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

3'-5' exoribonuclease 1 (EC 3.1.-.-) (3'-5' exonuclease ERI1) (Eri-1 homolog) (Histone mRNA 3'-exonuclease 1)

 ERI1_MOUSE              Reviewed;         345 AA.
Q7TMF2; Q3TA98; Q3TNT0; Q80UN4; Q8BWR6; Q9CQ63;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
15-MAR-2004, sequence version 2.
07-NOV-2018, entry version 117.
RecName: Full=3'-5' exoribonuclease 1;
EC=3.1.-.-;
AltName: Full=3'-5' exonuclease ERI1;
AltName: Full=Eri-1 homolog;
AltName: Full=Histone mRNA 3'-exonuclease 1;
Name=Eri1; Synonyms=3'exo, Thex1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Eye, Head, Liver, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
[3]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-107; LYS-108; ASP-130 AND
GLU-132.
PubMed=18438418; DOI=10.1038/nsmb.1417;
Ansel K.M., Pastor W.A., Rath N., Lapan A.D., Glasmacher E., Wolf C.,
Smith L.C., Papadopoulou N., Lamperti E.D., Tahiliani M.,
Ellwart J.W., Shi Y., Kremmer E., Rao A., Heissmeyer V.;
"Mouse Eri1 interacts with the ribosome and catalyzes 5.8S rRNA
processing.";
Nat. Struct. Mol. Biol. 15:523-530(2008).
[4]
IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, AND RNA-BINDING.
PubMed=19470752; DOI=10.1128/MCB.00296-09;
Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.;
"Three proteins of the U7-specific Sm ring function as the molecular
ruler to determine the site of 3'-end processing in mammalian histone
pre-mRNA.";
Mol. Cell. Biol. 29:4045-4056(2009).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: RNA exonuclease that binds to the 3'-end of histone
mRNAs and degrades them, suggesting that it plays an essential
role in histone mRNA decay after replication. A 2' and 3'-hydroxyl
groups at the last nucleotide of the histone 3'-end is required
for efficient degradation of RNA substrates. Also able to degrade
the 3'-overhangs of short interfering RNAs (siRNAs) in vitro,
suggesting a possible role as regulator of RNA interference
(RNAi). Binds with high affinity to the 3' side of the stem-loop
structure and to the downstream cleavage product (DCP) of histone
pre-mRNAs. Requires for binding the 5'-ACCCA-3' sequence present
in stem-loop structure. Able to bind other mRNAs (By similarity).
Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s
ribosomal RNA. {ECO:0000250, ECO:0000269|PubMed:18438418}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
-!- ACTIVITY REGULATION: Although it can bind simultaneously with SLBP
to the 3'-end of histone mRNA, the presence of SLBP prevents the
exonuclease activity. {ECO:0000250}.
-!- SUBUNIT: Identified in a histone pre-mRNA complex, at least
composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Binds to
40S and 60S ribosomal subunits and to 80S assembled ribosomes.
Interacts in a cooperative manner with SLBP to the mature 3'-end
of histone mRNAs. Found in a ternary complex with SLBP and the
stem-loop structure of the 3'-end of histone mRNAs (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q8VC85:Lsm1; NbExp=3; IntAct=EBI-16026214, EBI-16026183;
Q9EPU0:Upf1; NbExp=2; IntAct=EBI-16026214, EBI-6876715;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18438418}.
Nucleus {ECO:0000269|PubMed:18438418}. Nucleus, nucleolus
{ECO:0000269|PubMed:18438418}.
-!- TISSUE SPECIFICITY: Widely expressed with high levels in spleen,
thymus and testis (at protein level).
{ECO:0000269|PubMed:18438418}.
-!- DOMAIN: The SAP domain is necessary for binding to the stem-loop
structure of histone mRNAs and to form the ternary complex with
SLBP, but not for 3'-end histone mRNA exonuclease activity.
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: High neonatal mortality rate. Reduced body
size in surviving mice which is observed as early as embryonic day
15.5 and remains significant in adults.
