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

UDP-arabinopyranose mutase 2 (EC 5.4.99.30) (Reversibly glycosylated polypeptide 2) (AtRGP2) (UDP-L-arabinose mutase 2)

 RGP2_ARATH              Reviewed;         360 AA.
Q9LFW1; O22428; Q8LB19;
27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 115.
RecName: Full=UDP-arabinopyranose mutase 2 {ECO:0000305};
EC=5.4.99.30 {ECO:0000269|PubMed:21478444};
AltName: Full=Reversibly glycosylated polypeptide 2 {ECO:0000303|PubMed:21478444};
Short=AtRGP2 {ECO:0000303|PubMed:21478444};
AltName: Full=UDP-L-arabinose mutase 2 {ECO:0000305};
Name=RGP2 {ECO:0000303|PubMed:21478444};
OrderedLocusNames=At5g15650 {ECO:0000312|Araport:AT5G15650};
ORFNames=F14F8_30 {ECO:0000312|EMBL:CAC01764.1};
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].
PubMed=9536051; DOI=10.1104/pp.116.4.1339;
Delgado I.J., Wang Z., de Rocher A., Keegstra K., Raikhel N.V.;
"Cloning and characterization of AtRGP1. A reversibly autoglycosylated
arabidopsis protein implicated in cell wall biosynthesis.";
Plant Physiol. 116:1339-1350(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
DISRUPTION PHENOTYPE.
PubMed=17071651; DOI=10.1104/pp.106.086363;
Drakakaki G., Zabotina O., Delgado I., Robert S., Keegstra K.,
Raikhel N.;
"Arabidopsis reversibly glycosylated polypeptides 1 and 2 are
essential for pollen development.";
Plant Physiol. 142:1480-1492(2006).
[7]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION
PHENOTYPE.
PubMed=21478444; DOI=10.1105/tpc.111.083931;
Rautengarten C., Ebert B., Herter T., Petzold C.J., Ishii T.,
Mukhopadhyay A., Usadel B., Scheller H.V.;
"The interconversion of UDP-L-arabinopyranose and UDP-L-
arabinofuranose is indispensable for plant development in
Arabidopsis.";
Plant Cell 23:1373-1390(2011).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: UDP-L-arabinose mutase involved in the biosynthesis of
cell wall non-cellulosic polysaccharides. Catalyzes the
interconvertion of UDP-L-arabinopyranose (UDP-Arap) and UDP-L-
arabinofuranose (UDP-Araf) in vitro. Preferentially catalyzes the
formation of UDP-Arap from UDP-Araf. At thermodynamic equilibrium
in vitro the ratio of the pyranose form over the furanose form is
95:5. Is not active on other UDP-sugars (UDP-Gal, UDP-Xyl, UDP-
Glc, GDP-Man and GDP-Fuc) (PubMed:21478444). Functions redundantly
with RGP2 and is essential for proper cell walls and pollen
development. Probably involved in the formation of the
pectocellulosic cell wall layer intine. Is probably active as
heteromer in vivo (PubMed:17071651). {ECO:0000269|PubMed:17071651,
ECO:0000269|PubMed:21478444}.
-!- CATALYTIC ACTIVITY: UDP-beta-L-arabinofuranose = UDP-beta-L-
arabinopyranose. {ECO:0000269|PubMed:21478444}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q8H8T0};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q8H8T0};
-!- SUBUNIT: Heteromers with RGP1, RGP4 and RGP5.
{ECO:0000269|PubMed:17071651}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus.
Note=Soluble and membrane-associated.
{ECO:0000269|PubMed:17071651, ECO:0000269|PubMed:21478444}.
-!- TISSUE SPECIFICITY: Predominantly expressed in shoot and root
apical meristems. Expressed in epidermal cells of leaves,
inflorescence stems and seed coat. Expressed in pollen.
{ECO:0000269|PubMed:17071651, ECO:0000269|PubMed:21478444}.
-!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
{ECO:0000250|UniProtKB:Q8H8T0}.
-!- PTM: Reversibly glycosylated in vitro by UDP-glucose, UDP-xylose
and UDP-galactose, but not UDP-mannose.
{ECO:0000250|UniProtKB:Q9SRT9}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
condition, but significant reduction in total cell wall arabinose.
