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

Potassium voltage-gated channel subfamily KQT member 1 (IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1) (KQT-like 1) (Voltage-gated potassium channel subunit Kv7.1)

 KCNQ1_RABIT             Reviewed;         661 AA.
Q9MYS6; G1SLX4;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
20-JAN-2016, sequence version 3.
31-JAN-2018, entry version 111.
RecName: Full=Potassium voltage-gated channel subfamily KQT member 1;
AltName: Full=IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 {ECO:0000250|UniProtKB:P51787};
AltName: Full=KQT-like 1 {ECO:0000250|UniProtKB:P51787};
AltName: Full=Voltage-gated potassium channel subunit Kv7.1 {ECO:0000250|UniProtKB:P51787};
Name=KCNQ1 {ECO:0000250|UniProtKB:P51787};
Synonyms=KVLQT1 {ECO:0000250|UniProtKB:P51787};
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Thorbecke;
PubMed=21993624; DOI=10.1038/nature10530;
Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
Pedersen J.S., Lander E.S., Kellis M.;
"A high-resolution map of human evolutionary constraint using 29
mammals.";
Nature 478:476-482(2011).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 151-304.
STRAIN=New Zealand white; TISSUE=Heart;
Sayeed R.A., Grace A.A., Vandenberg J.I.;
"Patterns of ion channel expression in cardiac hypertrophy.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Potassium channel that plays an important role in a
number of tissues, including heart, inner ear, stomach and colon
(By similarity). Associates with KCNE beta subunits that modulates
current kinetics (By similarity). Induces a voltage-dependent by
rapidly activating and slowly deactivating potassium-selective
outward current (By similarity). Promotes also a delayed voltage
activated potassium current showing outward rectification
characteristic (By similarity). During beta-adrenergic receptor
stimulation participates in cardiac repolarization by associating
with KCNE1 to form the I(Ks) cardiac potassium current that
increases the amplitude and slows down the activation kinetics of
outward potassium current I(Ks) (By similarity). Muscarinic
agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By
similarity). When associated with KCNE3, forms the potassium
channel that is important for cyclic AMP-stimulated intestinal
secretion of chloride ions (By similarity). This interaction with
KCNE3 is reduced by 17beta-estradiol, resulting in the reduction
of currents (By similarity). During conditions of increased
substrate load, maintains the driving force for proximal tubular
and intestinal sodium ions absorption, gastric acid secretion, and
cAMP-induced jejunal chloride ions secretion (By similarity).
Allows the provision of potassium ions to the luminal membrane of
the secretory canaliculus in the resting state as well as during
stimulated acid secretion (By similarity). When associated with
KCNE2, forms a heterooligomer complex leading to currents with an
apparently instantaneous activation, a rapid deactivation process
and a linear current-voltage relationship and decreases the
amplitude of the outward current (By similarity). When associated
with KCNE4, inhibits voltage-gated potassium channel activity (By
similarity). When associated with KCNE5, this complex only
conducts current upon strong and continued depolarization (By
similarity). Also forms a heterotetramer with KCNQ5 that has a
voltage-gated potassium channel activity (By similarity). Binds
with phosphatidylinositol 4,5-bisphosphate (By similarity).
{ECO:0000250|UniProtKB:P51787, ECO:0000250|UniProtKB:P97414,
ECO:0000250|UniProtKB:Q9Z0N7}.
-!- SUBUNIT: Tetramer. Heterotetramer with KCNE1; targets to the
membrane raft. Interacts (via C-terminus) with CALM; forms an
heterotetramer in a calcium-independent manner. Interacts with
AKAP9; targets protein kinase A (PKA) catalytic and regulatory
subunits and protein phosphatase 1 (PP1) to the KCNQ1-KCNE1
complex, allowing PKA-mediated phosphorylation and increase of
delayed rectifier potassium channel activity. Interacts with
KCNE2; form a heterooligomer complex that targets to the membrane
raft and leading to currents with an apparently instantaneous
activation, a rapid deactivation process and a linear current-
voltage relationship and decreases the amplitude of the outward
current. Interacts with AP2M1; mediates estrogen-induced
internalization via clathrin-coated vesicles. Interacts with
NEDD4L; promotes internalization and decreases I(Ks) currents.
