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

Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2]

 SPIKE_IBVM              Reviewed;        1162 AA.
P12651; Q0GNB8; Q5I5X9;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
23-MAY-2018, entry version 99.
RecName: Full=Spike glycoprotein {ECO:0000255|HAMAP-Rule:MF_04098};
Short=S glycoprotein {ECO:0000255|HAMAP-Rule:MF_04098};
AltName: Full=E2 {ECO:0000255|HAMAP-Rule:MF_04098};
AltName: Full=Peplomer protein {ECO:0000255|HAMAP-Rule:MF_04098};
Contains:
RecName: Full=Spike protein S1 {ECO:0000255|HAMAP-Rule:MF_04098};
Contains:
RecName: Full=Spike protein S2 {ECO:0000255|HAMAP-Rule:MF_04098};
Contains:
RecName: Full=Spike protein S2' {ECO:0000255|HAMAP-Rule:MF_04098};
Flags: Precursor;
Name=S {ECO:0000255|HAMAP-Rule:MF_04098}; ORFNames=2;
Avian infectious bronchitis virus (strain M41) (IBV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Gammacoronavirus.
NCBI_TaxID=11127;
NCBI_TaxID=9031; Gallus gallus (Chicken).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2429473; DOI=10.1016/0168-1702(86)90022-5;
Niesters H.G.M., Lenstra J.A., Spaan W.J.M., Zijderveld A.J.,
Bleumink-Pluym N.M.C., Hong F., van Scharrenburg G.J.M.,
Horzinek M.C., van der Zeijst B.A.M.;
"The peplomer protein sequence of the M41 strain of coronavirus IBV
and its comparison with Beaudette strains.";
Virus Res. 5:253-263(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Mondal S.P., Buckles E.L.;
"Avian infectious bronchitis virus strain M41.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16934878; DOI=10.1016/j.jviromet.2006.07.018;
Callison S.A., Hilt D.A., Boynton T.O., Sample B.F., Robison R.,
Swayne D.E., Jackwood M.W.;
"Development and evaluation of a real-time Taqman RT-PCR assay for the
detection of infectious bronchitis virus from infected chickens.";
J. Virol. Methods 138:60-65(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Madu I.G., Chu V.C., Lee H., Regan A.D., Bauman B.E., Whittaker G.R.;
"Heparan sulfate is a selective attachment factor for the avian
coronavirus IBV Beaudette.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Spike protein S1: attaches the virion to the host cell
membrane by interacting with sialic acids, initiating the
infection. {ECO:0000255|HAMAP-Rule:MF_04098}.
-!- FUNCTION: Spike protein S2: mediates fusion of the virion and
cellular membranes by acting as a class I viral fusion protein.
Under the current model, the protein has at least 3 conformational
states: pre-fusion native state, pre-hairpin intermediate state,
and post-fusion hairpin state. During viral and target cell
membrane fusion, the coiled coil regions (heptad repeats) assume a
trimer-of-hairpins structure, positioning the fusion peptide in
close proximity to the C-terminal region of the ectodomain. The
formation of this structure appears to drive apposition and
subsequent fusion of viral and target cell membranes.
{ECO:0000255|HAMAP-Rule:MF_04098}.
-!- FUNCTION: Spike protein S2': Acts as a viral fusion peptide after
S2 cleavage occurring upon virus endocytosis. {ECO:0000255|HAMAP-
Rule:MF_04098}.
-!- SUBUNIT: Homotrimer; each monomer consists of a S1 and a S2
subunit. The resulting peplomers protrude from the virus surface
as spikes. {ECO:0000255|HAMAP-Rule:MF_04098}.
-!- SUBCELLULAR LOCATION: Spike protein S2: Virion membrane
{ECO:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic
reticulum-Golgi intermediate compartment membrane
{ECO:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04098}. Note=Accumulates in the
endoplasmic reticulum-Golgi intermediate compartment, where it
participates in virus particle assembly. Some S oligomers may be
transported to the plasma membrane, where they may mediate cell-
cell fusion. {ECO:0000255|HAMAP-Rule:MF_04098}.
