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

Ribonuclease H2 subunit A (RNase H2 subunit A) (EC 3.1.26.4) (Ribonuclease HI large subunit) (RNase HI large subunit) (Ribonuclease HI subunit A)

 RNH2A_MOUSE             Reviewed;         301 AA.
Q9CWY8; Q8CHY8;
15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 2.
05-DEC-2018, entry version 133.
RecName: Full=Ribonuclease H2 subunit A;
Short=RNase H2 subunit A;
EC=3.1.26.4;
AltName: Full=Ribonuclease HI large subunit;
Short=RNase HI large subunit;
AltName: Full=Ribonuclease HI subunit A;
Name=Rnaseh2a; Synonyms=Rnasehi;
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; TISSUE=Embryonic stem cell, and Kidney;
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=C57BL/6J; TISSUE=Mammary gland;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and 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).
[5]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
SUBUNIT, COFACTOR, AND MUTAGENESIS OF ASP-34; GLU-35; GLY-37; ASP-142
AND ASP-170.
PubMed=19923215; DOI=10.1074/jbc.M109.059048;
Shaban N.M., Harvey S., Perrino F.W., Hollis T.;
"The structure of the mammalian RNase H2 complex provides insight into
RNA.NA hybrid processing to prevent immune dysfunction.";
J. Biol. Chem. 285:3617-3624(2010).
-!- FUNCTION: Catalytic subunit of RNase HII, an endonuclease that
specifically degrades the RNA of RNA:DNA hybrids. Participates in
DNA replication, possibly by mediating the removal of lagging-
strand Okazaki fragment RNA primers during DNA replication.
Mediates the excision of single ribonucleotides from DNA:RNA
duplexes. {ECO:0000269|PubMed:19923215}.
-!- CATALYTIC ACTIVITY:
Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.;
EC=3.1.26.4; Evidence={ECO:0000269|PubMed:19923215};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Manganese or magnesium. Binds 1 divalent metal ion per
monomer in the absence of substrate. May bind a second metal ion
after substrate binding. {ECO:0000250};
-!- SUBUNIT: The RNase H2 complex is a heterotrimer composed of the
catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B
and RNASEH2C. {ECO:0000269|PubMed:19923215}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
{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; AK010292; BAB26828.1; -; mRNA.
EMBL; AK146518; BAE27230.1; -; mRNA.
EMBL; BC038158; AAH38158.1; -; mRNA.
CCDS; CCDS22486.1; -.
RefSeq; NP_081463.1; NM_027187.3.
RefSeq; XP_011246799.1; XM_011248497.2.
RefSeq; XP_011246800.1; XM_011248498.2.
UniGene; Mm.182470; -.
PDB; 3KIO; X-ray; 2.90 A; A=1-301.
PDB; 3P5J; X-ray; 2.90 A; A=1-301.
PDBsum; 3KIO; -.
PDBsum; 3P5J; -.
ProteinModelPortal; Q9CWY8; -.
SMR; Q9CWY8; -.
STRING; 10090.ENSMUSP00000105358; -.
iPTMnet; Q9CWY8; -.
PhosphoSitePlus; Q9CWY8; -.
EPD; Q9CWY8; -.
MaxQB; Q9CWY8; -.
PaxDb; Q9CWY8; -.
PeptideAtlas; Q9CWY8; -.
PRIDE; Q9CWY8; -.
DNASU; 69724; -.
Ensembl; ENSMUST00000109736; ENSMUSP00000105358; ENSMUSG00000052926.
Ensembl; ENSMUST00000109738; ENSMUSP00000105360; ENSMUSG00000052926.
Ensembl; ENSMUST00000147812; ENSMUSP00000120374; ENSMUSG00000052926.
GeneID; 69724; -.
KEGG; mmu:69724; -.
UCSC; uc009mok.1; mouse.
CTD; 10535; -.
MGI; MGI:1916974; Rnaseh2a.
eggNOG; KOG2299; Eukaryota.
eggNOG; COG0164; LUCA.
GeneTree; ENSGT00390000010768; -.
HOGENOM; HOG000100290; -.
HOVERGEN; HBG023585; -.
InParanoid; Q9CWY8; -.
KO; K10743; -.
OrthoDB; EOG091G0E06; -.
PhylomeDB; Q9CWY8; -.