{ECO:0000269|PubMed:18438418}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AK014041; BAB29127.2; -; mRNA.
EMBL; AK014410; BAB29333.2; -; mRNA.
EMBL; AK050230; BAC34136.1; -; mRNA.
EMBL; AK165026; BAE38007.1; -; mRNA.
EMBL; AK172005; BAE42771.1; -; mRNA.
EMBL; BC046412; AAH46412.1; -; mRNA.
CCDS; CCDS22244.1; -.
RefSeq; NP_080343.4; NM_026067.3.
UniGene; Mm.207534; -.
ProteinModelPortal; Q7TMF2; -.
SMR; Q7TMF2; -.
BioGrid; 212065; 1.
DIP; DIP-60112N; -.
IntAct; Q7TMF2; 3.
STRING; 10090.ENSMUSP00000033927; -.
iPTMnet; Q7TMF2; -.
PhosphoSitePlus; Q7TMF2; -.
EPD; Q7TMF2; -.
MaxQB; Q7TMF2; -.
PaxDb; Q7TMF2; -.
PeptideAtlas; Q7TMF2; -.
PRIDE; Q7TMF2; -.
GeneID; 67276; -.
KEGG; mmu:67276; -.
UCSC; uc009lky.2; mouse.
CTD; 90459; -.
MGI; MGI:1914526; Eri1.
eggNOG; KOG0542; Eukaryota.
eggNOG; COG5018; LUCA.
HOGENOM; HOG000006635; -.
HOVERGEN; HBG048925; -.
InParanoid; Q7TMF2; -.
KO; K18416; -.
PhylomeDB; Q7TMF2; -.
TreeFam; TF313449; -.
PRO; PR:Q7TMF2; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_THEX1; -.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008408; F:3'-5' exonuclease activity; ISS:UniProtKB.
GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
GO; GO:0071207; F:histone pre-mRNA stem-loop binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IBA:GO_Central.
GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
GO; GO:0031125; P:rRNA 3'-end processing; IDA:UniProtKB.
Gene3D; 1.10.720.30; -; 1.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR003034; SAP_dom.
InterPro; IPR036361; SAP_dom_sf.
Pfam; PF00929; RNase_T; 1.
Pfam; PF02037; SAP; 1.
SMART; SM00479; EXOIII; 1.
SMART; SM00513; SAP; 1.
SUPFAM; SSF53098; SSF53098; 1.
SUPFAM; SSF68906; SSF68906; 1.
PROSITE; PS50800; SAP; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Magnesium;
Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
RNA-binding; RNA-mediated gene silencing; rRNA processing.
CHAIN 1 345 3'-5' exoribonuclease 1.
/FTId=PRO_0000187008.
DOMAIN 72 106 SAP. {ECO:0000255|PROSITE-
ProRule:PRU00186}.
DOMAIN 126 302 Exonuclease.
ACT_SITE 132 132 Proton acceptor. {ECO:0000255}.
ACT_SITE 289 289 Proton acceptor. {ECO:0000255}.
METAL 130 130 Magnesium 1. {ECO:0000250}.
METAL 130 130 Magnesium 2. {ECO:0000250}.
METAL 132 132 Magnesium 1. {ECO:0000250}.
METAL 230 230 Magnesium 2. {ECO:0000250}.
METAL 294 294 Magnesium 1. {ECO:0000250}.
BINDING 132 132 AMP. {ECO:0000250}.
BINDING 133 133 AMP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 289 289 AMP. {ECO:0000250}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IV48}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IV48}.
MUTAGEN 107 107 K->A: Impairs binding to and processing
of 5.8S rRNA; when associated with A-108.
{ECO:0000269|PubMed:18438418}.
MUTAGEN 108 108 K->A: Impairs binding to and processing
of 5.8S rRNA; when associated with A-107.
{ECO:0000269|PubMed:18438418}.
MUTAGEN 130 130 D->G: No effect on binding to 5.8S rRNA;
when associated with G-132.
{ECO:0000269|PubMed:18438418}.
MUTAGEN 132 132 E->G: No effect on binding to 5.8S rRNA;
when associated with G-130.
{ECO:0000269|PubMed:18438418}.
CONFLICT 15 16 QQ -> HE (in Ref. 1; BAB29127).
{ECO:0000305}.
CONFLICT 176 176 A -> D (in Ref. 1; BAB29127/BAB29333/
BAE38007). {ECO:0000305}.
CONFLICT 303 303 V -> I (in Ref. 1; BAB29127/BAB29333/
BAC34136/BAE38007). {ECO:0000305}.
CONFLICT 344 344 R -> K (in Ref. 1; BAC34136).
{ECO:0000305}.
SEQUENCE 345 AA; 39493 MW; 96BDFD215D950AEF CRC64;
MEDERGRERG GDAAQQKTPR PECEESRPLS VEKKQRCRLD GKETDGSKFI SSNGSDFSDP
VYKEIAMTNG CINRMSKEEL RAKLSEFKLE TRGVKDVLKK RLKNYYKKQK LMLKESSAGD
SYYDYICIID FEATCEEGNP AEFLHEIIEF PVVLLNTHTL EIEDTFQQYV RPEVNAQLSE
FCIGLTGITQ DQVDRADAFP QVLKKVIEWM KSKELGTKYK YCILTDGSWD MSKFLSIQCR
LSRLKHPAFA KKWINIRKSY GNFYKVPRSQ TKLTIMLEKL GMDYDGRPHS GLDDSKNIAR
IAVRMLQDGC ELRINEKILG GQLMSVSSSL PVEGAPAPQM PHSRK


Related products :

