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

Protein wntless (Evenness interrupted) (Sprinter)

 WLS_DROME               Reviewed;         594 AA.
Q95ST2; Q9VTG4;
19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
27-SEP-2017, entry version 116.
RecName: Full=Protein wntless {ECO:0000303|PubMed:16678095, ECO:0000303|PubMed:18160348, ECO:0000303|PubMed:18193032, ECO:0000303|PubMed:18193037};
AltName: Full=Evenness interrupted {ECO:0000303|PubMed:16678096, ECO:0000303|PubMed:19837038};
AltName: Full=Sprinter {ECO:0000303|PubMed:17108000};
Flags: Precursor;
Name=wls {ECO:0000303|PubMed:16678095, ECO:0000303|PubMed:18160348,
ECO:0000303|PubMed:18193032, ECO:0000303|PubMed:18193037};
Synonyms=evi {ECO:0000303|PubMed:16678096,
ECO:0000303|PubMed:19837038}, srt {ECO:0000303|PubMed:17108000};
ORFNames=CG6210;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:ABD58936.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DEVELOPMENTAL STAGE,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-250.
PubMed=16678095; DOI=10.1016/j.cell.2006.02.049;
Baenziger C., Soldini D., Schuett C., Zipperlen P., Hausmann G.,
Basler K.;
"Wntless, a conserved membrane protein dedicated to the secretion of
Wnt proteins from signaling cells.";
Cell 125:509-522(2006).
[2] {ECO:0000312|EMBL:AAF50085.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000305, ECO:0000312|EMBL:AAF50085.2}
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000305, ECO:0000312|EMBL:AAL28148.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley {ECO:0000312|EMBL:AAL28148.1};
TISSUE=Head {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=16678096; DOI=10.1016/j.cell.2006.04.009;
Bartscherer K., Pelte N., Ingelfinger D., Boutros M.;
"Secretion of Wnt ligands requires Evi, a conserved transmembrane
protein.";
Cell 125:523-533(2006).
[6] {ECO:0000305}
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=17108000; DOI=10.1242/dev.02674;
Goodman R.M., Thombre S., Firtina Z., Gray D., Betts D., Roebuck J.,
Spana E.P., Selva E.M.;
"Sprinter: a novel transmembrane protein required for Wg secretion and
signaling.";
Development 133:4901-4911(2006).
[7] {ECO:0000305}
INTERACTION WITH VPS35, AND SUBCELLULAR LOCATION.
PubMed=18160348; DOI=10.1016/j.devcel.2007.12.003;
Belenkaya T.Y., Wu Y., Tang X., Zhou B., Cheng L., Sharma Y.V.,
Yan D., Selva E.M., Lin X.;
"The retromer complex influences Wnt secretion by recycling wntless
from endosomes to the trans-Golgi network.";
Dev. Cell 14:120-131(2008).
[8] {ECO:0000305}
FUNCTION, INTERACTION WITH WG, AND SUBCELLULAR LOCATION.
PubMed=18193037; DOI=10.1038/ncb1678;
Franch-Marro X., Wendler F., Guidato S., Griffith J., Baena-Lopez A.,
Itasaki N., Maurice M.M., Vincent J.P.;
"Wingless secretion requires endosome-to-Golgi retrieval of
Wntless/Evi/Sprinter by the retromer complex.";
Nat. Cell Biol. 10:170-177(2008).
[9] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18193032; DOI=10.1038/ncb1687;
Port F., Kuster M., Herr P., Furger E., Banziger C., Hausmann G.,
Basler K.;
"Wingless secretion promotes and requires retromer-dependent cycling
of Wntless.";
Nat. Cell Biol. 10:178-185(2008).
[10] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19837038; DOI=10.1016/j.cell.2009.07.051;
Korkut C., Ataman B., Ramachandran P., Ashley J., Barria R.,
Gherbesi N., Budnik V.;
"Trans-synaptic transmission of vesicular Wnt signals through
Evi/Wntless.";
Cell 139:393-404(2009).