-!- SUBCELLULAR LOCATION: Spike protein S1: Virion membrane
{ECO:0000255|HAMAP-Rule:MF_04098}; Peripheral membrane protein
{ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic reticulum-
Golgi intermediate compartment membrane {ECO:0000255|HAMAP-
Rule:MF_04098}; Peripheral membrane protein {ECO:0000255|HAMAP-
Rule:MF_04098}. Note=Accumulates in the endoplasmic reticulum-
Golgi intermediate compartment, where it participates in virus
particle assembly. Some S oligomers may be transported to the
plasma membrane, where they may mediate cell-cell fusion. S1 is
not anchored to the viral envelope, but associates with the
extravirion surface through its binding to S2. {ECO:0000255|HAMAP-
Rule:MF_04098}.
-!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
localization for type I membrane proteins. {ECO:0000255|HAMAP-
Rule:MF_04098}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
The precursor is processed into S1 and S2 by host cell furin or
furin-like protease to yield the mature S1 and S2 proteins. The
cleavage site between S1 and S2 requires the optimal sequence
[KR]-X-[KR]-R. Additionally, a second cleavage leads to the
release of a fusion peptide after viral attachment to host cell
receptor. {ECO:0000255|HAMAP-Rule:MF_04098}.
-!- SIMILARITY: Belongs to the gammacoronaviruses spike protein
family. {ECO:0000255|HAMAP-Rule:MF_04098}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M21883; AAA66575.1; -; Genomic_RNA.
EMBL; DQ834384; ABI26423.1; -; Genomic_RNA.
EMBL; AY851295; AAW33786.1; -; Genomic_RNA.
EMBL; DQ830980; ABH01141.1; -; Genomic_DNA.
PIR; S07421; S07421.
ProteinModelPortal; P12651; -.
SMR; P12651; -.
OrthoDB; VOG0900000Z; -.
Proteomes; UP000007642; Genome.
Proteomes; UP000096468; Genome.
GO; GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:InterPro.
Gene3D; 1.20.5.790; -; 1.
HAMAP; MF_04098; GAMMA_CORONA_SPIKE; 1.
InterPro; IPR002551; Corona_S1.
InterPro; IPR002552; Corona_S2.
InterPro; IPR027400; S_HR2.
Pfam; PF01600; Corona_S1; 1.
Pfam; PF01601; Corona_S2; 1.
3: Inferred from homology;
Cleavage on pair of basic residues; Coiled coil; Complete proteome;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host membrane; Host-virus interaction; Membrane; Signal;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral penetration into host cytoplasm; Virion;
Virulence; Virus endocytosis by host; Virus entry into host cell.
SIGNAL 1 18 {ECO:0000255|HAMAP-Rule:MF_04098}.
CHAIN 19 1162 Spike glycoprotein. {ECO:0000255|HAMAP-
Rule:MF_04098}.
/FTId=PRO_0000037171.
CHAIN 19 537 Spike protein S1. {ECO:0000255|HAMAP-
Rule:MF_04098}.
/FTId=PRO_0000037172.
CHAIN 538 1162 Spike protein S2. {ECO:0000255|HAMAP-
Rule:MF_04098}.
/FTId=PRO_0000037173.
CHAIN 691 1162 Spike protein S2'. {ECO:0000255|HAMAP-
Rule:MF_04098}.
/FTId=PRO_0000444095.
TOPO_DOM 19 1095 Extracellular. {ECO:0000255|HAMAP-
Rule:MF_04098}.
TRANSMEM 1096 1116 Helical. {ECO:0000255|HAMAP-
Rule:MF_04098}.
TOPO_DOM 1117 1162 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_04098}.
COILED 822 866 {ECO:0000255|HAMAP-Rule:MF_04098}.
COILED 1055 1083 {ECO:0000255|HAMAP-Rule:MF_04098}.
