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

Coatomer subunit beta (Beta-coat protein) (Beta-COP)

 COPB_DROME              Reviewed;         964 AA.
P45437; Q9VWV7; Q9Y116;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
20-JUN-2003, sequence version 2.
12-SEP-2018, entry version 143.
RecName: Full=Coatomer subunit beta;
AltName: Full=Beta-coat protein;
Short=Beta-COP;
Name=betaCOP {ECO:0000312|FlyBase:FBgn0008635};
ORFNames=CG6223 {ECO:0000312|FlyBase:FBgn0008635};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
TISSUE=Embryo;
PubMed=8127899; DOI=10.1073/pnas.91.5.1878;
Ripoche J., Link B., Yucel J.K., Tokuyasu K., Malhotra V.;
"Location of Golgi membranes with reference to dividing nuclei in
syncytial Drosophila embryos.";
Proc. Natl. Acad. Sci. U.S.A. 91:1878-1882(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
SUBCELLULAR LOCATION.
PubMed=10953008; DOI=10.1083/jcb.150.4.849;
Lecuit T., Wieschaus E.;
"Polarized insertion of new membrane from a cytoplasmic reservoir
during cleavage of the Drosophila embryo.";
J. Cell Biol. 150:849-860(2000).
[6]
SUBCELLULAR LOCATION.
PubMed=11533661; DOI=10.1038/ncb0901-816;
Goto S., Taniguchi M., Muraoka M., Toyoda H., Sado Y., Kawakita M.,
Hayashi S.;
"UDP-sugar transporter implicated in glycosylation and processing of
Notch.";
Nat. Cell Biol. 3:816-822(2001).
[7]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=16169286; DOI=10.1016/j.modgep.2005.06.001;
Grieder N.C., Kloter U., Gehring W.J.;
"Expression of COPI components during development of Drosophila
melanogaster.";
Gene Expr. Patterns 6:11-21(2005).
[8]
FUNCTION.
PubMed=16452979; DOI=10.1038/nature04377;
Bard F., Casano L., Mallabiabarrena A., Wallace E., Saito K.,
Kitayama H., Guizzunti G., Hu Y., Wendler F., Dasgupta R.,
Perrimon N., Malhotra V.;
"Functional genomics reveals genes involved in protein secretion and
Golgi organization.";
Nature 439:604-607(2006).
[9]
FUNCTION.
PubMed=19067489; DOI=10.1371/journal.pbio.0060292;
Beller M., Sztalryd C., Southall N., Bell M., Jackle H., Auld D.S.,
Oliver B.;
"COPI complex is a regulator of lipid homeostasis.";
PLoS Biol. 6:E292-E292(2008).
-!- FUNCTION: The coatomer is a cytosolic protein complex that binds
to dilysine motifs and reversibly associates with Golgi non-
clathrin-coated vesicles, which further mediate biosynthetic
protein transport from the ER, via the Golgi up to the trans Golgi
network. Coatomer complex is required for budding from Golgi
membranes, and is essential for the retrograde Golgi-to-ER
transport of dilysine-tagged proteins. Required for limiting lipid
storage in lipid droplets. {ECO:0000269|PubMed:16452979,
ECO:0000269|PubMed:19067489}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
Peripheral membrane protein; Cytoplasmic side. Cytoplasmic
vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
side of the Golgi, as well as on the vesicles/buds originating
from it (By similarity). Present within the clusters of tubulo-
vesicular structures of Golgi membrane and cis-Golgi membranes.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: During oogenesis and spermatogenesis,
expressed in ovariole, germarium, testis tip and testis.
{ECO:0000269|PubMed:16169286}.
-!- DEVELOPMENTAL STAGE: Before the first zygotic nuclear division,
seen in membrane structures confined in the embryonic cortex. This
cortical distribution is maintained through stage 6. In cycles 10
and 11, the presence in the Golgi membranes between hexagonally
arranged nuclei is readily observed in tangential optical sections
through the embryonic surface. In stage 14, present in a thin
vitelloplasmic layer below the plane that represents the basal
borders of the cells separating the cellularized cortex from the
rest of the embryo, and also within cells. Within the cells,
appear to be more abundant in the cytoplasmic region between the
nucleus and the embryonic surface. In early embryos, a large
proportion appears randomly diffused, but in the later stages of
embryogenesis, a larger proportion is associated with the
membranes. In early embryos, expressed in the ovary. During
