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Tenascin (TN) (Cytotactin) (GMEM) (GP 150-225) (Glioma-associated-extracellular matrix antigen) (Hexabrachion) (JI) (Myotendinous antigen) (Neuronectin) (Tenascin-C) (TN-C)

 TENA_HUMAN              Reviewed;        2201 AA.
P24821; C9IYT7; C9J575; C9J6D9; C9J848; Q14583; Q15567; Q5T7S3;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
15-DEC-2009, sequence version 3.
22-NOV-2017, entry version 205.
RecName: Full=Tenascin;
Short=TN;
AltName: Full=Cytotactin;
AltName: Full=GMEM;
AltName: Full=GP 150-225;
AltName: Full=Glioma-associated-extracellular matrix antigen;
AltName: Full=Hexabrachion;
AltName: Full=JI;
AltName: Full=Myotendinous antigen;
AltName: Full=Neuronectin;
AltName: Full=Tenascin-C;
Short=TN-C;
Flags: Precursor;
Name=TNC; Synonyms=HXB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-539; LEU-1677
AND GLN-2008.
PubMed=1704365;
Nies D.E., Hemesath T.J., Kim J.H., Gulcher J.R., Stefansson K.;
"The complete cDNA sequence of human hexabrachion (Tenascin). A
multidomain protein containing unique epidermal growth factor
repeats.";
J. Biol. Chem. 266:2818-2823(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 5), PROTEIN SEQUENCE
OF 23-32, AND VARIANTS ARG-680 AND GLN-2008.
TISSUE=Fetal brain, and Melanoma;
PubMed=1707164; DOI=10.1093/nar/19.3.525;
Siri A., Carnemolla B., Saginati M., Leprini A., Casari G.,
Baralle F., Zardi L.;
"Human tenascin: primary structure, pre-mRNA splicing patterns and
localization of the epitopes recognized by two monoclonal
antibodies.";
Nucleic Acids Res. 19:525-531(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-539; LEU-1677
AND GLN-2008.
PubMed=1719530; DOI=10.1073/pnas.88.21.9438;
Gulcher J.R., Nies D.E., Alexakos M.J., Ravikant N.A., Sturgill M.E.,
Marton L.S., Stefansson K.;
"Structure of the human hexabrachion (tenascin) gene.";
Proc. Natl. Acad. Sci. U.S.A. 88:9438-9442(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LEU-1677 AND
GLN-2008.
PubMed=7531707; DOI=10.1074/jbc.270.7.3429;
Gherzi R., Carnemolla B., Siri A., Ponassi M., Balza E., Zardi L.;
"Human tenascin gene. Structure of the 5'-region, identification, and
characterization of the transcription regulatory sequences.";
J. Biol. Chem. 270:3429-3434(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 46-125 (ISOFORMS 1/2/3/4/5/6).
TISSUE=Fetal cartilage;
PubMed=7524681; DOI=10.1016/0167-4781(94)90220-8;
Glumoff V., Savontaus M., Vehanen J., Vuorio E.;
"Analysis of aggrecan and tenascin gene expression in mouse skeletal
tissues by northern and in situ hybridization using species specific
cDNA probes.";
Biochim. Biophys. Acta 1219:613-622(1994).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 431-2055 (ISOFORMS 1 AND 6), AND
VARIANTS ARG-539; LEU-1677 AND GLN-2008.
TISSUE=Glioblastoma;
PubMed=2466295; DOI=10.1073/pnas.86.5.1588;
Gulcher J.R., Nies D.E., Marton L.S., Stefansson K.;
"An alternatively spliced region of the human hexabrachion contains a
repeat of potential N-glycosylation sites.";
Proc. Natl. Acad. Sci. U.S.A. 86:1588-1592(1989).
[8]
INTERACTION WITH CSPG4.
PubMed=8824254; DOI=10.1074/jbc.271.42.26110;
Burg M.A., Tillet E., Timpl R., Stallcup W.B.;
"Binding of the NG2 proteoglycan to type VI collagen and other
extracellular matrix molecules.";
J. Biol. Chem. 271:26110-26116(1996).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1809.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-1079; ASN-1093;
ASN-1261; ASN-1301; ASN-1485 AND ASN-2162.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1018; ASN-1034; ASN-1184;
ASN-1275; ASN-1301; ASN-1366 AND ASN-1485.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[12]
FUNCTION.
