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

Myocilin (Trabecular meshwork-induced glucocorticoid response protein) [Cleaved into: Myocilin, N-terminal fragment (Myocilin 20 kDa N-terminal fragment); Myocilin, C-terminal fragment (Myocilin 35 kDa N-terminal fragment)]

 MYOC_MOUSE              Reviewed;         490 AA.
O70624; O70289;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
28-FEB-2018, entry version 135.
RecName: Full=Myocilin;
AltName: Full=Trabecular meshwork-induced glucocorticoid response protein;
Contains:
RecName: Full=Myocilin, N-terminal fragment;
AltName: Full=Myocilin 20 kDa N-terminal fragment;
Contains:
RecName: Full=Myocilin, C-terminal fragment;
AltName: Full=Myocilin 35 kDa N-terminal fragment;
Flags: Precursor;
Name=Myoc; Synonyms=Tigr;
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 [MRNA], TISSUE SPECIFICITY, AND VARIANT ALA-164.
STRAIN=BALB/cJ, C3H/HeJ, and C57BL/6J; TISSUE=Brain, and Muscle;
PubMed=9588210; DOI=10.1006/bbrc.1998.8541;
Tomarev S.I., Tamm E.R., Chang B.;
"Characterization of the mouse Myoc/Tigr gene.";
Biochem. Biophys. Res. Commun. 245:887-893(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT ALA-164.
STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
PubMed=9675094; DOI=10.1006/bbrc.1998.8917;
Takahashi H., Noda S., Imamura Y., Nagasawa A., Kubota R., Mashima Y.,
Kudoh J., Oguchi Y., Shimizu N.;
"Mouse myocilin (Myoc) gene expression in ocular tissues.";
Biochem. Biophys. Res. Commun. 248:104-109(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9548973;
Fingert J.H., Ying L., Swiderski R.E., Nystuen A.M., Arbour N.C.,
Alward W.L.M., Sheffield V.C., Stone E.M.;
"Characterization and comparison of the human and mouse GLC1A glaucoma
genes.";
Genome Res. 8:377-384(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=129/Sv;
PubMed=9680392; DOI=10.1007/s003359900844;
Abderrahim H., Jaramillo-Babb V.L., Zhou Z., Vollrath D.;
"Characterization of the murine TIGR/myocilin gene.";
Mamm. Genome 9:673-675(1998).
[5]
INTERACTION WITH OLFM3.
PubMed=12019210; DOI=10.1093/hmg/11.11.1291;
Torrado M., Trivedi R., Zinovieva R., Karavanova I., Tomarev S.I.;
"Optimedin: a novel olfactomedin-related protein that interacts with
myocilin.";
Hum. Mol. Genet. 11:1291-1301(2002).
[6]
INTERACTION WITH SNCG, AND SUBCELLULAR LOCATION.
PubMed=16392033; DOI=10.1007/s10571-005-8471-4;
Surgucheva I., Park B.C., Yue B.Y., Tomarev S., Surguchov A.;
"Interaction of myocilin with gamma-synuclein affects its secretion
and aggregation.";
Cell. Mol. Neurobiol. 25:1009-1033(2005).
[7]
INTERACTION WITH FRZB AND SFRP1.
PubMed=19188438; DOI=10.1128/MCB.01274-08;
Kwon H.S., Lee H.S., Ji Y., Rubin J.S., Tomarev S.I.;
"Myocilin is a modulator of Wnt signaling.";
Mol. Cell. Biol. 29:2139-2154(2009).
[8]
FUNCTION IN MUSCLE HYPERTROPHY, AND INTERACTION WITH SNTA1.
PubMed=22371502; DOI=10.1074/jbc.M111.224063;
Joe M.K., Kee C., Tomarev S.I.;
"Myocilin interacts with syntrophins and is member of dystrophin-
associated protein complex.";
J. Biol. Chem. 287:13216-13227(2012).
[9]
FUNCTION IN BONE FORMATION, DISRUPTION PHENOTYPE, AND SUBCELLULAR
LOCATION.
PubMed=23629661; DOI=10.1074/jbc.M112.422972;
Kwon H.S., Johnson T.V., Tomarev S.I.;
"Myocilin stimulates osteogenic differentiation of mesenchymal stem
cells through mitogen-activated protein kinase signaling.";
J. Biol. Chem. 288:16882-16894(2013).
[10]
FUNCTION IN MYELINATION, INTERACTION WITH NFASC; GLDN; NRCAM; ERBB2
AND ERBB3, AND TISSUE SPECIFICITY.