-!- FUNCTION: A segment polarity gene required for wingless (wg)-
dependent patterning processes, acting in both wg-sending cells
and wg-target cells. In non-neuronal cells wls directs wg
secretion. The wls traffic loop encompasses the Golgi, the cell
surface, an endocytic compartment and a retrograde route leading
back to the Golgi, and involves clathrin-mediated endocytosis and
the retromer complex (a conserved protein complex consisting of
Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ),
the wg signal moves across the synapse via the release of wls-
containing exosome-like vesicles. Postsynaptic wls is required for
the trafficking of fz2 through the fz2-interacting protein Grip.
{ECO:0000269|PubMed:16678095, ECO:0000269|PubMed:16678096,
ECO:0000269|PubMed:17108000, ECO:0000269|PubMed:18193032,
ECO:0000269|PubMed:18193037, ECO:0000269|PubMed:19837038}.
-!- SUBUNIT: Interacts with wg; in the Golgi. Interacts with Vps35, a
component of the retromer complex; wls stability is regulated by
Vps35. {ECO:0000269|PubMed:18160348, ECO:0000269|PubMed:18193037}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell
membrane {ECO:0000269|PubMed:16678096,
ECO:0000269|PubMed:18160348, ECO:0000269|PubMed:18193032,
ECO:0000269|PubMed:18193037, ECO:0000269|PubMed:19837038}; Multi-
pass membrane protein {ECO:0000269|PubMed:16678096,
ECO:0000269|PubMed:18160348, ECO:0000269|PubMed:18193032,
ECO:0000269|PubMed:18193037, ECO:0000269|PubMed:19837038}. Cell
junction, synapse, postsynaptic cell membrane
{ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
ECO:0000269|PubMed:19837038}; Multi-pass membrane protein
{ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
ECO:0000269|PubMed:19837038}. Cell membrane
{ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
ECO:0000269|PubMed:19837038}; Multi-pass membrane protein
{ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
ECO:0000269|PubMed:19837038}. Endosome membrane
{ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
ECO:0000269|PubMed:19837038}; Multi-pass membrane protein
{ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
ECO:0000269|PubMed:19837038}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
ECO:0000269|PubMed:19837038}; Multi-pass membrane protein
{ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
ECO:0000269|PubMed:19837038}. Golgi apparatus membrane
{ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
ECO:0000269|PubMed:19837038}; Multi-pass membrane protein
{ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18160348,
ECO:0000269|PubMed:18193032, ECO:0000269|PubMed:18193037,
ECO:0000269|PubMed:19837038}. Note=In non-neuronal cells, wls
binds to wg in the Golgi and accompanies it to the plasma membrane
where the two proteins dissociate. Wg is secreted and wls is then
internalized and returns to the Golgi apparatus in a retromer-
dependent manner. Wls and wg colocalize in the Golgi apparatus in
wg-producing cells, and reduced expression is seen in non-
producing cells. Endoplasmic recticulum expression is unchanged in
wg-producing versus non-producing cells. In neuronal cells, wls is
localized both pre- and postsynaptically and is transferred trans-
synaptically from the pre- to the postsynaptic compartment.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A {ECO:0000269|PubMed:18193032};
IsoId=Q95ST2-1; Sequence=Displayed;
Name=B {ECO:0000269|PubMed:10731132};
IsoId=Q95ST2-2; Sequence=VSP_053188;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Ubiquitously expressed in the wing imaginal
disk, increased expression is observed in a stripe at the dorso-
ventral boundary and other regions of the wing disk that express
wg. Also expresses in the leg imaginal disk. During larval
development, expression is seen in both motorneurons and muscle.
{ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:18193032,
ECO:0000269|PubMed:19837038}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
throughout development. {ECO:0000269|PubMed:16678095,
ECO:0000269|PubMed:17108000}.
-!- DISRUPTION PHENOTYPE: Segment polarity phenotype (cuticles are
smaller and lack the alternate naked regions) and wing margin
defects (a reduced number of posterior wing-margin bristles and
the even bristles distribution is interrupted). Heterozygotes die
as pharate adults with appendage malformations, such as lack of
arista and antennal segments, rudimentary legs and wing-to-notum
transformations. {ECO:0000269|PubMed:16678095,
ECO:0000269|PubMed:16678096, ECO:0000269|PubMed:17108000}.
-!- SIMILARITY: Belongs to the wntless family. {ECO:0000255}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DQ305404; ABD58936.1; -; mRNA.
EMBL; AE014296; AAF50085.2; -; Genomic_DNA.
EMBL; AE014296; AAN11905.1; -; Genomic_DNA.