PubMed=19884327; DOI=10.1096/fj.09-140491;
Martina E., Degen M., Rueegg C., Merlo A., Lino M.M.,
Chiquet-Ehrismann R., Brellier F.;
"Tenascin-W is a specific marker of glioma-associated blood vessels
and stimulates angiogenesis in vitro.";
FASEB J. 24:778-787(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-70; SER-72 AND
THR-905, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
PHOSPHORYLATION AT SER-72.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[16]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF FIBRONECTIN TYPE-III 3.
PubMed=1279805; DOI=10.1126/science.1279805;
Leahy D.J., Hendrickson W.A., Aukhil I., Erickson H.P.;
"Structure of a fibronectin type III domain from tenascin phased by
MAD analysis of the selenomethionyl protein.";
Science 258:987-991(1992).
[17]
VARIANTS DFNA56 MET-1773 AND SER-1796.
PubMed=23936043; DOI=10.1371/journal.pone.0069549;
Zhao Y., Zhao F., Zong L., Zhang P., Guan L., Zhang J., Wang D.,
Wang J., Chai W., Lan L., Li Q., Han B., Yang L., Jin X., Yang W.,
Hu X., Wang X., Li N., Li Y., Petit C., Wang J., Wang H.Y., Wang Q.;
"Exome sequencing and linkage analysis identified tenascin-C (TNC) as
a novel causative gene in nonsyndromic hearing loss.";
PLoS ONE 8:E69549-E69549(2013).
-!- FUNCTION: Extracellular matrix protein implicated in guidance of
migrating neurons as well as axons during development, synaptic
plasticity as well as neuronal regeneration. Promotes neurite
outgrowth from cortical neurons grown on a monolayer of
astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1,
alpha-V/beta-3 and alpha-V/beta-6. In tumors, stimulates
angiogenesis by elongation, migration and sprouting of endothelial
cells (PubMed:19884327). {ECO:0000269|PubMed:19884327}.
-!- SUBUNIT: Homohexamer; disulfide-linked. A homotrimer may be formed
in the triple coiled-coil region and may be stabilized by
disulfide rings at both ends. Two of such half-hexabrachions may
be disulfide linked within the central globule. Interacts with
CSPG4. {ECO:0000269|PubMed:8824254}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Isoforms are produced in a tissue- and time-specific
manner during development.;
Name=1;
IsoId=P24821-1; Sequence=Displayed;
Name=2; Synonyms=HT-5;
IsoId=P24821-2; Sequence=VSP_001412, VSP_001413;
Name=3;
IsoId=P24821-3; Sequence=VSP_001412;
Name=4; Synonyms=HT-33;
IsoId=P24821-4; Sequence=VSP_001413;
Name=5;
IsoId=P24821-5; Sequence=VSP_001414;
Name=6; Synonyms=P31;
IsoId=P24821-6; Sequence=VSP_001415;
-!- INDUCTION: By TGFB1.
-!- DISEASE: Deafness, autosomal dominant, 56 (DFNA56) [MIM:615629]: A
form of non-syndromic sensorineural hearing loss. Sensorineural
deafness results from damage to the neural receptors of the inner
ear, the nerve pathways to the brain, or the area of the brain
that receives sound information. DFNA56 is characterized by
progressive hearing impairment with post-lingual onset.
{ECO:0000269|PubMed:23936043}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the tenascin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TNCID42597ch9q33.html";
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EMBL; M55618; AAA88083.1; -; mRNA.
EMBL; X56160; CAA39628.1; -; mRNA.
EMBL; X78565; CAA55309.1; -; mRNA.
EMBL; AL162425; CAI15110.1; -; Genomic_DNA.
EMBL; X80280; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M24630; AAA52703.1; -; mRNA.
CCDS; CCDS6811.1; -. [P24821-1]
PIR; I38337; A32160.
RefSeq; NP_002151.2; NM_002160.3. [P24821-1]
RefSeq; XP_005252029.1; XM_005251972.3. [P24821-4]
RefSeq; XP_005252031.1; XM_005251974.3. [P24821-5]
RefSeq; XP_005252032.1; XM_005251975.3. [P24821-6]
RefSeq; XP_011516931.1; XM_011518629.2. [P24821-2]
UniGene; Hs.143250; -.
UniGene; Hs.684865; -.
UniGene; Hs.734766; -.
PDB; 1TEN; X-ray; 1.80 A; A=802-891.