TreeFam; TF314302; -.
BRENDA; 3.1.26.4; 3474.
ChiTaRS; Rnaseh2a; mouse.
EvolutionaryTrace; Q9CWY8; -.
PRO; PR:Q9CWY8; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000052926; Expressed in 236 organ(s), highest expression level in testis.
CleanEx; MM_RNASEH2A; -.
ExpressionAtlas; Q9CWY8; baseline and differential.
Genevisible; Q9CWY8; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0032299; C:ribonuclease H2 complex; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; ISS:UniProtKB.
GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
GO; GO:0006298; P:mismatch repair; IMP:MGI.
GO; GO:0006401; P:RNA catabolic process; ISS:UniProtKB.
Gene3D; 1.10.10.460; -; 1.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR004649; RNase_H2_suA.
InterPro; IPR001352; RNase_HII/HIII.
InterPro; IPR024567; RNase_HII/HIII_dom.
InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
PANTHER; PTHR10954; PTHR10954; 1.
Pfam; PF01351; RNase_HII; 1.
SUPFAM; SSF53098; SSF53098; 1.
TIGRFAMs; TIGR00729; TIGR00729; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Endonuclease; Hydrolase;
Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 301 Ribonuclease H2 subunit A.
/FTId=PRO_0000111711.
METAL 34 34 Divalent metal cation. {ECO:0000305}.
METAL 35 35 Divalent metal cation. {ECO:0000305}.
METAL 142 142 Divalent metal cation. {ECO:0000305}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O75792}.
MOD_RES 217 217 Phosphothreonine.
{ECO:0000250|UniProtKB:O75792}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MUTAGEN 34 34 D->N: Loss of enzyme activity.
{ECO:0000269|PubMed:19923215}.
MUTAGEN 35 35 E->A: Loss of enzyme activity.
{ECO:0000269|PubMed:19923215}.
MUTAGEN 37 37 G->S: Strongly reduced in vitro enzyme
activity. {ECO:0000269|PubMed:19923215}.
MUTAGEN 142 142 D->N: Loss of enzyme activity.
{ECO:0000269|PubMed:19923215}.
MUTAGEN 170 170 D->N: Loss of enzyme activity.
{ECO:0000269|PubMed:19923215}.
CONFLICT 132 132 Q -> R (in Ref. 1; BAB26828).
{ECO:0000305}.
TURN 3 6 {ECO:0000244|PDB:3KIO}.
HELIX 7 9 {ECO:0000244|PDB:3KIO}.
STRAND 11 17 {ECO:0000244|PDB:3KIO}.
HELIX 23 26 {ECO:0000244|PDB:3KIO}.
STRAND 29 36 {ECO:0000244|PDB:3KIO}.
STRAND 41 43 {ECO:0000244|PDB:3KIO}.
STRAND 45 53 {ECO:0000244|PDB:3KIO}.
HELIX 54 59 {ECO:0000244|PDB:3KIO}.
HELIX 60 64 {ECO:0000244|PDB:3KIO}.
HELIX 73 85 {ECO:0000244|PDB:3KIO}.
TURN 86 89 {ECO:0000244|PDB:3KIO}.
STRAND 91 97 {ECO:0000244|PDB:3KIO}.
HELIX 99 106 {ECO:0000244|PDB:3KIO}.
STRAND 108 110 {ECO:0000244|PDB:3KIO}.
HELIX 114 131 {ECO:0000244|PDB:3KIO}.
STRAND 136 142 {ECO:0000244|PDB:3KIO}.
HELIX 148 156 {ECO:0000244|PDB:3KIO}.
STRAND 161 166 {ECO:0000244|PDB:3KIO}.
HELIX 169 171 {ECO:0000244|PDB:3KIO}.
HELIX 174 200 {ECO:0000244|PDB:3KIO}.
STRAND 209 211 {ECO:0000244|PDB:3KIO}.
HELIX 215 222 {ECO:0000244|PDB:3KIO}.
TURN 227 229 {ECO:0000244|PDB:3KIO}.
HELIX 240 249 {ECO:0000244|PDB:3KIO}.
STRAND 253 255 {ECO:0000244|PDB:3P5J}.
HELIX 287 293 {ECO:0000244|PDB:3P5J}.
STRAND 295 297 {ECO:0000244|PDB:3P5J}.
SEQUENCE 301 AA; 33513 MW; 3B95211289847CBC CRC64;
MDLSELERDN TGRCRLSSPV PAVCLKEPCV LGVDEAGRGP VLGPMVYAIC YCPLSRLADL
EALKVADSKT LTENERERLF AKMEEDGDFV GWALDVLSPN LISTSMLGRV KYNLNSLSHD
TAAGLIQYAL DQNVNVTQVF VDTVGMPETY QARLQQHFPG IEVTVKAKAD SLFPVVSAAS
IFAKVARDKA VKNWQFVENL QDLDSDYGSG YPNDPKTKAW LRKHVDPVFG FPQFVRFSWS
TAQAILEKEA EDVIWEDSEA EEDPERPGKI TSYFSQGPQT CRPQAPHRYF QERGLEAASS
L


Related products :

