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

Deoxyribodipyrimidine photo-lyase (EC 4.1.99.3) (AtCPDII) (DNA photolyase) (Photoreactivating enzyme 1) (Protein UV RESISTANCE 2)

 PHR_ARATH               Reviewed;         496 AA.
Q9SB00; O24374; Q94CC5; Q9LNA9;
03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 100.
RecName: Full=Deoxyribodipyrimidine photo-lyase;
EC=4.1.99.3;
AltName: Full=AtCPDII;
AltName: Full=DNA photolyase;
AltName: Full=Photoreactivating enzyme 1;
AltName: Full=Protein UV RESISTANCE 2;
Name=PHR1; Synonyms=UVR2; OrderedLocusNames=At1g12370;
ORFNames=F5O11.9;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=9061951; DOI=10.1105/tpc.9.2.199;
Ahmad M., Jarillo J.A., Klimczak L.J., Landry L.G., Peng T.,
Last R.L., Cashmore A.R.;
"An enzyme similar to animal type II photolyases mediates
photoreactivation in Arabidopsis.";
Plant Cell 9:199-207(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Taylor R., Tobin A., Bray C.;
"The cloning and sequence analysis of a putative type II CPD
photolyases from Arabidopsis thaliana.";
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8990208; DOI=10.1073/pnas.94.1.328;
Landry L.G., Stapleton A.E., Lim J., Hoffman P., Hays J.B., Walbot V.,
Last R.L.;
"An Arabidopsis photolyase mutant is hypersensitive to ultraviolet-B
radiation.";
Proc. Natl. Acad. Sci. U.S.A. 94:328-332(1997).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9750104; DOI=10.1073/pnas.94.14.7441;
Jiang C.Z., Yee J., Mitchell D.L., Britt A.B.;
"Photorepair mutants of Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 94:7441-7445(1997).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11069284; DOI=10.1073/pnas.230251897;
Ries G., Buchholz G., Frohnmeyer H., Hohn B.;
"UV-damage-mediated induction of homologous recombination in
Arabidopsis is dependent on photosynthetically active radiation.";
Proc. Natl. Acad. Sci. U.S.A. 97:13425-13429(2000).
[9]
INDUCTION.
PubMed=12011338; DOI=10.1104/pp.010894;
Tanaka A., Sakamoto A., Ishigaki Y., Nikaido O., Sun G., Hase Y.,
Shikazono N., Tano S., Watanabe H.;
"An ultraviolet-B-resistant mutant with enhanced DNA repair in
Arabidopsis.";
Plant Physiol. 129:64-71(2002).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19521716; DOI=10.1007/s00425-009-0962-y;
Kaiser G., Kleiner O., Beisswenger C., Batschauer A.;
"Increased DNA repair in Arabidopsis plants overexpressing CPD
photolyase.";
Planta 230:505-515(2009).
[11]
FUNCTION, AND COFACTOR.
PubMed=20227927; DOI=10.1016/j.dnarep.2010.01.014;
Okafuji A., Biskup T., Hitomi K., Getzoff E.D., Kaiser G.,
Batschauer A., Bacher A., Hidema J., Teranishi M., Yamamoto K.,
Schleicher E., Weber S.;
"Light-induced activation of class II cyclobutane pyrimidine dimer
photolyases.";
DNA Repair 9:495-505(2010).
-!- FUNCTION: Involved in repair of UV radiation-induced DNA damage.
Catalyzes the light-dependent monomerization (300-600 nm) of
cyclobutylpyrimidine dimers (CPDs), which are formed between
adjacent bases on the same DNA strand upon exposure to ultraviolet
radiation. Required for plant survival in the presence of UV-B
light. Not involved in the repair of (6-4) photoproducts.
{ECO:0000269|PubMed:11069284, ECO:0000269|PubMed:19521716,
ECO:0000269|PubMed:20227927, ECO:0000269|PubMed:8990208,
ECO:0000269|PubMed:9061951, ECO:0000269|PubMed:9750104}.