embryogenesis, up-regulated in regions 2 and 3 of the germarium in
meiotic cysts and in follicle cells. Expressed in testis tip
starting in early meiotic spermatocytes. Also detected in
paragonia. During embryogenesis, appears to be expressed
ubiquitously at low levels and markedly up-regulated in the cells
of the presumptive proventriculus and the salivary glands starting
at stage 10. {ECO:0000269|PubMed:16169286,
ECO:0000269|PubMed:8127899}.
-!- MISCELLANEOUS: Brefeldin A induces dissociation from the Golgi of
betaCOP and presumably the other coatomer subunits. {ECO:0000250}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L31852; AAA21090.1; -; mRNA.
EMBL; AE014298; AAF48830.2; -; Genomic_DNA.
EMBL; AF145656; AAD38631.1; -; mRNA.
RefSeq; NP_523400.1; NM_078676.4.
UniGene; Dm.2883; -.
ProteinModelPortal; P45437; -.
BioGrid; 59137; 35.
DIP; DIP-23112N; -.
IntAct; P45437; 7.
STRING; 7227.FBpp0074348; -.
PaxDb; P45437; -.
PRIDE; P45437; -.
EnsemblMetazoa; FBtr0074576; FBpp0074348; FBgn0008635.
GeneID; 32820; -.
KEGG; dme:Dmel_CG6223; -.
CTD; 32820; -.
FlyBase; FBgn0008635; betaCOP.
eggNOG; KOG1058; Eukaryota.
eggNOG; COG5096; LUCA.
GeneTree; ENSGT00390000005270; -.
InParanoid; P45437; -.
KO; K17301; -.
OMA; QCGFMAA; -.
OrthoDB; EOG091G03TX; -.
PhylomeDB; P45437; -.
Reactome; R-DME-6798695; Neutrophil degranulation.
Reactome; R-DME-6807878; COPI-mediated anterograde transport.
Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
ChiTaRS; betaCOP; fly.
GenomeRNAi; 32820; -.
PRO; PR:P45437; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0008635; Expressed in 41 organ(s), highest expression level in embryo.
Genevisible; P45437; DM.
GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
GO; GO:0010883; P:regulation of lipid storage; IDA:FlyBase.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IBA:GO_Central.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR011710; Coatomer_bsu_C.
InterPro; IPR016460; COPB1.
InterPro; IPR029446; COPB1_appendage_platform_dom.
PANTHER; PTHR10635; PTHR10635; 1.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF07718; Coatamer_beta_C; 1.
Pfam; PF14806; Coatomer_b_Cpla; 1.
PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
SUPFAM; SSF48371; SSF48371; 2.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
Golgi apparatus; Membrane; Protein transport; Reference proteome;
Repeat; Transport.
CHAIN 1 964 Coatomer subunit beta.
/FTId=PRO_0000193837.
REPEAT 129 166 HEAT 1.
REPEAT 238 275 HEAT 2.
REPEAT 314 351 HEAT 3.
REPEAT 393 430 HEAT 4.
REPEAT 466 506 HEAT 5.
CONFLICT 68 68 Q -> E (in Ref. 1; AAA21090).
{ECO:0000305}.
CONFLICT 168 168 V -> A (in Ref. 1; AAA21090).
{ECO:0000305}.
CONFLICT 239 240 ER -> DG (in Ref. 1; AAA21090).
{ECO:0000305}.
CONFLICT 325 325 R -> P (in Ref. 1; AAA21090).
{ECO:0000305}.
CONFLICT 507 515 AGGNAAGSA -> EAAMQLDR (in Ref. 1;
AAA21090). {ECO:0000305}.
CONFLICT 543 543 A -> P (in Ref. 1; AAA21090).
{ECO:0000305}.
CONFLICT 938 943 IRAKSQ -> LRQES (in Ref. 1; AAA21090).
{ECO:0000305}.
SEQUENCE 964 AA; 107407 MW; 08AB7F17F04F361D CRC64;
MTSQVPCYTI INSPDLEVTN EMQLKRDLEK GDTNVKIETL KRVIKLLLNG ERYPGLIMTI
IRFVLPVQNH TIKKLLLIFW EIVPKTSADG KLLQEMILVC DAYRKDLQHP NEFLRGSTLR
FLCKLKEPEL LEPLMPAIRA CLDHRHSYVR RNAVLAIFTI YKNFDWLVPD GPELIASFLD
TQQDMSCKRN AFLMLLHADQ ERALNYLASC IDQVHTFGDI LQLVIVELIY KVCHANPAER
SRFIRCIYNL LNSSSNAVRY ESAGTLITLS LAPTAIKAAA SCYIELVVKE SDNNVKLIVL
DRLVAMKEHE GMEKVMQDLV MDVLRVLAAP DIEVRRKTLA LALDLVYSRN IGEMVLVLKK
EVAKTHNVEH EDTGKYRQLL VRTLHTCSIK FPDVAANVIP VLVEFLSDTN ELAAADVLIF
IREAIQKFPA LRALIIEHLI EAFPQIKSSK IHRAAVWILG EYVEGSQILE VIAVIQQTLG
EVPMVEAEQR RLAGDQTEEQ KQQQGSAGGN AAGSAAEGSG SGNASNKVTS DGTYATQSAY
SLAPVAKAEK RPPLRQYLMD GDFFIGAALS ATLTKLALRY AELETEARAQ NRLTTQVMLI
MSSILHLGKS GFPSKPITND DTDRIFVCLR TLSERTPEAI SVFTLYCREA LGKMLDAQHD
EDQRMLKEKQ KATAKVQPDD PVLFAQLSNG RDNQLGENVF ESSLNQALAG SKNAQLSDVA
SPNSKLNKVT QLTGFSDPVY AEAYVNVNQY DIVLDVLIVN QTNDTLQNCT LELATLGDLK
LVERPHPVVL APHDFCNIKA NVKVSSTENG IIFGNIVYET ALNTNVVVLN TIHIDIMDYI
IPASCTDTEF RQMWQDFEWE NKVTVNTSFT DLHEYLKHLL KSTNMKCLTP EKALSGQCGF
MAANMYAKSI FGENALANLS IEKPVDDPDS KVTGHIRIRA KSQGMALSLG DKISSSQKQS
VQAA


