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

Receptor-interacting serine/threonine-protein kinase 3 (EC 2.7.11.1) (Homocysteine respondent protein HCYP2) (RIP-like protein kinase 3) (Receptor-interacting protein 3) (RIP-3)

 RIPK3_RAT               Reviewed;         478 AA.
Q9Z2P5; B0BMV6;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
19-FEB-2014, sequence version 3.
25-APR-2018, entry version 136.
RecName: Full=Receptor-interacting serine/threonine-protein kinase 3;
EC=2.7.11.1;
AltName: Full=Homocysteine respondent protein HCYP2;
AltName: Full=RIP-like protein kinase 3;
AltName: Full=Receptor-interacting protein 3;
Short=RIP-3;
Name=Ripk3; Synonyms=Rip3;
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=Wistar Kyoto;
Chen K.H., Tang J.;
"A homocysteine-respondent gene cloned from WKY VSMCs by differential
display.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
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]
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).
-!- FUNCTION: Essential for necroptosis, a programmed cell death
process in response to death-inducing TNF-alpha family members.
Upon induction of necrosis, RIPK3 interacts with, and
phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex.
RIPK3 binds to and enhances the activity of three metabolic
enzymes: GLUL, GLUD1, and PYGL. These metabolic enzymes may
eventually stimulate the tricarboxylic acid cycle and oxidative
phosphorylation, which could result in enhanced ROS production (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts (via RIP homotypic interaction motif) with
RIPK1 (via RIP homotypic interaction motif); this interaction
induces RIPK1 phosphorylation and formation of a RIPK1-RIPK3
necroptosis-inducing complex. Upon TNF-induced necrosis, the
RIPK1-RIPK3 dimer further interacts with PGAM5 and MLKL; the
formation of this complex leads to PGAM5 phosphorylation and
increase in PGAM5 phosphatase activity (By similarity). Interacts
with MLKL; the interaction is direct. Binds TRAF2 and is recruited
to the TNFR-1 signaling complex. Interacts with PYGL, GLUL and
GLUD1; these interactions result in activation of these metabolic
enzymes (By similarity). Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2
and XIAP/BIRC4. Interacts with ARHGEF2 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell
membrane {ECO:0000250}. Mitochondrion {ECO:0000305}.
-!- PTM: RIPK1 and RIPK3 undergo reciprocal auto- and trans-
phosphorylation. Phosphorylation of Ser-201 plays a role in the
necroptotic function of RIPK3 (By similarity). {ECO:0000250}.
-!- PTM: Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by
BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-
B. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF036537; AAD02059.2; -; mRNA.
EMBL; AABR06083269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH474049; EDM14285.1; -; Genomic_DNA.
EMBL; CH474049; EDM14286.1; -; Genomic_DNA.
EMBL; BC158580; AAI58581.1; -; mRNA.
RefSeq; NP_647558.1; NM_139342.1.
UniGene; Rn.7110; -.
ProteinModelPortal; Q9Z2P5; -.
SMR; Q9Z2P5; -.
IntAct; Q9Z2P5; 1.
MINT; Q9Z2P5; -.
STRING; 10116.ENSRNOP00000027759; -.
iPTMnet; Q9Z2P5; -.
PhosphoSitePlus; Q9Z2P5; -.
PaxDb; Q9Z2P5; -.
PRIDE; Q9Z2P5; -.
Ensembl; ENSRNOT00000027759; ENSRNOP00000027759; ENSRNOG00000020465.
GeneID; 246240; -.
KEGG; rno:246240; -.
UCSC; RGD:628899; rat.
CTD; 11035; -.
RGD; 628899; Ripk3.
eggNOG; KOG0192; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00550000074536; -.
HOGENOM; HOG000035101; -.
HOVERGEN; HBG062538; -.
InParanoid; Q9Z2P5; -.
KO; K08847; -.
OMA; KWGYDVA; -.
OrthoDB; EOG091G0DXD; -.
Reactome; R-RNO-3295583; TRP channels.
Reactome; R-RNO-5213460; RIPK1-mediated regulated necrosis.
PRO; PR:Q9Z2P5; -.