-!- CATALYTIC ACTIVITY: Cyclobutadipyrimidine (in DNA) = 2 pyrimidine
residues (in DNA).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:20227927};
Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:20227927};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19521716}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9SB00-1; Sequence=Displayed;
Name=2;
IsoId=Q9SB00-2; Sequence=VSP_040972;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in flowers. Expressed in
roots and stems. {ECO:0000269|PubMed:9061951}.
-!- INDUCTION: By high-fluence white light, UV-A and UV-B.
{ECO:0000269|PubMed:12011338, ECO:0000269|PubMed:9061951}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under white light, but
inhibition of growth and leaf necrosis under white light and UV-B.
Increasesd accumulation of CPDs under UV-B.
{ECO:0000269|PubMed:11069284, ECO:0000269|PubMed:8990208,
ECO:0000269|PubMed:9061951, ECO:0000269|PubMed:9750104}.
-!- MISCELLANEOUS: Over-expression of PHR1 decreases CPDs accumulation
during UV-B treatment.
-!- SIMILARITY: Belongs to the DNA photolyase class-2 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF79657.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF053365; AAC08008.1; -; mRNA.
EMBL; X99301; CAA67683.1; -; mRNA.
EMBL; AB010875; BAA74701.1; -; Genomic_DNA.
EMBL; AC025416; AAF79657.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE28871.1; -; Genomic_DNA.
EMBL; CP002684; AEE28872.1; -; Genomic_DNA.
EMBL; AY034961; AAK59467.1; -; mRNA.
EMBL; AY113909; AAM44957.1; -; mRNA.
PIR; T52112; T52112.
RefSeq; NP_563906.1; NM_101109.1. [Q9SB00-2]
RefSeq; NP_849651.1; NM_179320.2. [Q9SB00-1]
UniGene; At.19160; -.
UniGene; At.70097; -.
ProteinModelPortal; Q9SB00; -.
SMR; Q9SB00; -.
STRING; 3702.AT1G12370.2; -.
PaxDb; Q9SB00; -.
EnsemblPlants; AT1G12370.1; AT1G12370.1; AT1G12370. [Q9SB00-2]
EnsemblPlants; AT1G12370.2; AT1G12370.2; AT1G12370. [Q9SB00-1]
GeneID; 837792; -.
Gramene; AT1G12370.1; AT1G12370.1; AT1G12370.
Gramene; AT1G12370.2; AT1G12370.2; AT1G12370.
KEGG; ath:AT1G12370; -.
Araport; AT1G12370; -.
TAIR; locus:2034675; AT1G12370.
eggNOG; KOG0133; Eukaryota.
eggNOG; COG0415; LUCA.
HOGENOM; HOG000016456; -.
InParanoid; Q9SB00; -.
KO; K01669; -.
OMA; MHGYMRM; -.
OrthoDB; EOG0936088L; -.
PhylomeDB; Q9SB00; -.
BioCyc; ARA:AT1G12370-MONOMER; -.
BRENDA; 4.1.99.3; 399.
PRO; PR:Q9SB00; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9SB00; baseline and differential.
Genevisible; Q9SB00; AT.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003913; F:DNA photolyase activity; IDA:TAIR.
GO; GO:0071949; F:FAD binding; IEA:EnsemblPlants.
GO; GO:0000719; P:photoreactive repair; IMP:TAIR.
GO; GO:0009650; P:UV protection; IMP:TAIR.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
InterPro; IPR036155; Crypto/Photolyase_N_sf.
InterPro; IPR008148; DNA_photolyase_2.
InterPro; IPR032673; DNA_photolyase_2_CS.
InterPro; IPR006050; DNA_photolyase_N.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF00875; DNA_photolyase; 1.
SUPFAM; SSF48173; SSF48173; 1.
SUPFAM; SSF52425; SSF52425; 1.
TIGRFAMs; TIGR00591; phr2; 1.
PROSITE; PS01083; DNA_PHOTOLYASES_2_1; 1.