Rgp1 and rgp2 double mutant is male gametophyte lethal, with an
arrest in pollen mitosis (PubMed:17071651). RNAi-mediated
knockdown of both RGP1 and RGP2 causes severe developmental
defects and strong reduction in total cell wall arabinose
(PubMed:21478444). {ECO:0000269|PubMed:17071651,
ECO:0000269|PubMed:21478444}.
-!- SIMILARITY: Belongs to the RGP family. {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; AF013628; AAC50001.1; -; mRNA.
EMBL; AL391144; CAC01764.1; -; Genomic_DNA.
EMBL; CP002688; AED92188.1; -; Genomic_DNA.
EMBL; AY039846; AAK63950.1; -; mRNA.
EMBL; AY120691; AAM52234.1; -; mRNA.
EMBL; AY087476; AAM65020.1; -; mRNA.
PIR; T51394; T51394.
RefSeq; NP_197069.1; NM_121569.3.
UniGene; At.24638; -.
SMR; Q9LFW1; -.
BioGrid; 16695; 3.
IntAct; Q9LFW1; 2.
STRING; 3702.AT5G15650.1; -.
CAZy; GT75; Glycosyltransferase Family 75.
iPTMnet; Q9LFW1; -.
PaxDb; Q9LFW1; -.
PRIDE; Q9LFW1; -.
ProMEX; Q9LFW1; -.
EnsemblPlants; AT5G15650.1; AT5G15650.1; AT5G15650.
GeneID; 831419; -.
Gramene; AT5G15650.1; AT5G15650.1; AT5G15650.
KEGG; ath:AT5G15650; -.
Araport; AT5G15650; -.
TAIR; locus:2143171; AT5G15650.
eggNOG; ENOG410IHTP; Eukaryota.
eggNOG; ENOG411144T; LUCA.
HOGENOM; HOG000234443; -.
InParanoid; Q9LFW1; -.
KO; K13379; -.
OMA; VTWIDAW; -.
OrthoDB; EOG09360C9G; -.
PhylomeDB; Q9LFW1; -.
BioCyc; ARA:AT5G15650-MONOMER; -.
PRO; PR:Q9LFW1; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9LFW1; baseline and differential.
Genevisible; Q9LFW1; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISS:TAIR.
GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
GO; GO:0016866; F:intramolecular transferase activity; IDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
GO; GO:0052691; F:UDP-arabinopyranose mutase activity; IDA:TAIR.
GO; GO:0019567; P:arabinose biosynthetic process; IMP:TAIR.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:TAIR.
GO; GO:0071669; P:plant-type cell wall organization or biogenesis; IMP:UniProtKB.
GO; GO:0009555; P:pollen development; IGI:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0033356; P:UDP-L-arabinose metabolic process; IMP:TAIR.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR004901; RGP.
InterPro; IPR037595; RGP_fam.
PANTHER; PTHR31682; PTHR31682; 1.
Pfam; PF03214; RGP; 1.
PIRSF; PIRSF016429; UPTG; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
Acetylation; Cell wall biogenesis/degradation; Complete proteome;
Cytoplasm; Glycoprotein; Golgi apparatus; Isomerase;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 360 UDP-arabinopyranose mutase 2.
/FTId=PRO_0000410985.
MOTIF 110 112 DXD motif.
{ECO:0000250|UniProtKB:Q8H8T0}.
SITE 158 158 Required for activity.
{ECO:0000250|UniProtKB:Q8H8T0}.
SITE 165 165 Required for activity.
{ECO:0000250|UniProtKB:Q8H8T0}.
MOD_RES 2 2 N-acetylvaline.
{ECO:0000244|PubMed:22223895}.
CARBOHYD 158 158 N-linked (Glc...) arginine.
{ECO:0000250|UniProtKB:P80607}.
CONFLICT 9 9 G -> R (in Ref. 5; AAM65020).
{ECO:0000305}.
CONFLICT 38 38 W -> R (in Ref. 5; AAM65020).
{ECO:0000305}.
CONFLICT 206 206 I -> N (in Ref. 1; AAC50001).
{ECO:0000305}.
CONFLICT 233 233 G -> V (in Ref. 1; AAC50001).
{ECO:0000305}.
CONFLICT 360 360 A -> SLRAV (in Ref. 1; AAC50001).
{ECO:0000305}.
SEQUENCE 360 AA; 40890 MW; 8FE4D48C555F97F1 CRC64;
MVEPANTVGL PVNPTPLLKD ELDIVIPTIR NLDFLEMWRP FLQPYHLIIV QDGDPSKKIH
VPEGYDYELY NRNDINRILG PKASCISFKD SACRCFGYMV SKKKYIFTID DDCFVAKDPS
GKAVNALEQH IKNLLCPSSP FFFNTLYDPY REGADFVRGY PFSLREGVST AVSHGLWLNI
PDYDAPTQLV KPKERNTRYV DAVMTIPKGT LFPMCGMNLA FDRDLIGPAM YFGLMGDGQP
IGRYDDMWAG WCIKVICDHL SLGVKTGLPY IYHSKASNPF VNLKKEYKGI FWQEEIIPFF
QNAKLSKEAV TVQQCYIELS KMVKEKLSSL DPYFDKLADA MVTWIEAWDE LNPPAASGKA