Proteomes; UP000002494; Chromosome 15.
Bgee; ENSRNOG00000020465; -.
Genevisible; Q9Z2P5; RN.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; ISO:RGD.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0004704; F:NF-kappaB-inducing kinase activity; ISO:RGD.
GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
GO; GO:1990000; P:amyloid fibril formation; ISS:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0048535; P:lymph node development; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0070266; P:necroptotic process; ISS:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:0051351; P:positive regulation of ligase activity; ISO:RGD.
GO; GO:0060545; P:positive regulation of necroptotic process; ISO:RGD.
GO; GO:0010940; P:positive regulation of necrotic cell death; ISO:RGD.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISO:RGD.
GO; GO:0010922; P:positive regulation of phosphatase activity; ISO:RGD.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:RGD.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
GO; GO:0046006; P:regulation of activated T cell proliferation; ISS:UniProtKB.
GO; GO:0070235; P:regulation of activation-induced cell death of T cells; ISS:UniProtKB.
GO; GO:0002819; P:regulation of adaptive immune response; ISS:UniProtKB.
GO; GO:2000452; P:regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation; ISS:UniProtKB.
GO; GO:0032649; P:regulation of interferon-gamma production; ISS:UniProtKB.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
GO; GO:0001914; P:regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
GO; GO:0048536; P:spleen development; ISS:UniProtKB.
GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
GO; GO:0043029; P:T cell homeostasis; ISS:UniProtKB.
GO; GO:0048538; P:thymus development; ISS:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR025735; RHIM_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF12721; RHIM; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Kinase;
Membrane; Methylation; Mitochondrion; Necrosis; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase; Ubl conjugation.
CHAIN 1 478 Receptor-interacting serine/threonine-
protein kinase 3.
/FTId=PRO_0000086612.
DOMAIN 22 290 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 28 36 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 437 461 RIP homotypic interaction motif (RHIM).
ACT_SITE 143 143 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 51 51 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZL0}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZL0}.
MOD_RES 201 201 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q9Y572}.
MOD_RES 228 228 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZL0}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y572}.
MOD_RES 254 254 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZL0}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZL0}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZL0}.
MOD_RES 335 335 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZL0}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZL0}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZL0}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZL0}.
MOD_RES 392 392 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZL0}.
MOD_RES 474 474 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9QZL0}.
CONFLICT 153 153 P -> L (in Ref. 1; AAD02059).
{ECO:0000305}.
SEQUENCE 478 AA; 52218 MW; 87C83BFD16287136 CRC64;
MSSVKLWLNG ASSISLVGSE ELENLGFVGK GGFGAVFRAR HTAWNLDVAV KIVNSKKISR
EVKAMVNLRH ENVLLLLGVT ENLEWDYVYG PALVTGFMEN GSLSGLLQPS CPRPWPLLCR
LLEEVVLGMC YLHSLNPSLL HRDLKPSNVL LDPELHAKLA DFGLSTFQGG SQSGSGSGSR
DSGGTLAYLA PELLDNDGKA SKASDVYSFG VLVWTVLAGR EAEVVDKTSL IRGAVCNRQR
RPPLTELPPD SPETPGLEGL KELMTHCWSS EPKDRPSFQD CESKTNNVYI LVQDKVDAAV