Related products :

Catalog number Product name Quantity
EIAAB08593 Beta-coat protein,Beta-COP,Coatomer subunit beta,Copb,Copb1,Rat,Rattus norvegicus
EIAAB08600 Beta'-coat protein,Beta'-COP,Coatomer subunit beta',Copb2,Mouse,Mus musculus,p102
EIAAB08599 Beta'-coat protein,Beta'-COP,Coatomer subunit beta',Copb2,p102,Rat,Rattus norvegicus
EIAAB08591 Beta-coat protein,Beta-COP,Coatomer subunit beta,Copb,Copb1,Mouse,Mus musculus
EIAAB08598 Beta'-coat protein,Beta'-COP,Bos taurus,Bovine,Coatomer subunit beta',COPB2,p102
EIAAB08592 Beta-coat protein,Beta-COP,Bos taurus,Bovine,Coatomer subunit beta,COPB1
EIAAB08597 Beta'-coat protein,Beta'-COP,Coatomer subunit beta',COPB2,Homo sapiens,Human,p102
EIAAB08595 Beta-coat protein,Beta-COP,Coatomer subunit beta,COPB1,Pig,Sus scrofa
EIAAB08596 Beta-coat protein,Beta-COP,Coatomer subunit beta,COPB,COPB1,Homo sapiens,Human,MSTP026
EIAAB08594 Beta-coat protein,Beta-COP,Chicken,Coatomer subunit beta,COPB,COPB1,Gallus gallus,RCJMB04_28l17
COPD1 COPB2 Gene coatomer protein complex, subunit beta 2 (beta prime)
EIAAB40065 Homo sapiens,HSD25,Human,Signal sequence receptor subunit beta,SSR2,SSR-beta,Translocon-associated protein subunit beta,TRAPB,TRAP-beta
EIAAB40066 Bos taurus,Bovine,Signal sequence receptor subunit beta,SSR2,SSR-beta,Translocon-associated protein subunit beta,TRAP-beta
EIAAB40067 Mouse,Mus musculus,Signal sequence receptor subunit beta,Ssr2,SSR-beta,Translocon-associated protein subunit beta,TRAP-beta
EIAAB30507 Cbfb,CBF-beta,Core-binding factor subunit beta,Mouse,Mus musculus,PEA2-beta,Pebp2b,PEBP2-beta,Pebpb2,Polyomavirus enhancer-binding protein 2 beta subunit,SL3_AKV core-binding factor beta subunit,SL3-3
E2224r ELISA Beta OL,Beta oligodendroglia,Fibronectin receptor subunit beta,Integrin beta-1,Itgb1,Rat,Rattus norvegicus,VLA-4 subunit beta 96T
U2224r CLIA Beta OL,Beta oligodendroglia,Fibronectin receptor subunit beta,Integrin beta-1,Itgb1,Rat,Rattus norvegicus,VLA-4 subunit beta 96T
U2224r CLIA kit Beta OL,Beta oligodendroglia,Fibronectin receptor subunit beta,Integrin beta-1,Itgb1,Rat,Rattus norvegicus,VLA-4 subunit beta 96T
E2224r ELISA kit Beta OL,Beta oligodendroglia,Fibronectin receptor subunit beta,Integrin beta-1,Itgb1,Rat,Rattus norvegicus,VLA-4 subunit beta 96T
E2224r Beta OL,Beta oligodendroglia,Fibronectin receptor subunit beta,Integrin beta-1,Itgb1,Rat,Rattus norvegicus,VLA-4 subunit beta
CSB-EL005784HU Human coatomer protein complex, subunit beta 2 (beta prime) (COPB2) ELISA kit, Species Human, Sample Type serum, plasma 96T
E1761h ELISA Homo sapiens,Human,IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,OSMR,OSMRB 96T
U1761h CLIA Homo sapiens,Human,IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,OSMR,OSMRB 96T
E1761h ELISA kit Homo sapiens,Human,IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,OSMR,OSMRB 96T
EIAAB30508 CBFB,CBF-beta,Core-binding factor subunit beta,Homo sapiens,Human,PEA2-beta,PEBP2-beta,Polyomavirus enhancer-binding protein 2 beta subunit,SL3_AKV core-binding factor beta subunit,SL3-3 enhancer fact


 

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