PDB; 2RB8; X-ray; 1.45 A; A=802-893.
PDB; 2RBL; X-ray; 2.10 A; A/B/M=802-893.
PDBsum; 1TEN; -.
PDBsum; 2RB8; -.
PDBsum; 2RBL; -.
ProteinModelPortal; P24821; -.
SMR; P24821; -.
BioGrid; 109602; 3.
CORUM; P24821; -.
STRING; 9606.ENSP00000265131; -.
ChEMBL; CHEMBL3712856; -.
iPTMnet; P24821; -.
PhosphoSitePlus; P24821; -.
BioMuta; TNC; -.
DMDM; 281185495; -.
EPD; P24821; -.
MaxQB; P24821; -.
PaxDb; P24821; -.
PeptideAtlas; P24821; -.
PRIDE; P24821; -.
Ensembl; ENST00000350763; ENSP00000265131; ENSG00000041982. [P24821-1]
Ensembl; ENST00000537320; ENSP00000443478; ENSG00000041982. [P24821-6]
GeneID; 3371; -.
KEGG; hsa:3371; -.
UCSC; uc004bjj.6; human. [P24821-1]
CTD; 3371; -.
DisGeNET; 3371; -.
EuPathDB; HostDB:ENSG00000041982.15; -.
GeneCards; TNC; -.
HGNC; HGNC:5318; TNC.
HPA; CAB004592; -.
HPA; HPA004823; -.
MalaCards; TNC; -.
MIM; 187380; gene.
MIM; 615629; phenotype.
neXtProt; NX_P24821; -.
OpenTargets; ENSG00000041982; -.
Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
PharmGKB; PA35103; -.
eggNOG; KOG1225; Eukaryota.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
GeneTree; ENSGT00830000128240; -.
HOVERGEN; HBG008949; -.
InParanoid; P24821; -.
KO; K06252; -.
OMA; HYTAKIQ; -.
OrthoDB; EOG091G03M1; -.
PhylomeDB; P24821; -.
TreeFam; TF329915; -.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P24821; -.
ChiTaRS; TNC; human.
EvolutionaryTrace; P24821; -.
GeneWiki; Tenascin_C; -.
GenomeRNAi; 3371; -.
PRO; PR:P24821; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000041982; -.
CleanEx; HS_TNC; -.
ExpressionAtlas; P24821; baseline and differential.
Genevisible; P24821; HS.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005614; C:interstitial matrix; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045545; F:syndecan binding; IDA:MGI.
GO; GO:0060447; P:bud outgrowth involved in lung branching; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071799; P:cellular response to prostaglandin D stimulus; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0060739; P:mesenchymal-epithelial cell signaling involved in prostate gland development; IEA:Ensembl.
GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl.
GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
GO; GO:0014012; P:peripheral nervous system axon regeneration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0071774; P:response to fibroblast growth factor; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0009611; P:response to wounding; IEP:BHF-UCL.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
CDD; cd00063; FN3; 15.
CDD; cd00087; FReD; 1.
Gene3D; 2.60.40.10; -; 14.
Gene3D; 3.90.215.10; -; 1.
Gene3D; 4.10.530.10; -; 1.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR013111; EGF_extracell.
InterPro; IPR036056; Fibrinogen-like_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR033078; TNC.
PANTHER; PTHR19143:SF38; PTHR19143:SF38; 9.
Pfam; PF07974; EGF_2; 6.
Pfam; PF00147; Fibrinogen_C; 1.
Pfam; PF00041; fn3; 15.
SMART; SM00181; EGF; 14.
SMART; SM00186; FBG; 1.
SMART; SM00060; FN3; 15.
SUPFAM; SSF49265; SSF49265; 12.
SUPFAM; SSF56496; SSF56496; 1.
PROSITE; PS00022; EGF_1; 15.
PROSITE; PS01186; EGF_2; 15.
PROSITE; PS50026; EGF_3; 5.
PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PROSITE; PS50853; FN3; 15.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Coiled coil;
Complete proteome; Deafness; Direct protein sequencing;
Disease mutation; Disulfide bond; EGF-like domain;
Extracellular matrix; Glycoprotein; Non-syndromic deafness;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted;
Signal.
SIGNAL 1 22 {ECO:0000269|PubMed:1707164}.
CHAIN 23 2201 Tenascin.
/FTId=PRO_0000007741.