Interacts with USP2; counteracts the NEDD4L-specific down-
regulation of I(Ks) and restore plasma membrane localization.
Heterotetramer with KCNQ5; has a voltage-gated potassium channel
activity. Interacts with KCNE3; alters membrane raft localization.
Interacts with KCNE4; impairs KCNQ1 localization in lipid rafts
and inhibits voltage-gated potassium channel activity. Interacts
with KCNE5; impairs KCNQ1 localization in lipid rafts and only
conducts current upon strong and continued depolarization.
{ECO:0000250|UniProtKB:P51787}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P51787}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P51787}. Cytoplasmic vesicle membrane
{ECO:0000250|UniProtKB:P51787}. Early endosome
{ECO:0000250|UniProtKB:P51787}. Membrane raft
{ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P51787}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P51787}. Note=Colocalized with KCNE3 at the
plasma membrane. Upon 17beta-oestradiol treatment, colocalizes
with RAB5A at early endosome. Heterotetramer with KCNQ5 is highly
retained at the endoplasmic reticulum and is localized outside of
lipid raft microdomains. During the early stages of epithelial
cell polarization induced by the calcium switch it removed from
plasma membrane to the endoplasmic reticulum where it retained and
it is redistributed to the basolateral cell surface in a PI3K-
dependent manner at a later stage. {ECO:0000250|UniProtKB:P51787}.
-!- DOMAIN: The segment S4 is probably the voltage-sensor and is
characterized by a series of positively charged amino acids at
every third position. {ECO:0000250|UniProtKB:P51787}.
-!- DOMAIN: The coiled-coil domain mediates tetramerization.
{ECO:0000250|UniProtKB:P51787}.
-!- DOMAIN: The segment S6 is involved in the inhibition of voltage-
gated potassium channel activity by KCNE4.
{ECO:0000250|UniProtKB:P51787}.
-!- DOMAIN: The C-terminal assembly domain promotes self-interactiona;
allows functional channel. {ECO:0000250|UniProtKB:P51787}.
-!- PTM: Phosphorylation at Ser-27 by PKA; increases delayed rectifier
potassium channel activity of the KCNQ1-KCNE1 complex through a
macromolecular complex that includes PKA, PP1, and the targeting
protein AKAP9. {ECO:0000250|UniProtKB:P51787}.
-!- PTM: Ubiquitinated by NEDD4L; promotes internalization. The
ubiquitinylated form is internalized through a clathrin-mediated
endocytosis by interacting with AP2M1 and is recycled back to the
cell membrane via RAB4A and RAB11A.
{ECO:0000250|UniProtKB:P51787}.
-!- PTM: Deubiquitinated by USP2; counteracts the NEDD4L-specific
down-regulation of I(Ks) and restores the membrane localization.
{ECO:0000250|UniProtKB:P51787}.
-!- SIMILARITY: Belongs to the potassium channel family. KQT (TC
1.A.1.15) subfamily. Kv7.1/KCNQ1 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB94848.1; Type=Frameshift; Positions=282; Evidence={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; AAGW02076516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAGW02076533; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AJ291316; CAB94848.1; ALT_FRAME; mRNA.
UniGene; Ocu.2456; -.
STRING; 9986.ENSOCUP00000003879; -.
PRIDE; Q9MYS6; -.
eggNOG; KOG1419; Eukaryota.
eggNOG; COG1226; LUCA.
HOGENOM; HOG000220839; -.
InParanoid; Q9MYS6; -.
OrthoDB; EOG091G02ZT; -.
TreeFam; TF315186; -.
Proteomes; UP000001811; Unplaced.
Bgee; ENSOCUG00000004492; -.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0034702; C:ion channel complex; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0015271; F:outward rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
GO; GO:0050892; P:intestinal absorption; ISS:UniProtKB.