PubMed=23897819; DOI=10.1074/jbc.M112.446138;
Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C.,
Tomarev S.I.;
"Myocilin mediates myelination in the peripheral nervous system
through ErbB2/3 signaling.";
J. Biol. Chem. 288:26357-26371(2013).
-!- FUNCTION: Secreted glycoprotein regulating the activation of
different signaling pathways in adjacent cells to control
different processes including cell adhesion, cell-matrix adhesion,
cytoskeleton organization and cell migration. Promotes substrate
adhesion, spreading and formation of focal contacts. Negatively
regulates cell-matrix adhesion and stress fiber assembly through
Rho protein signal transduction. Modulates the organization of
actin cytoskeleton by stimulating the formation of stress fibers
through interactions with components of Wnt signaling pathways.
Promotes cell migration through activation of PTK2 and the
downstream phosphatidylinositol 3-kinase signaling (By
similarity). Plays a role in bone formation and promotes
osteoblast differentiation in a dose-dependent manner through
mitogen-activated protein kinase signaling (PubMed:23629661).
Mediates myelination in the peripheral nervous system through
ERBB2/ERBB3 signaling (PubMed:23897819). Plays a role as a
regulator of muscle hypertrophy through the components of
dystrophin-associated protein complex (PubMed:22371502). Involved
in positive regulation of mitochondrial depolarization. Plays a
role in neurite outgrowth. May participate in the obstruction of
fluid outflow in the trabecular meshwork (By similarity).
{ECO:0000250|UniProtKB:Q99972, ECO:0000269|PubMed:22371502,
ECO:0000269|PubMed:23629661, ECO:0000269|PubMed:23897819}.
-!- SUBUNIT: Homodimer (via N-terminus). Interacts with OLFM3, FN1,
NRCAM, GLDN and NFASC. Interacts (via N-terminus) with MYL2.
Interacts with SFRP1, FRZB, FZD7, FZD10, FZD1 and WIF1; regulates
Wnt signaling. Interacts with SNTA1; regulates muscle hypertrophy
(PubMed:22371502). Interacts with ERBB2 and ERBB3; acivates ERBB2-
ERBB3 signaling pathway (PubMed:23897819). Interacts with SNCG;
affects its secretion and its aggregation (PubMed:16392033).
{ECO:0000250|UniProtKB:Q99972, ECO:0000269|PubMed:12019210,
ECO:0000269|PubMed:16392033, ECO:0000269|PubMed:19188438,
ECO:0000269|PubMed:22371502, ECO:0000269|PubMed:23897819}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16392033}.
Golgi apparatus {ECO:0000269|PubMed:23629661}. Cytoplasmic vesicle
{ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space
{ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space,
extracellular matrix {ECO:0000250|UniProtKB:Q99972}. Secreted,
exosome {ECO:0000250|UniProtKB:Q99972}. Mitochondrion
{ECO:0000250|UniProtKB:Q99972}. Mitochondrion intermembrane space
{ECO:0000250|UniProtKB:Q99972}. Mitochondrion inner membrane
{ECO:0000250|UniProtKB:Q99972}. Mitochondrion outer membrane
{ECO:0000250|UniProtKB:Q99972}. Rough endoplasmic reticulum
{ECO:0000269|PubMed:23629661}. Cell projection
{ECO:0000250|UniProtKB:Q99972}. Cell projection, cilium
{ECO:0000250|UniProtKB:Q99972}. Note=Located preferentially in the
ciliary rootlet and basal body of the connecting cilium of
photoreceptor cells, and in the rough endoplasmic reticulum. It is
only imported to mitochondria in the trabecular meshwork.
Localizes to the Golgi apparatus in Schlemm's canal endothelial
cells. Appears in the extracellular space of trabecular meshwork
cells by an unconventional mechanism, likely associated with
exosome-like vesicles. Localizes in trabecular meshwork
extracellular matrix. {ECO:0000250|UniProtKB:Q99972}.
-!- SUBCELLULAR LOCATION: Myocilin, C-terminal fragment: Secreted
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Myocilin, N-terminal fragment: Endoplasmic
reticulum. Note=Remains retained in the endoplasmic reticulum.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in ciliary body, iris, retina,
trabecular network and sclera but not in lens or cornea. Also
expressed strongly in skeletal muscle and weakly in heart, brain,
testis, liver, kidney, thyroid and epididymis. No expression
detected in embryo. Expressed in sciatic nerve.
{ECO:0000269|PubMed:23897819, ECO:0000269|PubMed:9588210,
ECO:0000269|PubMed:9675094, ECO:0000269|PubMed:9680392}.
-!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q2PT31}.
-!- PTM: Undergoes a calcium-dependent proteolytic cleavage at Gln-212
by CAPN2 in the endoplasmic reticulum. The result is the
production of two fragments, one of 35 kDa containing the C-
terminal olfactomedin-like domain, and another of 20 kDa
containing the N-terminal leucine zipper-like domain (By
similarity). {ECO:0000250}.
