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

Dystroglycan (Dystrophin-associated glycoprotein 1) [Cleaved into: Alpha-dystroglycan (Alpha-DG); Beta-dystroglycan (Beta-DG)]

 DAG1_RABIT              Reviewed;         895 AA.
Q28685;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 124.
RecName: Full=Dystroglycan;
AltName: Full=Dystrophin-associated glycoprotein 1;
Contains:
RecName: Full=Alpha-dystroglycan;
Short=Alpha-DG;
Contains:
RecName: Full=Beta-dystroglycan;
Short=Beta-DG;
Flags: Precursor;
Name=DAG1;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 783-793, AND TISSUE
SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=1741056; DOI=10.1038/355696a0;
Ibraghimov-Beskrovnaya O., Ervasti J.M., Leveille C.J.,
Slaughter C.A., Sernett S.W., Campbell K.P.;
"Primary structure of dystrophin-associated glycoproteins linking
dystrophin to the extracellular matrix.";
Nature 355:696-702(1992).
[2]
STRUCTURE OF CARBOHYDRATES.
PubMed=9838223; DOI=10.1016/S0304-4165(98)00114-7;
Sasaki T., Yamada H., Matsumura K., Shimizu T., Kobata A., Endo T.;
"Detection of O-mannosyl glycans in rabbit skeletal muscle alpha-
dystroglycan.";
Biochim. Biophys. Acta 1425:599-606(1998).
[3]
INTERACTION WITH LARGE1, AND LIGAND-BINDING.
PubMed=15210115; DOI=10.1016/j.cell.2004.06.003;
Kanagawa M., Saito F., Kunz S., Yoshida-Moriguchi T., Barresi R.,
Kobayashi Y.M., Muschler J., Dumanski J.P., Michele D.E.,
Oldstone M.B., Campbell K.P.;
"Molecular recognition by LARGE is essential for expression of
functional dystroglycan.";
Cell 117:953-964(2004).
-!- FUNCTION: The dystroglycan complex is involved in a number of
processes including laminin and basement membrane assembly,
sacrolemmal stability, cell survival, peripheral nerve
myelination, nodal structure, cell migration, and epithelial
polarization. {ECO:0000250}.
-!- FUNCTION: Alpha-dystroglycan is an extracellular peripheral
glycoprotein that acts as a receptor for both extracellular matrix
proteins containing laminin-G domains. Receptor for laminin-2
(LAMA2) and agrin in peripheral nerve Schwann cells.
{ECO:0000250}.
-!- FUNCTION: Beta-dystroglycan is a transmembrane protein that plays
important roles in connecting the extracellular matrix to the
cytoskeleton. Acts as a cell adhesion receptor in both muscle and
non-muscle tissues. Receptor for both DMD and UTRN and, through
these interactions, scaffolds axin to the cytoskeleton. Also
functions in cell adhesion-mediated signaling and implicated in
cell polarity (By similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer (By similarity). Heterodimer of alpha- and beta-
dystroglycan subunits which are the central components of the
dystrophin-glycoprotein complex. This complex then can form a
dystrophin-associated glycoprotein complex (DGC) which is composed
of three subcomplexes: a cytoplasmic complex comprised of DMD (or
UTRN), DTNA and a number of syntrophins, such as SNTB1, SNTB2,
SNTG1 and SNTG2, the transmembrane dystroglycan complex, and the
sarcoglycan-sarcospan complex. Interacts (via the N-terminal of
alphaDAG1) with LARGE1; the interaction enhances laminin binding
(PubMed:15210115). Interacts with AGR2 and AGR3. Interacts
(betaDAG1) with DMD; the interaction is inhibited by
phosphorylation on the PPXY motif. Interacts (betaDAG1, via its
PPXY motif) with UTRN (via its WWW and ZZ domains); the
interaction is inhibited by phosphorylation on the PPXY motif.
Interacts (betaDAG1, via its phosphorylated PPXY motif) with the
SH2 domain-containing proteins, FYN, CSK, NCK and SHC. Interacts
(betaDAG1) with CAV3 (via a central WW-like domain); the
interaction disrupts the binding of DMD (By similarity). Interacts
with SGCD. BetaDAG1 directly interacts with ANK3, but not with
ANK2; this interaction does not interfere with DMD-binding and is
required for retention at costameres. Identified in a dystroglycan
complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (By
similarity). {ECO:0000250|UniProtKB:Q14118,
ECO:0000250|UniProtKB:Q62165, ECO:0000269|PubMed:15210115}.