GO; GO:0086009; P:membrane repolarization; ISS:UniProtKB.
GO; GO:0060453; P:regulation of gastric acid secretion; ISS:UniProtKB.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0070293; P:renal absorption; ISS:UniProtKB.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
InterPro; IPR005827; K_chnl_volt-dep_KCQN1.
InterPro; IPR028325; VG_K_chnl.
PANTHER; PTHR11537; PTHR11537; 1.
PANTHER; PTHR11537:SF109; PTHR11537:SF109; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF03520; KCNQ_channel; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01460; KCNQ1CHANNEL.
PRINTS; PR01459; KCNQCHANNEL.
2: Evidence at transcript level;
Calmodulin-binding; Cell membrane; Coiled coil; Complete proteome;
Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Glycoprotein;
Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
Potassium channel; Potassium transport; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
Voltage-gated channel.
CHAIN 1 661 Potassium voltage-gated channel subfamily
KQT member 1.
/FTId=PRO_0000054026.
TOPO_DOM 1 120 Cytoplasmic. {ECO:0000255}.
TRANSMEM 121 141 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 142 146 Extracellular. {ECO:0000255}.
TRANSMEM 147 167 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 168 195 Cytoplasmic. {ECO:0000255}.
TRANSMEM 196 216 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 217 224 Extracellular. {ECO:0000255}.
TRANSMEM 225 247 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 248 260 Cytoplasmic. {ECO:0000255}.
TRANSMEM 261 281 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 282 298 Extracellular. {ECO:0000255}.
INTRAMEM 299 319 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 320 326 Extracellular. {ECO:0000255}.
TRANSMEM 327 347 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 348 661 Cytoplasmic. {ECO:0000255}.
REGION 534 571 Interaction with KCNE1 C-terminus.
{ECO:0000250|UniProtKB:P51787}.
REGION 587 615 Interaction with AKAP9.
{ECO:0000250|UniProtKB:P51787}.
REGION 588 619 C-terminal assembly domain.
{ECO:0000250|UniProtKB:P51787}.
COILED 584 620 {ECO:0000250|UniProtKB:P51787}.
MOTIF 311 316 Selectivity filter. {ECO:0000250}.
MOD_RES 27 27 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P51787}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000250|UniProtKB:P97414}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000250|UniProtKB:P97414}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 661 AA; 73636 MW; E90BB42E0D3328DB CRC64;
MAAASTPPRA ERKRXSWSRL PGAQRESAGL AKKCPFSLEL AESGPPSSAL YAPVSPPSAP
EPAPPASPAS PAPPAADQGP QPPVSLDPRV SIYSVRRPLL ARTHIQGRVY NFLERPTGWK
CFAYHFTVFL IVLVCLIFSV LSTIEQYATL ATGTLFWMEI VLVVFFGTEY VVRLWSAGCR
SKYVGLWGRL RFARKPISII DLIVVVASMV VLCVGSKGQV FATSAIRGIR FLQILRMLHV
DRQGGTWRLL GSVVFIHRQE LITTLYIGFL GLIFSSYFVY LAEKDAVNES GRVEFGSYAD
ALWWGVVTVT TIGYGDKVPQ TWVGKTIASC FSVFAISFFA LPAGILGSGF ALKVQQKQRQ
KHFNRQIPAA ASLIQTAWRC YAAENPDSAT WKIYIRKPTR GHALLSPSPK PKKSAMVKKK
KFKLDKDNGV SPGEKTLPVP QITCEPPEER RPDHFPVDSH DGSVRKSPAL LEVSTPQFLR
TNSFAEDLDL EGETLLAPIT HVSQLREHHR ATVKVIRRMQ YFVAKKKFQQ ARKPYDVRDV
IEQYSQGHLN LMVRIKELQR RLDQSIGKPS LFVPISEKSK DRGSNSIGAR LNRVEDKVTQ
LDQRLVLIAD MLQQLLALHQ GRCHGGAHPA QARDGDPADP ELFLPTYEQL TVPRRDPEEG
S


Related products :

Catalog number Product name Quantity