SKVKHYLSQY RSSDTKLSAR ESSQKGTEVD CPRETIVYEM LDRLHLEEPS GSVPERLTSL
TERRGKEASF GHATPAGTSS DTLAGTPQIP HTLPSRGTTP RPAFTETPGP DPQRNQGDGR
NSNPWYTWNA PNPMTGLQSI VLNNCSEVQI GQHNCMSVQP RTAFPKKEPA QFGRGRGW


Related products :

Catalog number Product name Quantity
EIAAB34871 Homocysteine respondent protein HCYP2,Rat,Rattus norvegicus,Receptor-interacting protein 3,Receptor-interacting serine_threonine-protein kinase 3,Rip3,RIP-3,Ripk3,RIP-like protein kinase 3
18-661-15094 Receptor-interacting serine-threonine kinase 3 - Receptor interacting protein 3 Polyclonal 0.1 mg
EIAAB40405 Homo sapiens,Human,MAP activator with WD repeats,MAWD,Serine-threonine kinase receptor-associated protein,STRAP,UNR-interacting protein,UNRIP,WD-40 repeat protein PT-WD
EIAAB40407 Mouse,Mus musculus,Serine-threonine kinase receptor-associated protein,Strap,UNR-interacting protein,Unrip
EIAAB40408 Rat,Rattus norvegicus,Serine-threonine kinase receptor-associated protein,Strap,UNR-interacting protein,Unrip
10-782-55111 Receptor-interacting serine_threonine-protein kinase 2 - EC 2.7.11.1; RIP-like-interacting CLARP kinase; Receptor-interacting protein 2; RIP-2; CARD-containing interleukin-1 beta-converting enzyme-ass 0.02 mg
18-661-15046 Receptor-interacting serine_threonine-protein kinase 2 - EC 2.7.11.1; RIP-like-interacting CLARP kinase; Receptor-interacting protein 2; RIP-2; CARD-containing interleukin-1 beta-converting enzyme-ass 0.1 mg
10-782-55111 Receptor-interacting serine_threonine-protein kinase 2 - EC 2.7.11.1; RIP-like-interacting CLARP kinase; Receptor-interacting protein 2; RIP-2; CARD-containing interleukin-1 beta-converting enzyme-ass 0.01 mg
10-782-55111 Receptor-interacting serine_threonine-protein kinase 2 - EC 2.7.11.1; RIP-like-interacting CLARP kinase; Receptor-interacting protein 2; RIP-2; CARD-containing interleukin-1 beta-converting enzyme-ass 0.001 mg
10-782-55111 Receptor-interacting serine_threonine-protein kinase 2 - EC 2.7.11.1; RIP-like-interacting CLARP kinase; Receptor-interacting protein 2; RIP-2; CARD-containing interleukin-1 beta-converting enzyme-ass 0.005 mg
ER446 Receptor-interacting serine per threonine-protein kinase 3 Elisa Kit 96T
G6868 Receptor-interacting serine threonine-protein kinase 3 (RIPK3), Rat, ELISA Kit 96T
EIAAB34870 Mouse,mRIP3,Mus musculus,Receptor-interacting protein 3,Receptor-interacting serine_threonine-protein kinase 3,Rip3,RIP-3,Ripk3,RIP-like protein kinase 3
EIAAB34869 Homo sapiens,Human,Receptor-interacting protein 3,Receptor-interacting serine_threonine-protein kinase 3,RIP3,RIP-3,RIPK3,RIP-like protein kinase 3
EIAAB34868 Cell death protein RIP,Homo sapiens,Human,Receptor-interacting protein 1,Receptor-interacting serine_threonine-protein kinase 1,RIP,RIP1,RIP-1,RIPK1,Serine_threonine-protein kinase RIP
G6867 Receptor-interacting serine threonine-protein kinase 3 (RIPK3), Mouse, ELISA Kit 96T
CSB-EL019737HU Human Receptor-interacting serine per threonine-protein kinase 3(RIPK3) ELISA kit 96T
CSB-EL019737MO Mouse Receptor-interacting serine per threonine-protein kinase 3(RIPK3) ELISA kit 96T
CSB-EL019735MO Mouse Receptor-interacting serine per threonine-protein kinase 1(RIPK1) ELISA kit 96T
G6864 Receptor-interacting serine threonine-protein kinase 2 (RIPK2), Bovine, ELISA Kit 96T
G6862 Receptor-interacting serine threonine-protein kinase 1 (RIPK1), Human, ELISA Kit 96T
G6865 Receptor-interacting serine threonine-protein kinase 2 (RIPK2), Mouse, ELISA Kit 96T
G6870 Receptor-interacting serine threonine-protein kinase 4 (RIPK4), Mouse, ELISA Kit 96T
G6866 Receptor-interacting serine threonine-protein kinase 3 (RIPK3), Human, ELISA Kit 96T
G6869 Receptor-interacting serine threonine-protein kinase 4 (RIPK4), Human, ELISA Kit 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