-!- SUBCELLULAR LOCATION: Alpha-dystroglycan: Secreted, extracellular
space {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Beta-dystroglycan: Cell membrane
{ECO:0000250}; Single-pass type I membrane protein. Cytoplasm,
cytoskeleton. Nucleus, nucleoplasm. Cell membrane, sarcolemma
{ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000250}. Note=The monomeric form translocates to the nucleus
via the action of importins and depends on RAN. Nuclear transport
is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this
phosphorylated form locates to a vesicular internal membrane
compartment. In muscle cells, sarcolemma localization requires the
presence of ANK2, while localization to costameres requires the
presence of ANK3 (By similarity). Localizes to neuromuscular
junctions (NMJs) in the presence of ANK2 (By similarity).
Colocalizes with ERM proteins in Schwann-cell microvilli (By
similarity). In peripheral nerves, localizes to the Schwann cell
membrane. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in skeletal muscle, cardiac muscle,
lung, brain, liver, kidney, diaphragm and stomach.
{ECO:0000269|PubMed:1741056}.
-!- PTM: O- and N-glycosylated (By similarity). Alpha-dystroglycan is
heavily O-glycosylated comprising of up to two thirds of its mass
and the carbohydrate composition differs depending on tissue type.
Mucin-type O-glycosylation is important for ligand binding
activity. O-mannosylation of alpha-DAG1 is found in high abundance
in both brain and muscle where the most abundant glycan is Sia-
alpha-2-3-Gal-beta-1-4-Glc-NAc-beta-1-2-Man. O-glycosylated in the
N-terminal region with a core 1 or possibly core 8 glycan. The
beta subunit is N-glycosylated (By similarity). In muscle,
glycosylation on Thr-317, Thr-319 and Thr-379 by a phosphorylated
O-mannosyl glycan with the structure 2-(N-acetylamido)-2-
deoxygalactosyl-beta-1,3-2-(N-acetylamido)-2-deoxyglucosyl-beta-
1,4-6-phosphomannose is mediated by like-
acetylglucosaminyltransferase (LARGE1) protein amd is required for
laminin binding. {ECO:0000250|UniProtKB:Q14118}.
-!- PTM: Autolytic cleavage produces the alpha and beta subunits. In
cutaneous cells, as well as in certain pathological conditions,
shedding of beta-dystroglcan can occur releasing a peptide of
about 30 kDa (By similarity). {ECO:0000250}.
-!- PTM: SRC-mediated phosphorylation of the PPXY motif of the beta
subunit recruits SH2 domain-containing proteins, but inhibits
binding to WWW domain-containing proteins, DMD and UTRN. This
phosphorylation also inhibits nuclear entry (By similarity).
{ECO:0000250}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X64393; CAA45732.1; -; mRNA.
PIR; PN0662; PN0662.
PIR; PN0663; PN0663.
PIR; S20582; S20582.
RefSeq; NP_001095170.1; NM_001101700.1.
RefSeq; XP_017199133.1; XM_017343644.1.
RefSeq; XP_017199134.1; XM_017343645.1.
UniGene; Ocu.2077; -.
ProteinModelPortal; Q28685; -.
SMR; Q28685; -.
CORUM; Q28685; -.
DIP; DIP-679N; -.
IntAct; Q28685; 2.
MINT; MINT-1534332; -.
STRING; 9986.ENSOCUP00000002981; -.
MEROPS; S72.001; -.
UniCarbKB; Q28685; -.
PRIDE; Q28685; -.
Ensembl; ENSOCUT00000003437; ENSOCUP00000002981; ENSOCUG00000003439.
GeneID; 100009278; -.
KEGG; ocu:100009278; -.
CTD; 1605; -.
eggNOG; KOG3781; Eukaryota.
eggNOG; ENOG410XQTU; LUCA.
GeneTree; ENSGT00390000008429; -.
HOGENOM; HOG000072580; -.