Related products :

Catalog number Product name Quantity
U1645h CLIA BPG-dependent PGAM 2,Homo sapiens,Human,Muscle-specific phosphoglycerate mutase,PGAM2,PGAMM,PGAM-M,Phosphoglycerate mutase 2,Phosphoglycerate mutase isozyme M 96T
E1645h ELISA kit BPG-dependent PGAM 2,Homo sapiens,Human,Muscle-specific phosphoglycerate mutase,PGAM2,PGAMM,PGAM-M,Phosphoglycerate mutase 2,Phosphoglycerate mutase isozyme M 96T
E1645h ELISA BPG-dependent PGAM 2,Homo sapiens,Human,Muscle-specific phosphoglycerate mutase,PGAM2,PGAMM,PGAM-M,Phosphoglycerate mutase 2,Phosphoglycerate mutase isozyme M 96T
EIAAB31647 2,3-bisphosphoglycerate mutase, erythrocyte,2,3-bisphosphoglycerate synthase,2,3-diphosphoglycerate mutase,Bisphosphoglycerate mutase,BPG-dependent PGAM,BPGM,BPGM,DPGM,Homo sapiens,Human
E1645r ELISA kit BPG-dependent PGAM 2,Muscle-specific phosphoglycerate mutase,Pgam2,PGAM-M,Phosphoglycerate mutase 2,Phosphoglycerate mutase isozyme M,Rat,Rattus norvegicus 96T
U1645r CLIA BPG-dependent PGAM 2,Muscle-specific phosphoglycerate mutase,Pgam2,PGAM-M,Phosphoglycerate mutase 2,Phosphoglycerate mutase isozyme M,Rat,Rattus norvegicus 96T
E1645m ELISA BPG-dependent PGAM 2,Mouse,Mus musculus,Muscle-specific phosphoglycerate mutase,Pgam2,PGAM-M,Phosphoglycerate mutase 2,Phosphoglycerate mutase isozyme M 96T
E1645m ELISA kit BPG-dependent PGAM 2,Mouse,Mus musculus,Muscle-specific phosphoglycerate mutase,Pgam2,PGAM-M,Phosphoglycerate mutase 2,Phosphoglycerate mutase isozyme M 96T
E1645r ELISA BPG-dependent PGAM 2,Muscle-specific phosphoglycerate mutase,Pgam2,PGAM-M,Phosphoglycerate mutase 2,Phosphoglycerate mutase isozyme M,Rat,Rattus norvegicus 96T
U1645m CLIA BPG-dependent PGAM 2,Mouse,Mus musculus,Muscle-specific phosphoglycerate mutase,Pgam2,PGAM-M,Phosphoglycerate mutase 2,Phosphoglycerate mutase isozyme M 96T
orb90045 Human 2,3-Bisphosphoglycerate Mutase protein BPGM Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 267 amino acids (1-259 a.a.) and having a molecular m 5
orb90216 Human Phosphoglycerate Mutase 1 protein PGAM1 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids (1-254 a.a.) and having a molecular mass 5
OBT1367 Phosphoglycerate Mutase 1 (PGAM1), Phosphoglycerate Mutase A (PGAMA), Brain, Nonmuscle form, ~28kD, Goat anti_Mouse; WB 100 µg.
EIAAB30676 BPG-dependent PGAM 1,CDABP0006,Homo sapiens,Human,PGAM1,PGAMA,PGAM-B,Phosphoglycerate mutase 1,Phosphoglycerate mutase isozyme B
EIAAB30678 BPG-dependent PGAM 1,Mouse,Mus musculus,Pgam1,PGAM-B,Phosphoglycerate mutase 1,Phosphoglycerate mutase isozyme B
EIAAB30679 Bos taurus,Bovine,BPG-dependent PGAM 1,PGAM1,PGAM-B,Phosphoglycerate mutase 1,Phosphoglycerate mutase isozyme B
EIAAB30677 BPG-dependent PGAM 1,Pgam1,PGAM-B,Phosphoglycerate mutase 1,Phosphoglycerate mutase isozyme B,Rat,Rattus norvegicus
EIAAB31644 2,3-bisphosphoglycerate mutase, erythrocyte,2,3-bisphosphoglycerate synthase,Bisphosphoglycerate mutase,BPG-dependent PGAM,BPGM,BPGM,Oryctolagus cuniculus,Rabbit
EIAAB31646 2,3-bisphosphoglycerate mutase, erythrocyte,2,3-bisphosphoglycerate synthase,Bisphosphoglycerate mutase,Bos taurus,Bovine,BPG-dependent PGAM,BPGM,BPGM
EIAAB31645 2,3-bisphosphoglycerate mutase, erythrocyte,2,3-bisphosphoglycerate synthase,Bisphosphoglycerate mutase,BPG-dependent PGAM,BPGM,Bpgm,Mouse,Mus musculus
GTX107137 Bisphosphoglycerate mutase 100 µl
GTX107137 Bisphosphoglycerate mutase 100 µl
GTX114284 Bisphosphoglycerate mutase 0.1 ml
ARP58217_P050 Bisphosphoglycerate mutase 50 µg
ARP58218_P050 Bisphosphoglycerate mutase 50 µg


 

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