DOMAIN 174 186 EGF-like 1; incomplete.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 186 217 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 217 248 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 248 280 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 280 311 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 311 342 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 342 373 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 373 404 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 404 435 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 435 466 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 466 497 EGF-like 11. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 497 528 EGF-like 12. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 528 559 EGF-like 13. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 559 590 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 590 621 EGF-like 15. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 625 715 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 716 804 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 805 894 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 895 990 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 991 1075 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1076 1165 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1167 1256 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1258 1350 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1351 1439 Fibronectin type-III 9.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1440 1531 Fibronectin type-III 10.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1533 1621 Fibronectin type-III 11.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1622 1711 Fibronectin type-III 12.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1712 1801 Fibronectin type-III 13.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1802 1888 Fibronectin type-III 14.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1889 1977 Fibronectin type-III 15.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1975 2190 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
COILED 118 145 {ECO:0000255}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 72 72 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
MOD_RES 905 905 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 788 788 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1018 1018 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1034 1034 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1079 1079 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
CARBOHYD 1093 1093 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
CARBOHYD 1119 1119 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1184 1184 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1210 1210 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1261 1261 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
CARBOHYD 1275 1275 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1301 1301 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:19159218}.
CARBOHYD 1366 1366 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1392 1392 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1445 1445 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1455 1455 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1485 1485 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:19159218}.
CARBOHYD 1534 1534 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1809 1809 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 2162 2162 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
DISULFID 190 200 {ECO:0000250}.
DISULFID 194 205 {ECO:0000250}.
DISULFID 207 216 {ECO:0000250}.
DISULFID 221 231 {ECO:0000250}.
DISULFID 225 236 {ECO:0000250}.
DISULFID 238 247 {ECO:0000250}.
DISULFID 252 263 {ECO:0000250}.
DISULFID 256 268 {ECO:0000250}.
DISULFID 270 279 {ECO:0000250}.
DISULFID 284 294 {ECO:0000250}.
DISULFID 288 299 {ECO:0000250}.
DISULFID 301 310 {ECO:0000250}.
DISULFID 315 325 {ECO:0000250}.
DISULFID 319 330 {ECO:0000250}.
DISULFID 332 341 {ECO:0000250}.
DISULFID 346 356 {ECO:0000250}.
DISULFID 350 361 {ECO:0000250}.
DISULFID 363 372 {ECO:0000250}.
DISULFID 377 387 {ECO:0000250}.
DISULFID 381 392 {ECO:0000250}.
DISULFID 394 403 {ECO:0000250}.
DISULFID 408 418 {ECO:0000250}.
DISULFID 412 423 {ECO:0000250}.
DISULFID 425 434 {ECO:0000250}.
DISULFID 439 449 {ECO:0000250}.
DISULFID 443 454 {ECO:0000250}.
DISULFID 456 465 {ECO:0000250}.
DISULFID 470 480 {ECO:0000250}.
DISULFID 474 485 {ECO:0000250}.
DISULFID 487 496 {ECO:0000250}.
DISULFID 501 511 {ECO:0000250}.
DISULFID 505 516 {ECO:0000250}.
DISULFID 518 527 {ECO:0000250}.
DISULFID 532 542 {ECO:0000250}.
DISULFID 536 547 {ECO:0000250}.
DISULFID 549 558 {ECO:0000250}.
DISULFID 563 573 {ECO:0000250}.
DISULFID 567 578 {ECO:0000250}.
DISULFID 580 589 {ECO:0000250}.
DISULFID 594 604 {ECO:0000250}.
DISULFID 598 609 {ECO:0000250}.
DISULFID 611 620 {ECO:0000250}.
VAR_SEQ 1072 1708 Missing (in isoform 6).
{ECO:0000303|PubMed:2466295}.
/FTId=VSP_001415.
VAR_SEQ 1072 1617 Missing (in isoform 5).
{ECO:0000303|PubMed:1707164}.
/FTId=VSP_001414.
VAR_SEQ 1072 1435 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:1707164}.
/FTId=VSP_001412.
VAR_SEQ 1527 1617 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:1707164}.
/FTId=VSP_001413.
VARIANT 213 213 G -> S (in dbSNP:rs7020958).
/FTId=VAR_055778.
VARIANT 539 539 Q -> R (in dbSNP:rs1757095).
{ECO:0000269|PubMed:1704365,
ECO:0000269|PubMed:1719530,
ECO:0000269|PubMed:2466295}.