Catalog number Product name Quantity
EIAAB35609 AGS4,Aicardi-Goutieres syndrome 4 protein,Homo sapiens,Human,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H(35),RNase H2 subunit A,RNase HI large subunit,RNA
18-003-43617 Ribonuclease H2 subunit A - EC 3.1.26.4; RNase H2 subunit A; Ribonuclease HI subunit A; Ribonuclease HI large subunit; RNase HI large subunit; RNase H(35); Aicardi-Goutieres syndrome 4 protein; AGS4 P 0.05 mg Aff Pur
18-003-43618 Ribonuclease H2 subunit A - EC 3.1.26.4; RNase H2 subunit A; Ribonuclease HI subunit A; Ribonuclease HI large subunit; RNase HI large subunit; RNase H(35); Aicardi-Goutieres syndrome 4 protein; AGS4 P 0.1 mg Protein A
EIAAB35607 Mouse,Mus musculus,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H2 subunit A,RNase HI large subunit,Rnaseh2a,Rnasehi
EIAAB35608 Bos taurus,Bovine,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H2 subunit A,RNase HI large subunit,RNASEH2A
EIAAB35606 Rat,Rattus norvegicus,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H2 subunit A,RNase HI large subunit,Rnaseh2a
EIAAB35615 AGS3,Aicardi-Goutieres syndrome 3 protein,AYP1,Homo sapiens,Human,Ribonuclease H2 subunit C,Ribonuclease HI subunit C,RNase H1 small subunit,RNase H2 subunit C,RNASEH2C
EIAAB35611 Deleted in lymphocytic leukemia 8 homolog,Dleu8,Mouse,Mus musculus,Ribonuclease H2 subunit B,Ribonuclease HI subunit B,RNase H2 subunit B,Rnaseh2b
EIAAB35610 AGS2,Aicardi-Goutieres syndrome 2 protein,Deleted in lymphocytic leukemia 8,DLEU8,Homo sapiens,Human,Ribonuclease H2 subunit B,Ribonuclease HI subunit B,RNase H2 subunit B,RNASEH2B
EIAAB35616 Ayp1,Mouse,Mus musculus,Ribonuclease H2 subunit C,Ribonuclease HI subunit C,RNase H2 subunit C,Rnaseh2c
EIAAB35614 Bos taurus,Bovine,Ribonuclease H2 subunit C,Ribonuclease HI subunit C,RNase H2 subunit C,RNASEH2C
EIAAB35613 Rat,Rattus norvegicus,Ribonuclease H2 subunit B,Ribonuclease HI subunit B,RNase H2 subunit B,Rnaseh2b
EIAAB35612 Bos taurus,Bovine,Ribonuclease H2 subunit B,Ribonuclease HI subunit B,RNase H2 subunit B,RNASEH2B
EIAAB35916 Homo sapiens,Human,Ribonuclease P protein subunit p30,RNase P subunit 2,RNaseP protein p30,RNASEP2,RPP30
EIAAB35921 Homo sapiens,Human,Ribonuclease P protein subunit p40,RNase P subunit 1,RNaseP protein p40,RNASEP1,RPP40
EIAAB35914 Mouse,Mus musculus,Ribonuclease P protein subunit p30,RNase P subunit 2,RNaseP protein p30,Rnasep2,Rpp30
EIAAB35915 Bos taurus,Bovine,Ribonuclease P protein subunit p30,RNase P subunit 2,RNaseP protein p30,RNASEP2,RPP30
EIAAB35908 Homo sapiens,Human,Ribonuclease P protein subunit p25,RNase P protein subunit p25,RPP25
EIAAB35909 Mouse,Mus musculus,Ribonuclease P protein subunit p25,RNase P protein subunit p25,Rpp25
EIAAB35907 Rat,Rattus norvegicus,Ribonuclease P protein subunit p25,RNase P protein subunit p25,Rpp25
EIAAB35513 Homo sapiens,HP-RNase,Human,RIB1,RIB-1,Ribonuclease 1,Ribonuclease A,Ribonuclease pancreatic,RNase 1,RNase A,RNase UpI-1,RNASE1,RNS1
10-288-22279F Ribonuclease P protein subunit p30 - EC 3.1.26.5; RNaseP protein p30; RNase P subunit 2 0.05 mg
10-288-22279F Ribonuclease P protein subunit p30 - EC 3.1.26.5; RNaseP protein p30; RNase P subunit 2 0.1 mg
20-372-60277 ribonuclease P_MRP 30kDa subunit (RPP30) - Mouse monoclonal anti-human RPP30 antibody; EC 3.1.26.5; RNaseP protein p30; RNase P subunit 2 Monoclonal 0.1 mg
20-272-191788 RFC1 - Mouse monoclonal [1320] to RFC1; Replication factor C large subunit; RF-C 140 kDa subunit; Activator 1 140 kDa subunit; Activator 1 large subunit; A1 140 kDa subunit; DNA-binding protein PO-GA 0.05 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





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