MOTIF 1159 1162 Di-lysine motif. {ECO:0000255|HAMAP-
Rule:MF_04098}.
COMPBIAS 1120 1137 Cys-rich.
SITE 537 538 Cleavage; by host furin.
{ECO:0000255|HAMAP-Rule:MF_04098}.
SITE 690 691 Cleavage; by host furin.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 77 77 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 163 163 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 247 247 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 425 425 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 447 447 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 530 530 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 579 579 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 591 591 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 669 669 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 676 676 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 714 714 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 947 947 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 960 960 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 979 979 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 1014 1014 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 1038 1038 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 1051 1051 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
CARBOHYD 1074 1074 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04098}.
VARIANT 203 203 K -> E.
VARIANT 291 291 L -> Q.
VARIANT 823 823 D -> H.
VARIANT 829 829 S -> N.
VARIANT 849 849 V -> L.
SEQUENCE 1162 AA; 128078 MW; 3C9CC70938492DDA CRC64;
MLVTPLLLVT LLCVLCSAAL YDSSSYVYYY QSAFRPPNGW HLHGGAYAVV NISSESNNAG
SSPGCIVGTI HGGRVVNASS IAMTAPSSGM AWSSSQFCTA HCNFSDTTVF VTHCYKYDGC
PITGMLQKNF LRVSAMKNGQ LFYNLTVSVA KYPTFKSFQC VNNLTSVYLN GDLVYTSNET
TDVTSAGVYF KAGGPITYKV MRKVKALAYF VNGTAQDVIL CDGSPRGLLA CQYNTGNFSD
GFYPFINSSL VKQKFIVYRE NSVNTTFTLH NFTFHNETGA NPNPSGVQNI LTYQTQTAQS
GYYNFNFSFL SSFVYKESNF MYGSYHPSCN FRLETINNGL WFNSLSVSIA YGPLQGGCKQ
SVFSGRATCC YAYSYGGPSL CKGVYSGELD LNFECGLLVY VTKSGGSRIQ TATEPPVITR
HNYNNITLNT CVDYNIYGRT GQGFITNVTD SAVSYNYLAD AGLAILDTSG SIDIFVVQGE
YGLTYYKVNP CEDVNQQFVV SGGKLVGILT SRNETGSQLL ENQFYIKITN GTRRFRRSIT
ENVANCPYVS YGKFCIKPDG SIATIVPKQL EQFVAPLLNV TENVLIPNSF NLTVTDEYIQ
TRMDKVQINC LQYVCGNSLD CRDLFQQYGP VCDNILSVVN SIGQKEDMEL LNFYSSTKPA
GFNTPFLSNV STGEFNISLL LTTPSSPRRR SFIEDLLFTS VESVGLPTDD AYKNCTAGPL
GFLKDLACAR EYNGLLVLPP IITAEMQTLY TSSLVASMAF GGITAAGAIP FATQLQARIN
HLGITQSLLL KNQEKIAASF NKAIGRMQEG FRSTSLALQQ IQDVVNKQSA ILTETMASLN
KNFGAISSVI QEIYQQLDAI QANAQVDRLI TGRLSSLSVL ASAKQAEHIR VSQQRELATQ
KINECVKSQS IRYSFCGNGR HVLTIPQNAP NGIVFIHFSY TPDSFVNVTA IVGFCVKPAN
ASQYAIVPAN GRGIFIQVNG SYYITARDMY MPRAITAGDI VTLTSCQANY VSVNKTVITT
FVDNDDFDFN DELSKWWNDT KHELPDFDKF NYTVPILDID SEIDRIQGVI QGLNDSLIDL
EKLSILKTYI KWPWYVWLAI AFATIIFILI LGWVFFMTGC CGCCCGCFGI MPLMSKCGKK
SSYYTTFDND VVTEQNRPKK SV


Related products :

Catalog number Product name Quantity
20-663-48070 SARS Spike protein - Mouse Anti SARS Spike protein; S glycoprotein; Peplomer protein; E2 Monoclonal 0.1 mg
20-663-48070 SARS Spike protein - Mouse Anti SARS Spike protein; S glycoprotein; Peplomer protein; E2 Monoclonal 0.2 mg
