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Teneurin-3 (Ten-3) (Protein Odd Oz/ten-m homolog 3) (Tenascin-M3) (Ten-m3) (Teneurin transmembrane protein 3)

 TEN3_DANRE              Reviewed;        2694 AA.
Q9W7R4; E7EYS1;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
25-APR-2018, sequence version 2.
18-JUL-2018, entry version 109.
RecName: Full=Teneurin-3;
Short=Ten-3;
AltName: Full=Protein Odd Oz/ten-m homolog 3;
AltName: Full=Tenascin-M3;
Short=Ten-m3;
AltName: Full=Teneurin transmembrane protein 3;
Name=tenm3; Synonyms=odz3, tnm3;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
TISSUE=Embryo;
PubMed=10495292; DOI=10.1016/S0925-4773(99)00155-0;
Mieda M., Kikuchi Y., Hirate Y., Aoki M., Okamoto H.;
"Compartmentalized expression of zebrafish ten-m3 and ten-m4,
homologues of the Drosophila tenm /odd Oz gene, in the central nervous
system.";
Mech. Dev. 87:223-227(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[3]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=24183672; DOI=10.1016/j.celrep.2013.09.045;
Antinucci P., Nikolaou N., Meyer M.P., Hindges R.;
"Teneurin-3 specifies morphological and functional connectivity of
retinal ganglion cells in the vertebrate visual system.";
Cell Rep. 5:582-592(2013).
[4]
FUNCTION.
PubMed=27374343; DOI=10.1016/j.cub.2016.05.035;
Antinucci P., Suleyman O., Monfries C., Hindges R.;
"Neural Mechanisms Generating Orientation Selectivity in the Retina.";
Curr. Biol. 26:1802-1815(2016).
-!- FUNCTION: Involved in neural development by regulating the
establishment of proper connectivity within the nervous system
(PubMed:24183672, PubMed:27374343). Acts in both pre- and
postsynaptic neurons in the hippocampus to control the assembly of
a precise topographic projection: required in both CA1 and
subicular neurons for the precise targeting of proximal CA1 axons
to distal subiculum, probably by promoting homophilic cell
adhesion (By similarity). Required by retinal ganglion cells for
acquisition of their correct morphological and functional
connectivity, thereby playing a key role in the development of the
visual pathway (PubMed:24183672, PubMed:27374343).
{ECO:0000250|UniProtKB:Q9WTS6, ECO:0000269|PubMed:24183672,
ECO:0000269|PubMed:27374343}.
-!- SUBUNIT: Homodimer; disulfide-linked; to mediate homophilic cell
adhesion. {ECO:0000250|UniProtKB:Q9WTS6}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q9WTS6}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q9WTS6}. Cell projection, axon
{ECO:0000250|UniProtKB:Q9WTS6}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9W7R4-1; Sequence=Displayed;
Name=2;
IsoId=Q9W7R4-2; Sequence=VSP_059563;
-!- TISSUE SPECIFICITY: Expressed by retinal ganglion cells and their
presynaptic amacrine and postsynaptic tectal cell targets.
{ECO:0000269|PubMed:24183672}.
-!- DEVELOPMENTAL STAGE: Expressed at the notochord and the somite
around tailbud stage. At 14 hours post-fertilization (hpf),
expressed in the somites, notochord, and the brain. Found in the
rhombomere 3 (r3) and r5. Expressed in the optic vesicles and a
region covering the caudal diencephalon and the mesencephalon with
the strongest expression at its most anterior part. Mesodermal
expression is observed in both forming and formed somites. In
forming and newly formed somites, transcripts are distributed
evenly. In contrast, distribution in somites located on more
anterior trunk seems to be uneven, strongest in the ventral,
intermediate in the dorsal, and weakest in the medial parts. At 23
hpf, there is no expression in the medial parts of somites.
Expression in somites fades away by 36 hpf. At 20 hpf, additional
expression is detected in the pharyngeal arches.
{ECO:0000269|PubMed:10495292}.
-!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
retinal ganglion cell dendrite stratification defects within the
inner plexiform layer, as well as mistargeting of dendritic
processes into outer portions of the retina.
{ECO:0000269|PubMed:24183672}.
-!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
{ECO:0000305}.
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EMBL; AB026979; BAA81892.1; -; mRNA.
EMBL; BX005481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX322797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX324137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX324208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_571043.1; NM_130968.1.
UniGene; Dr.77510; -.
ProteinModelPortal; Q9W7R4; -.
STRING; 7955.ENSDARP00000109423; -.
PaxDb; Q9W7R4; -.
PRIDE; Q9W7R4; -.
Ensembl; ENSDART00000122700; ENSDARP00000109423; ENSDARG00000005479. [Q9W7R4-2]
Ensembl; ENSDART00000137676; ENSDARP00000113440; ENSDARG00000005479. [Q9W7R4-2]
GeneID; 30155; -.