/FTId=VAR_024266.
VARIANT 605 605 V -> I (in dbSNP:rs3827816).
/FTId=VAR_024267.
VARIANT 680 680 Q -> R (in dbSNP:rs1061494).
{ECO:0000269|PubMed:1707164}.
/FTId=VAR_024268.
VARIANT 850 850 D -> H (in dbSNP:rs3748169).
/FTId=VAR_055779.
VARIANT 1677 1677 I -> L (in dbSNP:rs2104772).
{ECO:0000269|PubMed:1704365,
ECO:0000269|PubMed:1719530,
ECO:0000269|PubMed:2466295,
ECO:0000269|PubMed:7531707}.
/FTId=VAR_060738.
VARIANT 1773 1773 V -> M (in DFNA56; dbSNP:rs137933052).
{ECO:0000269|PubMed:23936043}.
/FTId=VAR_070984.
VARIANT 1781 1781 A -> T (in dbSNP:rs2274750).
/FTId=VAR_020169.
VARIANT 1796 1796 T -> S (in DFNA56; dbSNP:rs431905513).
{ECO:0000269|PubMed:23936043}.
/FTId=VAR_070985.
VARIANT 2008 2008 E -> Q (in dbSNP:rs13321).
{ECO:0000269|PubMed:1704365,
ECO:0000269|PubMed:1707164,
ECO:0000269|PubMed:1719530,
ECO:0000269|PubMed:2466295,
ECO:0000269|PubMed:7531707}.
/FTId=VAR_014665.
CONFLICT 244 244 Missing (in Ref. 2; CAA39628).
{ECO:0000305}.
CONFLICT 370 370 V -> L (in Ref. 1; no nucleotide entry,
3; AAA88083 and 4; CAA55309).
{ECO:0000305}.
CONFLICT 1066 1066 R -> H (in Ref. 1; no nucleotide entry,
3; AAA88083 and 7; AAA52703).
{ECO:0000305}.
CONFLICT 1600 1608 SGFTQGHQT -> LWLHPRASN (in Ref. 1; no
nucleotide entry, 3; AAA88083 and 7;
AAA52703). {ECO:0000305}.
CONFLICT 2054 2054 F -> FLH (in Ref. 1; no nucleotide entry
and 3; AAA88083). {ECO:0000305}.
CONFLICT 2055 2055 W -> L (in Ref. 7; AAA52703).
{ECO:0000305}.
CONFLICT 2140 2143 YKGA -> TRG (in Ref. 2; CAA39628).
{ECO:0000305}.
STRAND 807 813 {ECO:0000244|PDB:2RB8}.
STRAND 819 824 {ECO:0000244|PDB:2RB8}.
HELIX 827 829 {ECO:0000244|PDB:2RBL}.
STRAND 831 839 {ECO:0000244|PDB:2RB8}.
STRAND 842 844 {ECO:0000244|PDB:2RBL}.
STRAND 847 852 {ECO:0000244|PDB:2RB8}.
STRAND 857 860 {ECO:0000244|PDB:2RB8}.
STRAND 868 877 {ECO:0000244|PDB:2RB8}.
STRAND 885 890 {ECO:0000244|PDB:2RB8}.