PROSITE; PS01084; DNA_PHOTOLYASES_2_2; 1.
PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; DNA damage; DNA repair;
DNA-binding; FAD; Flavoprotein; Lyase; Nucleotide-binding; Nucleus;
Reference proteome.
CHAIN 1 496 Deoxyribodipyrimidine photo-lyase.
/FTId=PRO_0000407851.
DOMAIN 28 160 Photolyase/cryptochrome alpha/beta.
NP_BIND 269 273 FAD. {ECO:0000250}.
NP_BIND 307 315 FAD. {ECO:0000250}.
NP_BIND 415 417 FAD. {ECO:0000250}.
BINDING 256 256 FAD. {ECO:0000250}.
BINDING 307 307 DNA. {ECO:0000255}.
SITE 366 366 Electron transfer via tryptophanyl
radical. {ECO:0000255}.
SITE 387 387 Electron transfer via tryptophanyl
radical. {ECO:0000255}.
SITE 394 394 Electron transfer via tryptophanyl
radical. {ECO:0000255}.
VAR_SEQ 365 370 Missing (in isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_040972.
CONFLICT 23 23 L -> S (in Ref. 1; AAC08008 and 2;
CAA67683). {ECO:0000305}.
CONFLICT 303 303 T -> I (in Ref. 1; AAC08008 and 2;
CAA67683). {ECO:0000305}.
CONFLICT 374 374 V -> L (in Ref. 1; AAC08008 and 2;
CAA67683). {ECO:0000305}.
SEQUENCE 496 AA; 57055 MW; 0EEC0511BE8F5639 CRC64;
MASTVSVQPG RIRILKKGSW QPLDQTVGPV VYWMFRDQRL KDNWALIHAV DLANRTNAPV
AVVFNLFDQF LDAKARQLGF MLKGLRQLHH QIDSLQIPFF LLQGDAKETI PNFLTECGAS
HLVTDFSPLR EIRRCKDEVV KRTSDSLAIH EVDAHNVVPM WAASSKLEYS ARTIRGKINK
LLPDYLIEFP KLEPPKKKWT GMMDKKLVDW DSLIDKVVRE GAEVPEIEWC VPGEDAGIEV
LMGNKDGFLT KRLKNYSTDR NNPIKPKALS GLSPYLHFGQ VSAQRCALEA RKVRSTSPQA
VDTFLEELIV RRELSDNFCY YQPHYDSLKG AWEWARKSLM DHASDKREHI YSLEQLEKGL
TADPLWNASQ LEMVYQGKMH GFMRMYWAKK ILEWTKGPEE ALSISIYLNN KYEIDGRDPS
GYVGCMWSIC GVHDQGWKER PVFGKIRYMN YAGCKRKFNV DSYISYVKSL VSVTKKKRKA
EEQLTRDSVD PKITIV


Related products :

Catalog number Product name Quantity
enz-702 Recombinant Human Deoxyribodipyrimidine photo-lyase 100
enz-702 Recombinant Human Deoxyribodipyrimidine photo-lyase 2
REN-702 Recombinant Human Deoxyribodipyrimidine photo-lyase 2
enz-702 Recombinant Human Deoxyribodipyrimidine photo-lyase 10
EIAAB25874 Influenza resistance protein,Interferon-induced GTP-binding protein Mx1,Mouse,Mus musculus,Mx1,Myxoma resistance protein 1,Myxovirus resistance protein 1
20-783-74648 MOUSE ANTI HUMAN BREAST CANCER RESISTANCE PROTEIN - Placenta-specific ATP-binding cassette transporter; Breast cancer resistance protein; Mitoxantrone resistance-associated protein; CD338 antigen; CDw 1 ml
EIAAB37200 Anthracycline-associated resistance ARX,Mouse,Mus musculus,Sae2,SUMO-activating enzyme subunit 2,Uba2,Ubiquitin-like 1-activating enzyme E1B,Uble1b
EIAAB37199 Anthracycline-associated resistance ARX,Homo sapiens,HRIHFB2115,Human,SAE2,SUMO-activating enzyme subunit 2,UBA2,Ubiquitin-like 1-activating enzyme E1B,UBLE1B
EIAAB25876 Interferon-induced GTP-binding protein Mx1,Mx1,Myxoma resistance protein 1,Myxovirus resistance protein 1,Rat,Rattus norvegicus