KEGG; dre:30155; -.
CTD; 55714; -.
ZFIN; ZDB-GENE-990714-19; tenm3.
eggNOG; KOG4659; Eukaryota.
eggNOG; ENOG410XQQD; LUCA.
GeneTree; ENSGT00760000119131; -.
HOGENOM; HOG000231701; -.
HOVERGEN; HBG080306; -.
InParanoid; Q9W7R4; -.
OMA; EYSVGKH; -.
OrthoDB; EOG091G02H3; -.
PhylomeDB; Q9W7R4; -.
PRO; PR:Q9W7R4; -.
Proteomes; UP000000437; Chromosome 1.
Bgee; ENSDARG00000005479; -.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0070983; P:dendrite guidance; IMP:ZFIN.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:1903385; P:regulation of homophilic cell adhesion; ISS:UniProtKB.
GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:ZFIN.
GO; GO:0097264; P:self proteolysis; IEA:InterPro.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0007601; P:visual perception; IMP:ZFIN.
Gene3D; 2.120.10.30; -; 2.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR008969; CarboxyPept-like_regulatory.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR022385; Rhs_assc_core.
InterPro; IPR027689; Ten-2/3.
InterPro; IPR009471; Ten_N.
InterPro; IPR028916; Tox-GHH_dom.
InterPro; IPR006530; YD.
PANTHER; PTHR11219:SF64; PTHR11219:SF64; 2.
Pfam; PF06484; Ten_N; 2.
Pfam; PF15636; Tox-GHH; 1.
SMART; SM00181; EGF; 8.
SUPFAM; SSF49464; SSF49464; 1.
TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
TIGRFAMs; TIGR01643; YD_repeat_2x; 1.
PROSITE; PS00022; EGF_1; 8.
PROSITE; PS01186; EGF_2; 7.
PROSITE; PS50026; EGF_3; 4.
PROSITE; PS51361; TENEURIN_N; 1.
2: Evidence at transcript level;
Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
Complete proteome; Differentiation; Disulfide bond; EGF-like domain;
Glycoprotein; Membrane; Reference proteome; Repeat; Transmembrane;
Transmembrane helix.
CHAIN 1 2694 Teneurin-3.
/FTId=PRO_0000259507.
TOPO_DOM 1 312 Cytoplasmic. {ECO:0000255}.
TRANSMEM 313 333 Helical. {ECO:0000255}.
TOPO_DOM 334 2694 Extracellular. {ECO:0000255}.
DOMAIN 1 306 Teneurin N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00694}.
DOMAIN 508 539 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 540 570 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 572 604 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 605 636 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 638 671 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 672 703 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 704 733 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 734 768 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1166 1192 NHL 1.
REPEAT 1194 1238 NHL 2.
REPEAT 1264 1308 NHL 3.
REPEAT 1325 1365 NHL 4.
REPEAT 1452 1495 NHL 5.
REPEAT 1505 1524 YD 1.
REPEAT 1541 1561 YD 2.
REPEAT 1604 1623 YD 3.
REPEAT 1624 1646 YD 4.
REPEAT 1817 1836 YD 5.
REPEAT 1858 1876 YD 6.
REPEAT 1877 1897 YD 7.
REPEAT 1904 1921 YD 8.
REPEAT 1922 1943 YD 9.
REPEAT 1944 1961 YD 10.
REPEAT 1964 1984 YD 11.
REPEAT 1987 2007 YD 12.
REPEAT 2015 2034 YD 13.
REPEAT 2040 2057 YD 14.
REPEAT 2058 2084 YD 15.
REPEAT 2086 2099 YD 16.
REPEAT 2100 2123 YD 17.
REPEAT 2126 2146 YD 18.
REPEAT 2147 2167 YD 19.
REPEAT 2169 2189 YD 20.
REPEAT 2201 2221 YD 21.
REPEAT 2223 2243 YD 22.
REPEAT 2269 2310 YD 23.
CARBOHYD 374 374 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 664 664 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 854 854 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 877 877 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1048 1048 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1196 1196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1521 1521 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1538 1538 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1634 1634 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1671 1671 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1729 1729 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1814 1814 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1915 1915 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2118 2118 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2258 2258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2571 2571 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 512 522 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 516 527 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 529 538 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 547 558 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 560 569 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 576 587 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 581 592 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 594 603 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 608 619 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 613 624 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 626 635 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 646 659 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 661 670 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 675 685 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 679 690 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 692 701 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 706 716 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 710 721 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 723 732 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 737 747 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 741 756 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 758 767 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VAR_SEQ 1 104 Missing (in isoform 2).
/FTId=VSP_059563.
CONFLICT 781 781 N -> S (in Ref. 1; BAA81892).