EMBL; AY060600; AAL28148.1; -; mRNA.
RefSeq; NP_648445.1; NM_140188.4. [Q95ST2-1]
RefSeq; NP_729681.1; NM_168450.3. [Q95ST2-2]
UniGene; Dm.7728; -.
BioGrid; 64631; 11.
STRING; 7227.FBpp0075947; -.
TCDB; 8.A.56.1.1; the wntless protein (wls) family.
PaxDb; Q95ST2; -.
PRIDE; Q95ST2; -.
EnsemblMetazoa; FBtr0076218; FBpp0075947; FBgn0036141. [Q95ST2-1]
EnsemblMetazoa; FBtr0076219; FBpp0075948; FBgn0036141. [Q95ST2-2]
GeneID; 39259; -.
KEGG; dme:Dmel_CG6210; -.
UCSC; CG6210-RA; d. melanogaster. [Q95ST2-1]
UCSC; CG6210-RB; d. melanogaster.
CTD; 79971; -.
FlyBase; FBgn0036141; wls.
eggNOG; ENOG410IG2W; Eukaryota.
eggNOG; ENOG410XQ06; LUCA.
GeneTree; ENSGT00390000005897; -.
InParanoid; Q95ST2; -.
OMA; LDYSRWQ; -.
OrthoDB; EOG091G06QO; -.
PhylomeDB; Q95ST2; -.
Reactome; R-DME-3238698; WNT ligand biogenesis and trafficking.
GenomeRNAi; 39259; -.
PRO; PR:Q95ST2; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0036141; -.
Genevisible; Q95ST2; DM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005769; C:early endosome; IDA:FlyBase.
GO; GO:0012505; C:endomembrane system; IDA:FlyBase.
GO; GO:0070062; C:extracellular exosome; IDA:FlyBase.
GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:UniProtKB.
GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0031302; C:intrinsic component of endosome membrane; IDA:UniProtKB.
GO; GO:0031228; C:intrinsic component of Golgi membrane; IDA:UniProtKB.
GO; GO:0005771; C:multivesicular body; IDA:FlyBase.
GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
GO; GO:0035017; P:cuticle pattern formation; IMP:FlyBase.
GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:FlyBase.
GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:UniProtKB.
GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
GO; GO:0061357; P:positive regulation of Wnt protein secretion; IMP:ParkinsonsUK-UCL.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0033157; P:regulation of intracellular protein transport; IMP:UniProtKB.
GO; GO:0007367; P:segment polarity determination; IMP:UniProtKB.
GO; GO:0061355; P:Wnt protein secretion; IMP:FlyBase.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR009551; Wntless.
PANTHER; PTHR13449; PTHR13449; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Complete proteome;
Developmental protein; Endoplasmic reticulum; Endosome; Glycoprotein;
Golgi apparatus; Membrane; Postsynaptic cell membrane;
Reference proteome; Segmentation polarity protein; Signal; Synapse;
Transmembrane; Transmembrane helix; Wnt signaling pathway.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 594 Protein wntless. {ECO:0000255}.
/FTId=PRO_0000390664.
TOPO_DOM 36 239 Extracellular. {ECO:0000255}.
TRANSMEM 240 260 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 261 270 Cytoplasmic. {ECO:0000255}.
TRANSMEM 271 291 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 292 311 Extracellular. {ECO:0000255}.
TRANSMEM 312 332 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 333 344 Cytoplasmic. {ECO:0000255}.
TRANSMEM 345 365 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 366 390 Extracellular. {ECO:0000255}.
TRANSMEM 391 411 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 412 473 Cytoplasmic. {ECO:0000255}.
TRANSMEM 474 494 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 495 514 Extracellular. {ECO:0000255}.
TRANSMEM 515 535 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 536 594 Cytoplasmic. {ECO:0000255}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 437 468 Missing (in isoform B).
{ECO:0000303|PubMed:10731132}.
/FTId=VSP_053188.
MUTAGEN 250 250 P->S: In wls-2; Homozygous lethal.
{ECO:0000269|PubMed:16678095}.