HOVERGEN; HBG000078; -.
InParanoid; Q28685; -.
KO; K06265; -.
OMA; AMICYRK; -.
OrthoDB; EOG091G05R9; -.
TreeFam; TF328370; -.
Proteomes; UP000001811; Chromosome 9.
Bgee; ENSOCUG00000003439; -.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0070938; C:contractile ring; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0016011; C:dystroglycan complex; IEA:Ensembl.
GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0030175; C:filopodium; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0033268; C:node of Ranvier; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:Ensembl.
GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0002162; F:dystroglycan binding; IEA:Ensembl.
GO; GO:0043237; F:laminin-1 binding; IDA:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
GO; GO:0008307; F:structural constituent of muscle; IEA:Ensembl.
GO; GO:0015631; F:tubulin binding; IEA:Ensembl.
GO; GO:0017166; F:vinculin binding; IEA:Ensembl.
GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
GO; GO:0071679; P:commissural neuron axon guidance; IEA:Ensembl.
GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IEA:Ensembl.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IDA:CACAO.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
GO; GO:0034453; P:microtubule anchoring; IEA:Ensembl.
GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:Ensembl.
GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0021682; P:nerve maturation; IEA:Ensembl.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; IEA:Ensembl.
GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; IEA:Ensembl.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IEA:Ensembl.
GO; GO:0010470; P:regulation of gastrulation; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.30.70.1040; -; 1.
InterPro; IPR027468; Alpha-dystroglycan_domain_2.
InterPro; IPR006644; Cadg.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR008465; DAG1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR030398; SEA_DG_dom.
Pfam; PF05454; DAG1; 1.
SMART; SM00736; CADG; 2.
SUPFAM; SSF111006; SSF111006; 1.
SUPFAM; SSF49313; SSF49313; 2.
PROSITE; PS51699; SEA_DG; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Disulfide bond; Glycoprotein;
Membrane; Nucleus; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Secreted; Signal; Synapse; Transmembrane;
Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 653 Alpha-dystroglycan.
/FTId=PRO_0000021069.
CHAIN 654 895 Beta-dystroglycan.
/FTId=PRO_0000021070.
TOPO_DOM 654 749 Extracellular.
TRANSMEM 750 775 Helical. {ECO:0000255}.
TOPO_DOM 776 895 Cytoplasmic. {ECO:0000255}.
DOMAIN 603 712 Peptidase S72.
REGION 30 408 Required for laminin recognition.
REGION 49 71 O-glycosylated at one site.
{ECO:0000250}.
REGION 316 485 Mucin-like domain. {ECO:0000250}.
REGION 463 485 O-glycosylated at seven sites with
GalNAc. {ECO:0000250}.
REGION 819 895 Required for interaction with CAV3.
{ECO:0000250}.
REGION 880 895 Required for binding DMD and UTRN.
{ECO:0000250}.
MOTIF 776 782 Nuclear localization signal.
{ECO:0000250}.
MOTIF 889 892 PPXY motif. {ECO:0000250}.
COMPBIAS 809 895 Pro-rich.
SITE 653 654 Cleavage; by autolysis. {ECO:0000250}.
SITE 715 716 Cleavage; by MMP9. {ECO:0000250}.
MOD_RES 790 790 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14118}.
MOD_RES 892 892 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:Q14118}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 317 317 O-linked (Man6P...) threonine.
{ECO:0000250|UniProtKB:Q14118}.
CARBOHYD 319 319 O-linked (Man6P...) threonine.
{ECO:0000250|UniProtKB:Q14118}.
CARBOHYD 379 379 O-linked (Man6P...) threonine.
{ECO:0000250}.
CARBOHYD 641 641 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 649 649 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 661 661 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 182 264 {ECO:0000250}.
DISULFID 669 713 {ECO:0000250}.