{ECO:0000305}.
CONFLICT 813 813 I -> F (in Ref. 1; BAA81892).
{ECO:0000305}.
CONFLICT 892 892 R -> Q (in Ref. 1; BAA81892).
{ECO:0000305}.
CONFLICT 1210 1210 R -> G (in Ref. 1; BAA81892).
{ECO:0000305}.
CONFLICT 1880 1884 QDRLS -> HGKQI (in Ref. 1; BAA81892).
{ECO:0000305}.
CONFLICT 2520 2520 A -> V (in Ref. 1; BAA81892).
{ECO:0000305}.
SEQUENCE 2694 AA; 300669 MW; 65C41528CC4B4A10 CRC64;
MDVKERRPYC SLTKSRREKE RRYTGSSGDS EDCRVPTQKS YSSSETLKAF DHDSSRLLYG
GHVKEMVHRE ADEYSRQGQN FNLRQLGICE PATRRGLAFC AEMGMPSSLS SPSVTEHSHS
QPPSPNLHDN QSSILSNATT QAVQDSDSEE EYTAVLYRPV TQPAPSHSCN EQPSNQHQQG
QSTLPPVPPP HKQQPSVTAL NHNSLSSRRN VSPAPPAALP AELQTTPESV PLQDSWVLGS
NVPLESRHFL FKTGTGTTPL FSTATPGYTM ATGAVYSPPT RPLPRNTLSR SAFKFKKSSK
YCSWRCTALS AMAVSILLSV LLCYCIAMHL FGLNWQLQET EGYAFENGQV KSDSTATNAV
TALSTENKVY FQENNTIDTG EVDVGRRAVQ DVPPGTFWRT QLFIDQPQSL KFNISVQRGA
LVGVYGRKGL PPTHTQYDFV ELLDGSRLIA KEKRGLVEVE GAARKARSVN VHEAEFIRFL
DSGTWHLAFY NDGKNAEQVS YNTIIIDTLT ECPHNCHGNG DCRTGTCHCF PGFLGPDCSR
AACPVLCSGN GQYSRGRCLC YSGWKGTECD VPSNQCIDIH CSGHGICIMG TCACNTGYKG
DNCEEVDCLD PSCSSHGVCI HGECHCNPGW GGNNCEILKT MCPDQCSGHG TYQTESGTCT
CDTNWTGPDC SIEVCAVDCG SHGVCIGGSC RCEEGWTGSV CDLKACHPRC TEHGTCKDGK
CECHQGWTGE HCTVEGCPGL CNSNGRCTLD QNGWHCVCQP GWRGAGCDVA METLCADGKD
NEGDGLVDCM DPDCCLQSSC QTQPFCRGSP DPIDIISQNQ PASPQQAAQS FYQQISFLTG
PESTHVINGE NPFNRSLVSI IRGQVLTADG TPLIGVNVSF VHYPDHGYTI TRQDGMFDIL
ANGGASLTLS FERAPFLTQF RTVWIPWNVF YVMDTLVMKK EENDIPSCDL SGFIRPSPLI
VATPLSTFFR SSPENGPIIP ETQVLQEETA IPGSDLNLMY LSSRAAGYRP VLKVTMTQAT
IPFNLMKVHL MVAVVGRLFQ KWFPAEPNLS YTFIWDKTDA YNQRVYGLSE AVVSVGFEYE
SCLDLILWEK RTAILQGYEL DASNMGGWTL DKHHVLDVQN GILYKGNGEN VFVSQQPPVI
STIMGNGRRR SISCPSCNGQ ADGNKLLAPV ALACGSDGSL FVGDFNYIRR IFPSGNVTSV
MELSNNPAHR YYLATDPMTG QLYVSDTNSR RIFRPKALTG TKELLQNAEV VAGTGEQCLP
FDEARCGDGG KATEALLLGP KGIAVDKNGF IYFVDGTMIR KVDRNGIIST LLGSNDLTSA
RPLTCDNSMH IGQVRLEWPT DLAINPMDNS IYVLDNNVVL QITENRQVRI VAGRPMHCQV
PGIEYTMGKR AIQTTLEGAT AISLSYSGVL YIAETDEKKI NRIRQVSTDG EISHLAGAPS
DCDCKNDANC DCYQTGDGYA KDARLNAPSS LVVSPDGTLY VADLGNIRIR AIRHNRPPQG
SSGLFEVASP ASQELYVFDS NGTHQYTMSL VTGDYKYNFS YSNEDDVTAV TDSSGNTLRV
RRDPNRMPVR IVAPDNQVIW LTIGTNGGLK TLTAQGQELV LFTYHGNSGL LATKSIQIGW
TTFYDYDSEG RLTNVTFPTG VITSLIGEMD RALTVDIETS GRDDDVSITT NLSSIDSFYT
LVQDQLRNSY QVGYDNSMRV IYANGMDSHF QTEPHILAGA SNPTVARRNM TLPGENGQNL
VEWRFRKEQN RGKVVVFGRK LRVNGRNLLS VDYDRSLRTE KIYDDHRKFL LKIVYDASGH