SEQUENCE 594 AA; 67890 MW; D8401B3C5D41E069 CRC64;
MSGTILENLS GRKLSILVAT LLLCQVLCFL LGGLYAPLPA GHVTVLGSLC REDHARQNDT
SFLLYSRGAG ACIPVTREEV EQDSTKMANE LVHVFQMPLP RDLRDLDYSR WQQNLIGVLQ
VEFGYDSSSE LREPPRELQL TIDMRLAYRN KGDPDNGWKL YAHGVEHRYL DCVTSHVGPT
ETLYSCDMIP LFELGALHHS FYLLNLRFPL DTPSQMNLQF GHMHDLTLTA IHQNGGFTQI
WLLLKTMLFP FVVGIMIWFW RRVHLLQRSP ALLEYMLIYL GAALTFLNLP LEYLSLVYEM
PYMLLLSDIR QGIFYAMLLT FWLVFAGEHM LIQDAPNKST IRSRYWKHLS AVVVGCISLF
VFDICERGVQ LRNPFYSIWT TPLGAKVAMT FIVLAGVSAA IYFLFLCYMI WKVFRNIGDK
RTSLPSMSQA RRLHYEVPLD QKVEDWAGIV YFYTKAFFFQ LHKANESKGL IYRFKFLMLA
TLVCAALTVA GFIMGQMAEG QWDWNDNVAI QPTSAFLTGV YGMWNIYIFA LLILYAPSHK
QWPTMHHSDE TTQSNENIVA SAASEEIEFS HLPSDSNPSE ISSLTSFTRK VAFD


Related products :

Catalog number Product name Quantity
EIAAB46376 C1orf139,EVI,GPR177,Homo sapiens,Human,Integral membrane protein GPR177,Protein evenness interrupted homolog,Protein wntless homolog,Putative NF-kappa-B-activating protein 373,UNQ85_PRO18667,WLS
EIAAB46379 EVI,Gpr177,Integral membrane protein GPR177,Protein evenness interrupted homolog,Protein wntless homolog,Rat,Rattus norvegicus,Wls
EIAAB46377 EVI,Gpr177,Integral membrane protein GPR177,Mouse,Mus musculus,Protein evenness interrupted homolog,Protein wntless homolog,Wls
ZBT41_MOUSE Mouse ELISA Kit FOR Protein wntless homolog 96T
E1908r Chicken ELISA Kit FOR Protein wntless homolog 96T
CB062_MOUSE Mouse ELISA Kit FOR Protein wntless homolog 96T
E0015r Mouse ELISA Kit FOR Protein wntless homolog 96T
CSB-EL009786HU Human Protein wntless homolog(GPR177) ELISA kit 96T
WLS_RAT ELISA Kit FOR Protein wntless homolog; organism: Rat; gene name: Wls 96T
G4474 Protein wntless homolog (GPR177), Human, ELISA Kit 96T
CSB-EL009786HU Human Protein wntless homolog(GPR177) ELISA kit SpeciesHuman 96T
WLS_HUMAN ELISA Kit FOR Protein wntless homolog; organism: Human; gene name: WLS 96T
WLS_MOUSE ELISA Kit FOR Protein wntless homolog; organism: Mouse; gene name: Wls 96T
28-111 Inhibition of NFkappa-B activity by the hepatitis C virus core protein might be related to its physical interaction with and interrupted nuclear localization of IKKbeta. Increased nuclear factor-kappa 0.1 mg
EIAAB46378 Chicken,Gallus gallus,GPR177,Integral membrane protein GPR177,Protein wntless homolog,RCJMB04_5c7,WLS
RPR-402 Recombinant Human Wntless 2
WLS WLS Gene wntless homolog (Drosophila)
pro-1402 Recombinant Human Wntless 2
pro-1402 Recombinant Human Wntless 10
pro-1402 Recombinant Human Wntless 1mg
E3705h Human Wntless Homolog ELISA Kit 96T
PAH-G1-2 Protein Arrays containing 234 Human Protein for simultaneous detection of Protein function, including Protein-protein interaction, Protein modification, antibody specificity, auto-antibody and small m 1 glass slide with 2 sub-arrays
29-844 RNF40 contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the 0.1 mg
29-850 The protein contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions.The protein encoded by this 0.1 mg
EIAAB10617 DCN1-like protein 1,DCUN1 domain-containing protein 1,Dcun1d1,Dcun1l1,Defective in cullin neddylation protein 1-like protein 1,Mouse,Mus musculus,Rp42,Tes3,Testis-specific protein 3


 

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