18-003-42663 Potassium voltage-gated channel subfamily KQT member 2 - Voltage-gated potassium channel subunit Kv7.2; Neuroblastoma-specific potassium channel subunit alpha KvLQT2; KQT-like 2 Polyclonal 0.05 mg Aff Pur
18-003-42664 Potassium voltage-gated channel subfamily KQT member 2 - Voltage-gated potassium channel subunit Kv7.2; Neuroblastoma-specific potassium channel subunit alpha KvLQT2; KQT-like 2 Polyclonal 0.1 mg Protein A
28-297 This gene encodes a member of the potassium channel, voltage-gated, subfamily H. This member is a pore-forming (alpha) subunit of a voltage-gated non-inactivating delayed rectifier potassium channel. 0.1 mg
18-662-20074 Potassium voltage-gated channel subfamily C member 1 - Voltage-gated potassium channel subunit Kv3.1; Kv4; NGK2; RAW2 Polyclonal 0.1 ml
18-662-20009 Potassium voltage-gated channel subfamily B member 2 - Voltage-gated potassium channel subunit Kv2.2; CDRK Polyclonal 0.1 ml
18-003-42629 Potassium voltage-gated channel subfamily D member 3 - Voltage-gated potassium channel subunit Kv4.3 Polyclonal 0.1 mg Protein A
18-003-43133 Potassium voltage-gated channel subfamily G member 1 - Voltage-gated potassium channel subunit Kv6.1; kH2 Polyclonal 0.05 mg Aff Pur
18-003-42631 Cyclic GMP gated potassium channel - Potassium voltage-gated channel. shaker-related subfamily. member 10 Polyclonal 0.1 mg Protein A
EIAAB26323 Four domain-type voltage-gated ion channel alpha-1 subunit,Nalcn,Nca,Rat,Rattus norvegicus,Sodium leak channel non-selective protein,Vgcnl1,Voltage gated channel-like protein 1
EIAAB05033 CACNA1H,Homo sapiens,Human,Low-voltage-activated calcium channel alpha1 3.2 subunit,Voltage-dependent T-type calcium channel subunit alpha-1H,Voltage-gated calcium channel subunit alpha Cav3.2
18-003-42670 Kv channel-interacting protein 2 - KChIP2; A-type potassium channel modulatory protein 2; Potassium channel-interacting protein 2; Cardiac voltage-gated potassium channel modulatory subunit Polyclonal 0.05 mg Aff Pur
18-003-42669 Kv channel-interacting protein 2 - KChIP2; A-type potassium channel modulatory protein 2; Potassium channel-interacting protein 2; Cardiac voltage-gated potassium channel modulatory subunit Polyclonal 0.05 mg Aff Pur
KCNH4_RAT Rat ELISA Kit FOR Potassium voltage-gated channel subfamily H member 4 96T
EH2214 Potassium voltage-gated channel subfamily B member 2 Elisa Kit 96T
KCNQ1_PIG Pig ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 1 96T
E1366h Rat ELISA Kit FOR Potassium voltage-gated channel subfamily H member 1 96T
KCNH2_RAT Rat ELISA Kit FOR Potassium voltage-gated channel subfamily H member 2 96T
KCNG3_RAT Rat ELISA Kit FOR Potassium voltage-gated channel subfamily G member 3 96T
WDR64_MOUSE Rat ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 2 96T
E0614m Rat ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 2 96T
E13768r Rat ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 4 96T
KCNA5_RAT Rat ELISA Kit FOR Potassium voltage-gated channel subfamily A member 5 96T
PPAC_MOUSE Rat ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 1 96T
E0522m Rat ELISA Kit FOR Potassium voltage-gated channel subfamily KQT member 1 96T
E15045p Pig ELISA Kit FOR Potassium voltage-gated channel subfamily H member 2 96T


 

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