-!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q99972}.
-!- POLYMORPHISM: Variant Ala-164 is found in strain BALB/cJ which has
a low intraocular pressure (PubMed:9588210, PubMed:9675094).
Variant Thr-164 is found in strains C3H/HeJ and C57BL/6J, two
strains which have a relatively high intraocular pressure
(PubMed:9588210, PubMed:9548973, PubMed:9680392).
{ECO:0000269|PubMed:9548973, ECO:0000269|PubMed:9588210,
ECO:0000269|PubMed:9675094, ECO:0000269|PubMed:9680392}.
-!- DISRUPTION PHENOTYPE: Mice lacking Myoc are viable, fertile and
show no significant differences in intraocular pressure or
clinical signs of glaucoma. They also show a reduction in cortical
bone thickness as well as trabecular volume.
{ECO:0000269|PubMed:23629661}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF041335; AAC32805.1; -; Genomic_DNA.
EMBL; AF041333; AAC32805.1; JOINED; Genomic_DNA.
EMBL; AF041334; AAC32805.1; JOINED; Genomic_DNA.
EMBL; AF049796; AAC14265.1; -; Genomic_DNA.
EMBL; AF049795; AAC14265.1; JOINED; Genomic_DNA.
EMBL; AF049794; AAC14265.1; JOINED; Genomic_DNA.
EMBL; AF039869; AAC40112.1; -; mRNA.
EMBL; AB013592; BAA32031.1; -; mRNA.
CCDS; CCDS15422.1; -.
PIR; JE0096; JE0096.
RefSeq; NP_034995.3; NM_010865.3.
UniGene; Mm.10694; -.
PDB; 5VR2; X-ray; 1.92 A; A/B/C/D=122-171.
PDBsum; 5VR2; -.
ProteinModelPortal; O70624; -.
SMR; O70624; -.
STRING; 10090.ENSMUSP00000028020; -.
PhosphoSitePlus; O70624; -.
PaxDb; O70624; -.
PRIDE; O70624; -.
Ensembl; ENSMUST00000028020; ENSMUSP00000028020; ENSMUSG00000026697.
GeneID; 17926; -.
KEGG; mmu:17926; -.
UCSC; uc007dgm.2; mouse.
CTD; 4653; -.
MGI; MGI:1202864; Myoc.
eggNOG; ENOG410INPA; Eukaryota.
eggNOG; ENOG410YBJJ; LUCA.
GeneTree; ENSGT00760000119005; -.
HOGENOM; HOG000059654; -.
HOVERGEN; HBG105662; -.
InParanoid; O70624; -.
OMA; RYKYSSM; -.
OrthoDB; EOG091G05HN; -.
PhylomeDB; O70624; -.
TreeFam; TF315964; -.
PRO; PR:O70624; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026697; -.
CleanEx; MM_MYOC; -.
ExpressionAtlas; O70624; baseline and differential.
Genevisible; O70624; MM.
GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISS:UniProtKB.
GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0033268; C:node of Ranvier; IDA:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0001968; F:fibronectin binding; ISO:MGI.
GO; GO:0005109; F:frizzled binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032027; F:myosin light chain binding; ISO:MGI.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0060348; P:bone development; IDA:UniProtKB.
GO; GO:0045162; P:clustering of voltage-gated sodium channels; IMP:UniProtKB.
GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; IDA:UniProtKB.
GO; GO:0022011; P:myelination in peripheral nervous system; IMP:UniProtKB.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISS:UniProtKB.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
GO; GO:0051497; P:negative regulation of stress fiber assembly; ISS:UniProtKB.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; ISS:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISS:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:0014734; P:skeletal muscle hypertrophy; IDA:UniProtKB.
InterPro; IPR031213; Myocilin.
InterPro; IPR003112; Olfac-like_dom.
PANTHER; PTHR23192:SF33; PTHR23192:SF33; 1.
Pfam; PF02191; OLF; 1.
SMART; SM00284; OLF; 1.
PROSITE; PS51132; OLF; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cell projection; Cilium; Coiled coil;
Complete proteome; Cytoplasmic vesicle; Disulfide bond;
Endoplasmic reticulum; Extracellular matrix; Glycoprotein;
Golgi apparatus; Lipoprotein; Membrane; Metal-binding; Mitochondrion;
Mitochondrion inner membrane; Mitochondrion outer membrane; Palmitate;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 490 Myocilin.
/FTId=PRO_0000020086.
CHAIN 19 212 Myocilin, N-terminal fragment.
{ECO:0000250}.
/FTId=PRO_0000428743.
CHAIN 213 490 Myocilin, C-terminal fragment.
{ECO:0000250}.