SEQUENCE 895 AA; 97030 MW; C2B9E4733A0AB82A CRC64;
MRMSVGLSLL LPLWGRTFLL LLCVAVAQSH WPSEPSEAVR DWENQLEASM HSVLSDLHEA
LPTVVGIPDG TAVVGRSFRV TIPTDLIGSS GEVIKVSTAG KEVLPSWLHW DPQSHTLEGL
PLDTDKGVHY ISVSAAQLDA NGSHIPQTSS VFSIEVYPED HSEPQSVRAA SPDLGEAAAS
ACAAEEPVTV LTVILDADLT KMTPKQRIDL LHRMQSFSEV ELHNMKLVPV VNNRLFDMSA
FMAGPGNAKK VVENGALLSW KLGCSLNQNS VPDIRGVEAP AREGTMSAQL GYPVVGWHIA
NKKPPLPKRI RRQIHATPTP VTAIGPPTTA IQEPPSRIVP TPTSPAIAPP TETMAPPVRD
PVPGKPTVTT RTRGAIIQTP TLGPIQPTRV SDAGTVVSGQ IRATVTIPGY VEPTAVATPP
TTTTKKPRVS TPKPATPSTD SSATTTRRPT KKPRTPRPVP RVTTKAPITR LETASPPTRI
RTTTSGVPRG GEPNQRPELK NHIDRVDAWV GTYFEVKIPS DTFYDKEDTT TDKLKLTLKL
REQQLVGEKS WVQFNSNSQL MYGLPDSSHV GKHEYFMHAT DKGGLSAVDA FEIHVHKRPQ
GDKAPARFKA KFVGDPAPVV NDIHKKIALV KKLAFAFGDR NCSTVTLQNI TRGSIVVEWT
NNTLPLEPCP KEQITGLSRR IAEDNGQPRP AFTNALEPDF KATSIAITGS GSCRHLQFIP
VAPPGIPSSV TPPTEVPDRD PEKSSEDDVY LHTVIPAVVV AAILLIAGII AMICYRKKRK
GKLTLEDQAT FIKKGVPIIF ADELDDSKPP PSSSMPLILQ EEKAPLPPPE YPSQSVPETT
PLNQDTVGEY TPLRDEDPNA PPYQPPPPFT APMEGKGSRP KNMTPYRSPP PYVPP


Related products :

Catalog number Product name Quantity
EIAAB38105 50 kDa dystrophin-associated glycoprotein,50DAG,Adhalin,ADL,Alpha-sarcoglycan,Alpha-SG,DAG2,Dystroglycan-2,Oryctolagus cuniculus,Rabbit,SGCA
EIAAB38106 50 kDa dystrophin-associated glycoprotein,50DAG,Adhalin,ADL,Alpha-sarcoglycan,Alpha-SG,DAG2,Dystroglycan-2,Homo sapiens,Human,SGCA
DAGLB DAG1 Gene dystroglycan 1 (dystrophin-associated glycoprotein 1)
EIAAB10394 DAG1,Dystroglycan,Dystrophin-associated glycoprotein 1,Pig,Sus scrofa
EIAAB10395 Dag1,Dag-1,Dystroglycan,Dystrophin-associated glycoprotein 1,Mouse,Mus musculus
CSB-EL006488HU Human dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit 96T
CSB-EL006488MO Mouse dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit 96T
EIAAB10391 Bos taurus,Bovine,DAG1,Dystroglycan,Dystrophin-associated glycoprotein 1
EIAAB10392 DAG1,Dystroglycan,Dystrophin-associated glycoprotein 1,Oryctolagus cuniculus,Rabbit
CSB-EL006488HU Human dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit SpeciesHuman 96T
CSB-EL006488MO Mouse dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit SpeciesMouse 96T
EIAAB10393 DAG1,Dystroglycan,Dystrophin-associated glycoprotein 1,Homo sapiens,Human
GS-0538a dystroglycan 1 (dystrophin-associated glycoprotein 1) primary antibody, Host: Rabbit 200ul
CSB-EL006488PI Pig dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL006488DO Dog dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL006488BO Bovine dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL006488HU Human dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL006488RB Rabbit dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
CSB-EL006488MO Mouse dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
NB100-79904 Dystroglycan Beta 0.1 ml
GWB-671E0F Beta-Dystroglycan, Antibody
AJ1095a Beta-Dystroglycan Antibody
NB100-79904 Dystroglycan Beta 0.1 ml
NBL1-09713 Alpha Dystroglycan Lysate 0.1 mg
Y090790 Anti-dystroglycan, beta- Monoclonal Antibody 100ul


 

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