SEQUENCE 2201 AA; 240853 MW; B2BEF378AA6F1D85 CRC64;
MGAMTQLLAG VFLAFLALAT EGGVLKKVIR HKRQSGVNAT LPEENQPVVF NHVYNIKLPV
GSQCSVDLES ASGEKDLAPP SEPSESFQEH TVDGENQIVF THRINIPRRA CGCAAAPDVK
ELLSRLEELE NLVSSLREQC TAGAGCCLQP ATGRLDTRPF CSGRGNFSTE GCGCVCEPGW
KGPNCSEPEC PGNCHLRGRC IDGQCICDDG FTGEDCSQLA CPSDCNDQGK CVNGVCICFE
GYAGADCSRE ICPVPCSEEH GTCVDGLCVC HDGFAGDDCN KPLCLNNCYN RGRCVENECV
CDEGFTGEDC SELICPNDCF DRGRCINGTC YCEEGFTGED CGKPTCPHAC HTQGRCEEGQ
CVCDEGFAGV DCSEKRCPAD CHNRGRCVDG RCECDDGFTG ADCGELKCPN GCSGHGRCVN
GQCVCDEGYT GEDCSQLRCP NDCHSRGRCV EGKCVCEQGF KGYDCSDMSC PNDCHQHGRC
VNGMCVCDDG YTGEDCRDRQ CPRDCSNRGL CVDGQCVCED GFTGPDCAEL SCPNDCHGQG
RCVNGQCVCH EGFMGKDCKE QRCPSDCHGQ GRCVDGQCIC HEGFTGLDCG QHSCPSDCNN
LGQCVSGRCI CNEGYSGEDC SEVSPPKDLV VTEVTEETVN LAWDNEMRVT EYLVVYTPTH
EGGLEMQFRV PGDQTSTIIQ ELEPGVEYFI RVFAILENKK SIPVSARVAT YLPAPEGLKF
KSIKETSVEV EWDPLDIAFE TWEIIFRNMN KEDEGEITKS LRRPETSYRQ TGLAPGQEYE
ISLHIVKNNT RGPGLKRVTT TRLDAPSQIE VKDVTDTTAL ITWFKPLAEI DGIELTYGIK
DVPGDRTTID LTEDENQYSI GNLKPDTEYE VSLISRRGDM SSNPAKETFT TGLDAPRNLR
RVSQTDNSIT LEWRNGKAAI DSYRIKYAPI SGGDHAEVDV PKSQQATTKT TLTGLRPGTE
YGIGVSAVKE DKESNPATIN AATELDTPKD LQVSETAETS LTLLWKTPLA KFDRYRLNYS
LPTGQWVGVQ LPRNTTSYVL RGLEPGQEYN VLLTAEKGRH KSKPARVKAS TEQAPELENL
TVTEVGWDGL RLNWTAADQA YEHFIIQVQE ANKVEAARNL TVPGSLRAVD IPGLKAATPY
TVSIYGVIQG YRTPVLSAEA STGETPNLGE VVVAEVGWDA LKLNWTAPEG AYEYFFIQVQ
EADTVEAAQN LTVPGGLRST DLPGLKAATH YTITIRGVTQ DFSTTPLSVE VLTEEVPDMG
NLTVTEVSWD ALRLNWTTPD GTYDQFTIQV QEADQVEEAH NLTVPGSLRS MEIPGLRAGT
PYTVTLHGEV RGHSTRPLAV EVVTEDLPQL GDLAVSEVGW DGLRLNWTAA DNAYEHFVIQ
VQEVNKVEAA QNLTLPGSLR AVDIPGLEAA TPYRVSIYGV IRGYRTPVLS AEASTAKEPE
IGNLNVSDIT PESFNLSWMA TDGIFETFTI EIIDSNRLLE TVEYNISGAE RTAHISGLPP
STDFIVYLSG LAPSIRTKTI SATATTEALP LLENLTISDI NPYGFTVSWM ASENAFDSFL
VTVVDSGKLL DPQEFTLSGT QRKLELRGLI TGIGYEVMVS GFTQGHQTKP LRAEIVTEAE
PEVDNLLVSD ATPDGFRLSW TADEGVFDNF VLKIRDTKKQ SEPLEITLLA PERTRDITGL
REATEYEIEL YGISKGRRSQ TVSAIATTAM GSPKEVIFSD ITENSATVSW RAPTAQVESF
RITYVPITGG TPSMVTVDGT KTQTRLVKLI PGVEYLVSII AMKGFEESEP VSGSFTTALD
GPSGLVTANI TDSEALARWQ PAIATVDSYV ISYTGEKVPE ITRTVSGNTV EYALTDLEPA
TEYTLRIFAE KGPQKSSTIT AKFTTDLDSP RDLTATEVQS ETALLTWRPP RASVTGYLLV
YESVDGTVKE VIVGPDTTSY SLADLSPSTH YTAKIQALNG PLRSNMIQTI FTTIGLLYPF
PKDCSQAMLN GDTTSGLYTI YLNGDKAEAL EVFCDMTSDG GGWIVFLRRK NGRENFYQNW
KAYAAGFGDR REEFWLGLDN LNKITAQGQY ELRVDLRDHG ETAFAVYDKF SVGDAKTRYK
LKVEGYSGTA GDSMAYHNGR SFSTFDKDTD SAITNCALSY KGAFWYRNCH RVNLMGRYGD
NNHSQGVNWF HWKGHEHSIQ FAEMKLRPSN FRNLEGRRKR A


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