/FTId=PRO_0000428744.
DOMAIN 230 489 Olfactomedin-like. {ECO:0000255|PROSITE-
ProRule:PRU00446}.
COILED 69 170 {ECO:0000255}.
METAL 366 366 Calcium. {ECO:0000250|UniProtKB:Q99972}.
METAL 414 414 Calcium. {ECO:0000250|UniProtKB:Q99972}.
METAL 415 415 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q99972}.
METAL 463 463 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q99972}.
METAL 464 464 Calcium. {ECO:0000250|UniProtKB:Q99972}.
SITE 212 213 Cleavage; by CAPN2. {ECO:0000250}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 231 419 {ECO:0000250|UniProtKB:Q99972,
ECO:0000255|PROSITE-ProRule:PRU00446}.
VARIANT 164 164 T -> A (in strain: BALB/cJ).
{ECO:0000269|PubMed:9588210}.
HELIX 124 167 {ECO:0000244|PDB:5VR2}.
SEQUENCE 490 AA; 55314 MW; 2F090571E97B0425 CRC64;
MPALHLLFLA CLVWGMGART AQFRKANDRS GRCQYTFTVA SPNESSCPRE DQAMSAIQDL
QRDSSIQHAD LESTKARVRS LESLLHQMTL GRVTGTQEAQ EGLQGQLGAL RRERDQLETQ
TRDLEAAYNN LLRDKSALEE EKRQLEQENE DLARRLESSS EEVTRLRRGQ CPSTQYPSQD
MLPGSREVSQ WNLDTLAFQE LKSELTEVPA SQILKENPSG RPRSKEGDKG CGALVWVGEP
VTLRTAETIA GKYGVWMRDP KPTHPYTQES TWRIDTVGTE IRQVFEYSQI SQFEQGYPSK
VHVLPRALES TGAVVYAGSL YFQGAESRTV VRYELDTETV KAEKEIPGAG YHGHFPYAWG
GYTDIDLAVD ESGLWVIYST EEAKGAIVLS KLNPANLELE RTWETNIRKQ SVANAFVICG
ILYTVSSYSS AHATVNFAYD TKTGTSKTLT IPFTNRYKYS SMIDYNPLER KLFAWDNFNM
VTYDIKLLEM


Related products :

Catalog number Product name Quantity
EIAAB26098 Bos taurus,Bovine,MYOC,Myocilin,TIGR,Trabecular meshwork-induced glucocorticoid response protein
EIAAB26099 Mouse,Mus musculus,Myoc,Myocilin,Tigr,Trabecular meshwork-induced glucocorticoid response protein
EIAAB26100 Myoc,Myocilin,Rat,Rattus norvegicus,Tigr,Trabecular meshwork-induced glucocorticoid response protein
EIAAB26096 MYOC,Myocilin,Oryctolagus cuniculus,Rabbit,TIGR,Trabecular meshwork-induced glucocorticoid response protein
EIAAB26097 GLC1A,Homo sapiens,Human,MYOC,Myocilin,TIGR,Trabecular meshwork-induced glucocorticoid response protein
MYOD1 MYOC Gene myocilin, trabecular meshwork inducible glucocorticoid response
201-20-3602 MYOC{myocilin, trabecular meshwork inducible glucocorticoid response}rabbit.pAb 0.2ml
GWB-BB1B9C Myocilin Trabecular Meshwork Inducible Glucocorticoid Response Rabbit anti-Human Polyclonal (aa69-85) Antibody
CSB-EL015356DO Dog myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL015356RA Rat myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL015356CA Cat myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Cat, Sample Type serum, plasma 96T
CSB-EL015356HU Human myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL015356BO Bovine myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL015356MO Mouse myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL015356RB Rabbit myocilin, trabecular meshwork inducible glucocorticoid response (MYOC) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
CSB-PA015356GA01HU Rabbit anti-human myocilin, trabecular meshwork inducible glucocorticoid response polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA015356GA01HU Rabbit anti-human myocilin, trabecular meshwork inducible glucocorticoid response polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
orb60055 Hgh fragment 176-191 Hgh fragment 176-191 is a modified form of amino acids 176-191 at the C-terminal region of the human growth hormone (hGH). For research use only. 5 mg
13090-H08H MYOC _ Myocilin Protein (His Tag) 20
orb71386 Angiotensin 2 Receptor, AT2,Amino Terminal Fragment peptide This is Angiotensin 2 Receptor, AT2,Amino Terminal Fragment peptide. For research use only. 1 mg
C491 Myocilin lmg
49-806 Myocilin Antibody 0.05 mg
C491 Myocilin 500
C828 Human Myocilin 50
AP10161PU-N Myocilin (Mid_Region) 0.1 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 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