10-271-82347 SARS-Associated Coronavirus Spike mosaic S(M) - S glycoprotein; Peplomer protein; E2 1 mg
10-271-82346 SARS-Associated Coronavirus Spike mosaic S(C) - S glycoprotein; Peplomer protein; E2 1 mg
orb81530 SARS Associated Spike Mosaic S(M) protein The E.coli derived 38 kDa recombinant mosaic protein contains the middle section of the Spike protein 408-470, 540-573 amino acids immunodominant regions. For 100
orb81529 SARS Associated Spike Mosaic S(N) protein The E.coli derived 38 kDa mosaic protein contains the N-terminal section of the Spike protein 12-53, 90-115, 171-203 amino acids immunodominant regions. For r 100
SCH-OBT1901 RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, Clone 0.1 mg
OBT1901X RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, WB, Clone 1 mg
SCH-OBT1901X RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, WB, Clone 1 mg
OBT1901 RECOMBINANT SARS SPIKE PROTEIN, Product Type Recombinant Protein, Specificity SARS SPIKE PROTEIN, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applications E, Clone 0.1 mg
18-663-49005 SARS Spike Protein - Rabbit Anti SARS Spike Protein Polyclonal 0.1 mg
18-663-49005 SARS Spike Protein - Rabbit Anti SARS Spike Protein Polyclonal 0.2 mg
RANT-157C SARS Spike Polyclonal Rabbit Anti SARS Spike Protein 300µg
RANT-157B SARS Spike Polyclonal Rabbit Anti SARS Spike Protein 200µg
RANT-157A SARS Spike Polyclonal Rabbit Anti SARS Spike Protein 100µg
orb82497 SARS-CoV, Spike (N-term) recombinant protein SARS-Associated Coronavirus (SARS-CoV) Spike protein (N-terminal) Recombinant is an infectious disease antigen_toxin. For research use only. 1 mg
orb82489 SARS-CoV, Spike (C-term) recombinant protein SARS-Associated Coronavirus (SARS-CoV) Spike protein (C-terminal) Recombinant is an infectious disease antigen_toxin. For research use only. 1 mg
OBT1902X RECOMBINANT SARS SPIKE MOSAIC S(M) (aa408_470 540_573), Product Type Recombinant Protein, Specificity SARS SPIKE MOSAIC, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicati 1 mg
SCH-OBT1902X RECOMBINANT SARS SPIKE MOSAIC S(M) (aa408_470 540_573), Product Type Recombinant Protein, Specificity SARS SPIKE MOSAIC, Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicati 1 mg
SCH-OBT1903X RECOMBINANT SARS SPIKE MOSAIC S(C) (aa1051_1076 1121_1154 1162_1190), Product Type Recombinant Protein, Specificity SARS SPIKE MOSAIC, Target Species Viral, Host N_A, Format Rec. Protein, Isotype 1 mg
OBT1903X RECOMBINANT SARS SPIKE MOSAIC S(C) (aa1051_1076 1121_1154 1162_1190), Product Type Recombinant Protein, Specificity SARS SPIKE MOSAIC, Target Species Viral, Host N_A, Format Rec. Protein, Isotype 1 mg
ant-157 Polyclonal Rabbit Anti SARS Spike Protein SARS Spike 100
ant-157 Polyclonal Rabbit Anti SARS Spike Protein SARS Spike 200
ant-157 Polyclonal Rabbit Anti SARS Spike Protein SARS Spike 300
SCH-AHP889 RABBIT ANTI SARS SPIKE PROTEIN (N_TERMINAL), Product Type Polyclonal Antibody, Specificity SARS SPIKE PROTEIN , Target Species Viral, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Appli 0.1 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