EIAAB25877 Bos taurus,Bovine,Interferon-induced GTP-binding protein Mx1,MX1,Myxoma resistance protein 1,Myxovirus resistance protein 1
EIAAB25875 Interferon-induced GTP-binding protein Mx1,MX1,Myxoma resistance protein 1,Myxovirus resistance protein 1,Pig,Sus scrofa
361094 Photo Sensor, Visible, NPN, Light On _ Photo Sensor, Visible, NPN, Light On AI AIDC;Pack-PC; 1 Pcs Per Pack
361093 Photo Sensor, Visible, NPN, Dark On _ Photo Sensor, Visible, NPN, Dark On AI AIDC;Pack-PC; 1 Pcs Per Pack
EIAAB25437 ABCC6,Anthracycline resistance-associated protein,ARA,ATP-binding cassette sub-family C member 6,Homo sapiens,Human,MOAT-E,MRP6,Multidrug resistance-associated protein 6,Multi-specific organic anion t
E0960h ELISA ABCG2,ABCP,ATP-binding cassette sub-family G member 2,BCRP,BCRP1,Breast cancer resistance protein,CDw338,Homo sapiens,Human,Mitoxantrone resistance-associated protein,MXR,Placenta-specific ATP-b 96T
U0960h CLIA ABCG2,ABCP,ATP-binding cassette sub-family G member 2,BCRP,BCRP1,Breast cancer resistance protein,CDw338,Homo sapiens,Human,Mitoxantrone resistance-associated protein,MXR,Placenta-specific ATP-bi 96T
E0960h ELISA kit ABCG2,ABCP,ATP-binding cassette sub-family G member 2,BCRP,BCRP1,Breast cancer resistance protein,CDw338,Homo sapiens,Human,Mitoxantrone resistance-associated protein,MXR,Placenta-specific 96T
EIAAB25880 Homo sapiens,Human,Interferon-induced GTP-binding protein Mx2,Interferon-regulated resistance GTP-binding protein MxB,MX2,Myxovirus resistance protein 2,p78-related protein
EIAAB25873 Canis familiaris,Canis lupus familiaris,Dog,Interferon-induced GTP-binding protein Mx1,MX1,Myxoma resistance protein 1,Myxovirus resistance protein 1
EIAAB25426 Abcc2,ATP-binding cassette sub-family C member 2,Canalicular multidrug resistance protein,Canalicular multispecific organic anion transporter 1,Cmoat,Cmrp,Mrp2,Multidrug resistance-associated protein
EIAAB25878 Homo sapiens,Human,IFI-78K,Interferon-induced GTP-binding protein Mx1,Interferon-induced protein p78,Interferon-regulated resistance GTP-binding protein MxA,MX1,Myxoma resistance protein 1,Myxovirus r
EIAAB27668 Bos taurus,Bovine,N-acetylneuraminate lyase,N-acetylneuraminate pyruvate-lyase,N-acetylneuraminic acid aldolase,NALase,NPL,Sialate lyase,Sialate-pyruvate lyase,Sialic acid aldolase,Sialic acid lyase
EIAAB27670 Mouse,Mus musculus,N-acetylneuraminate lyase,N-acetylneuraminate pyruvate-lyase,N-acetylneuraminic acid aldolase,NALase,Npl,Sialate lyase,Sialate-pyruvate lyase,Sialic acid aldolase,Sialic acid lyase
EIAAB08028 Citrate lyase beta-like,Citrate lyase subunit beta-like protein, mitochondrial,CLB,CLYBL,Homo sapiens,Human
223868 PICTOPACK5_Evacuation photo 1


 

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