PTLWVPSSKL MSVNLTYSST GQVTSLQRGP TTERVEYDSQ GRIVSRTFAD AKIWSYTYLD
KSMVLLLHSQ RQYIFDYDLQ DRLSAITMPS VARHTMQTIR SVGYYRNIYN PPESNASVTV
DYSEDGQLLR VAHLGTGRRV LYKYRRQNKL SEILYDSTRV SFTYDETAGV LKTVNLQSEG
FICSIRYRQI GPLVDRQIFR FSEDGMVNAR FDYTYDNSFR VTSMQGVINE TPLPIDLYQF
DDISGKVEQF GKFGVIYYDI NQIISTAVMT YTKHFDVHGR IKEIQYEIFR SLMYWITIQY
DNMGRVTKRE IKIGPFANTT KYGYEYDVDG QLQTVYLNEK MMWRYNYDLN GNLHLLNPGN
SARLTPLRYD LRDRITRLGD VQYRMDEDGF LRQRGAEIFE YNSKGLLVRV HSKASGWTIQ
YRYDGLGRRL ASRNSLGQHL QFFYADLNYP TRITHVYNHS SSEITSLYYD LQGHLFAMEI
SSGEEFYIAC DNTGTPLAVF SSNGLLLKQV QYTAYGEIYF DSNPDFQLVI GFHGGLYDPL
TRLLHFGERD YDIQAGRWTT PDISTWTRVG KDPAPFNLYM FRNNNPISKI HEVKEYVTDV
NIWLVTFGFH LHNVIPGFPI PKFDLTQPSL EMRKSQLWDD LPSISGVQQE VMRQAKAFLS
FERMPEIQLS RRRSSREKPW LWFATVKSLI GKGVMLAITS KGQVATNALN IANEDCIKVA
TVLNNAFYLE DLHFTVEGRD THYFIKTSLP ESDLGALRLT SGRKSLENGV NVTVSQSTTV
VNGRTRRFAD VELQYGALAL HVRYGMTLDE EKARVLEQAR QRALSSAWAR EQQRVRDGEE
GVRLWTEGEK RQLLSSGKVL GYDGYYVLSV EQYPELADSA NNVQFLRQSE IGKR


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EIAAB41947 Homo sapiens,Human,KIAA1302,ODZ4,Protein Odd Oz_ten-m homolog 4,Ten-4,Tenascin-M4,Teneurin-4,Ten-m4,TNM4
EIAAB41941 Homo sapiens,Human,KIAA1127,ODZ2,Protein Odd Oz_ten-m homolog 2,Ten-2,Tenascin-M2,Teneurin-2,Ten-m2,TNM2
EIAAB41946 Doc4,Downstream of CHOP4,Kiaa1302,Mouse,Mus musculus,Odz4,Protein Odd Oz_ten-m homolog 4,Ten-4,Tenascin-M4,Teneurin-4,Ten-m4,Tnm4
EIAAB41935 Chicken,Gallus gallus,ODZ1,Protein Odd Oz_ten-m homolog 1,Ten-1,Tenascin-M1,Teneurin-1,Ten-m1,TNM1
EIAAB41942 Chicken,Gallus gallus,Neurestin,ODZ2,Protein Odd Oz_ten-m homolog 2,Ten-2,Tenascin-M2,Teneurin-2,Ten-m2,TNM2
E0319h Rat ELISA Kit FOR Teneurin-2 96T
IPO7_MOUSE Rat ELISA Kit FOR Teneurin-2 96T
ANKH1_HUMAN Rat ELISA Kit FOR Teneurin-2 96T
'H00010178-Q01-25 Teneurin-1 _ ODZ1 antigen 25
E1926m Mouse ELISA Kit FOR Teneurin-4 96T
'H00010178-Q01-10 Teneurin-1 _ ODZ1 antigen 10
H5087 Teneurin-2 (ODZ2), Rat, ELISA Kit 96T
E1225c Human ELISA Kit FOR Teneurin-1 96T
TEN3_MOUSE Mouse ELISA Kit FOR Teneurin-3 96T
CSB-EL016281RA Rat Teneurin-2(ODZ2) ELISA kit 96T
E11921h Human ELISA Kit FOR Teneurin-3 96T
Y214162 ODZ3 _ Teneurin-3 Antibody 200ul
'AP09621PU-N Teneurin-3 antibody Ab host: Goat 0.1 mg
AP09621PU-N Teneurin-3 Goat antibody Ab Aff - Purified 0.1 mg


 

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