Catalog number Product name Quantity
EIAAB13233 3'-5' exonuclease ERI1,3'-5' exoribonuclease 1,3'EXO,ERI1,Eri-1 homolog,HEXO,Histone mRNA 3'-end-specific exoribonuclease,Histone mRNA 3'-exonuclease 1,Homo sapiens,Human,Protein 3'hExo,THEX1
EIAAB13234 3'-5' exonuclease ERI1,3'-5' exoribonuclease 1,3'exo,Eri1,Eri-1 homolog,Histone mRNA 3'-exonuclease 1,Mouse,Mus musculus,Thex1
18-003-44239 Histone mRNA 3'-exonuclease 1 - EC 3.1.-.-; 3'-5' exonuclease ERI1; Eri-1 homolog; Histone mRNA 3'-end-specific exoribonuclease; Protein 3'hExo; HEXO Polyclonal 0.1 mg Protein A
EIAAB13232 3'-5' exoribonuclease 1,Eri1,Histone mRNA 3'-exonuclease 1,Rat,Rattus norvegicus,Thex1
EIAAB13236 ERI1 exoribonuclease 2,Eri2,Exod1,Exonuclease domain-containing protein 1,Kiaa1504,Mouse,Mus musculus
EIAAB13235 ERI1 exoribonuclease 2,ERI2,EXOD1,Exonuclease domain-containing protein 1,Homo sapiens,Human,KIAA1504
18-003-43097 RNA exonuclease 4 - EC 3.1.-.-; Exonuclease XPMC2; hPMC2; Prevents mitotic catastrophe 2 protein homolog Polyclonal 0.05 mg Aff Pur
18-003-43366 RNA exonuclease 4 - EC 3.1.-.-; Exonuclease XPMC2; hPMC2; Prevents mitotic catastrophe 2 protein homolog Polyclonal 0.1 mg Protein A
EIAAB25855 EXD3,Exonuclease 3'-5' domain-containing protein 3,HBE269,Homo sapiens,Human,Probable exonuclease mut-7 homolog
EIAAB34334 Exonuclease XPMC2,Gm111,Mouse,Mus musculus,Pmc2,Prevents mitotic catastrophe 2 protein homolog,Rexo4,RNA exonuclease 4,Xpmc2h
EIAAB34333 Exonuclease XPMC2,Homo sapiens,hPMC2,Human,PMC2,Prevents mitotic catastrophe 2 protein homolog,REXO4,RNA exonuclease 4,XPMC2H
29-513 THEX1 contains 1 SAP domain and 1 exonuclease domain. It is an RNA exonuclease that binds to the 3' end of histone mRNAs and probably degrades them, suggesting that it plays an essential role in histo 0.05 mg
29-514 THEX1 contains 1 SAP domain and 1 exonuclease domain. It is an RNA exonuclease that binds to the 3' end of histone mRNAs and probably degrades them, suggesting that it plays an essential role in histo 0.1 mg
GWB-F4A025 Anti- THEX1 (three prime histone mRNA exonuclease 1) Antibody
EIAAB13447 EXO1,EXOI,Exonuclease 1,Exonuclease I,HEX1,hExo1,hExoI,Homo sapiens,Human
EIAAB13448 Exo1,Exonuclease 1,Exonuclease I,mExo1,Mouse,Mus musculus
18-003-44234 Exosome complex exonuclease MTR3 - EC 3.1.13.-; mRNA transport regulator 3 homolog; hMtr3; Exosome component 6; p11 Polyclonal 0.05 mg Aff Pur
18-003-43666 Exosome complex exonuclease MTR3 - EC 3.1.13.-; mRNA transport regulator 3 homolog; hMtr3; Exosome component 6; p11 Polyclonal 0.1 mg Protein A
29-286 ISG20 belongs to the the exonuclease superfamily. It is exonuclease with specificity for single-stranded RNA and, to a lesser extent for DNA. It degrades RNA at a rate that is approximately 35-fold hi 0.05 mg
29-287 ISG20 belongs to the the exonuclease superfamily. It is exonuclease with specificity for single-stranded RNA and, to a lesser extent for DNA. It degrades RNA at a rate that is approximately 35-fold hi 0.1 mg
201-20-4850 REX2{Homo sapiens REX2, RNA exonuclease 2 homolog (S. cerevisiae), mRNA (cDNA clone IMAGE 3611742), complete cds}rabbit.pAb 0.2ml
EIAAB43821 3'-5' exonuclease TREX1,DNase III,Homo sapiens,Human,Three prime repair exonuclease 1,TREX1
EIAAB43824 3'-5' exonuclease TREX2,Homo sapiens,Human,Three prime repair exonuclease 2,TREX2
EIAAB43823 3'-5' exonuclease TREX1,Mouse,Mus musculus,Three prime repair exonuclease 1,Trex1
EIAAB43825 3'-5' exonuclease TREX2,Mouse,Mus musculus,Three prime repair exonuclease 2,Trex2


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | 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 | 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 | 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 | Gentaur