncogene fos,FOS,G0_G1 switch regulatory protein 7,G0S7,Homo sapiens,Human,Proto-oncogene c-Fos 96T
18-003-42997 Proto-oncogene protein c-fos - Cellular oncogene fos; G0_G1 switch regulatory protein 7 Polyclonal 0.1 mg Protein A
15-288-21144 Proto-oncogene protein c-fos - Cellular oncogene fos; G0_G1 switch regulatory protein 7 Polyclonal 0.05 mg


 

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