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Interleukin-6 receptor subunit beta (IL-6 receptor subunit beta) (IL-6R subunit beta) (IL-6R-beta) (IL-6RB) (CDw130) (Interleukin-6 signal transducer) (Membrane glycoprotein 130) (gp130) (Oncostatin-M receptor subunit alpha) (CD antigen CD130)

 IL6RB_HUMAN             Reviewed;         918 AA.
P40189; A0N0L4; Q5FC04; Q9UQ41;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
27-SEP-2017, entry version 205.
RecName: Full=Interleukin-6 receptor subunit beta;
Short=IL-6 receptor subunit beta;
Short=IL-6R subunit beta;
Short=IL-6R-beta;
Short=IL-6RB;
AltName: Full=CDw130;
AltName: Full=Interleukin-6 signal transducer;
AltName: Full=Membrane glycoprotein 130;
Short=gp130;
AltName: Full=Oncostatin-M receptor subunit alpha;
AltName: CD_antigen=CD130;
Flags: Precursor;
Name=IL6ST;
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), FUNCTION, TISSUE SPECIFICITY,
AND VARIANT VAL-8.
TISSUE=Myeloma, and Placenta;
PubMed=2261637; DOI=10.1016/0092-8674(90)90411-7;
Hibi M., Murakami M., Saito M., Hirano T., Taga T., Kishimoto T.;
"Molecular cloning and expression of an IL-6 signal transducer,
gp130.";
Cell 63:1149-1157(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-8.
TISSUE=Synovium;
PubMed=10880057; DOI=10.1172/JCI7479;
Tanaka M., Kishimura M., Ozaki S., Osakada F., Hashimoto H., Okubo M.,
Murakami M., Nakao K.;
"Cloning of novel soluble gp130 and detection of its neutralizing
autoantibodies in rheumatoid arthritis.";
J. Clin. Invest. 106:137-144(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Hayashi A., Sameshima E., Tabata Y., Iida K., Mitsuyama M., Kanai S.,
Furuya T., Saito T.;
"IL6ST mRNA, nirs splice variant 4.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION AT
ASN-43; ASN-83; ASN-131; ASN-157; ASN-227; ASN-379; ASN-383; ASN-553
AND ASN-564.
PubMed=11098061; DOI=10.1074/jbc.M009979200;
Moritz R.L., Hall N.E., Connolly L.M., Simpson R.J.;
"Determination of the disulfide structure and N-glycosylation sites of
the extracellular domain of the human signal transducer gp130.";
J. Biol. Chem. 276:8244-8253(2001).
[8]
SUBUNIT, AND INDUCTION.
PubMed=8999038; DOI=10.1074/jbc.271.51.32635;
Mosley B., De Imus C., Friend D., Boiani N., Thoma B., Park L.S.,
Cosman D.;
"Dual oncostatin M (OSM) receptors. Cloning and characterization of an
alternative signaling subunit conferring OSM-specific receptor
activation.";
J. Biol. Chem. 271:32635-32643(1996).
[9]
INTERACTION WITH HCK.
PubMed=9406996;
Hallek M., Neumann C., Schaffer M., Danhauser-Riedl S.,
von Bubnoff N., de Vos G., Druker B.J., Yasukawa K., Griffin J.D.,
Emmerich B.;
"Signal transduction of interleukin-6 involves tyrosine
phosphorylation of multiple cytosolic proteins and activation of Src-
family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines.";
Exp. Hematol. 25:1367-1377(1997).
[10]
PHOSPHORYLATION AT SER-782, MUTAGENESIS OF SER-782, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=10811661; DOI=10.1074/jbc.M907658199;
Gibson R.M., Schiemann W.P., Prichard L.B., Reno J.M., Ericsson L.H.,
Nathanson N.M.;
"Phosphorylation of human gp130 at Ser-782 adjacent to the di-leucine
internalization motif. Effects on expression and signaling.";
J. Biol. Chem. 275:22574-22582(2000).
[11]
INTERACTION WITH HHV-8 PROTEIN VIL6.
PubMed=11238858; DOI=10.1128/JVI.75.7.3325-3334.2001;
Li H., Wang H., Nicholas J.;
"Detection of direct binding of human herpesvirus 8-encoded
interleukin-6 (vIL-6) to both gp130 and IL-6 receptor (IL-6R) and
identification of amino acid residues of vIL-6 important for IL-6R-
dependent and -independent signaling.";
J. Virol. 75:3325-3334(2001).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-379 AND ASN-383.
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227 AND ASN-390.
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).
[17]
GLYCOSYLATION AT ASN-390.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=19915009; DOI=10.1074/jbc.M109.075952;
Waetzig G.H., Chalaris A., Rosenstiel P., Suthaus J., Holland C.,
Karl N., Valles Uriarte L., Till A., Scheller J., Grotzinger J.,
Schreiber S., Rose-John S., Seegert D.;
"N-linked glycosylation is essential for the stability but not the
signaling function of the interleukin-6 signal transducer glycoprotein
130.";
J. Biol. Chem. 285:1781-1789(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
FUNCTION, AND MUTAGENESIS OF CYS-172; 186-TYR--TYR-190; VAL-189;
TYR-190; ASP-215 AND VAL-252.
PubMed=23294003; DOI=10.1042/BJ20121660;
Schutt A., Zacharias M., Schneider N., Horn S., Grotzinger J.,
Rose-John S., Schmidt-Arras D.;
"gp130 activation is regulated by D2-D3 interdomain connectivity.";
Biochem. J. 450:487-496(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667 AND SER-839, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661 AND SER-667, 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).
[23]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 122-325.
PubMed=9501088; DOI=10.1093/emboj/17.6.1665;
Bravo J., Staunton D., Heath J.K., Jones E.Y.;
"Crystal structure of a cytokine-binding region of gp130.";
EMBO J. 17:1665-1674(1998).
[24]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-325 IN COMPLEX WITH HERPES
VIRUS IL6, SUBUNIT, AND GLYCOSYLATION.
PubMed=11251120; DOI=10.1126/science.1058308;
Chow D.-C., He X.-L., Snow A.L., Rose-John S., Garcia K.C.;
"Structure of an extracellular gp130 cytokine receptor signaling
complex.";
Science 291:2150-2155(2001).
[25]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 123-323 IN COMPLEX WITH LIF.
PubMed=14527405; DOI=10.1016/S1097-2765(03)00365-4;
Boulanger M.J., Bankovich A.J., Kortemme T., Baker D., Garcia K.C.;
"Convergent mechanisms for recognition of divergent cytokines by the
shared signaling receptor gp130.";
Mol. Cell 12:577-589(2003).
[26]
X-RAY CRYSTALLOGRAPHY (3.65 ANGSTROMS) OF 23-321 IN COMPLEX WITH IL6
AND IL6R, AND SUBUNIT.
PubMed=12829785; DOI=10.1126/science.1083901;
Boulanger M.J., Chow D.-C., Brevnova E.E., Garcia K.C.;
"Hexameric structure and assembly of the interleukin-6/IL-6 alpha-
receptor/gp130 complex.";
Science 300:2101-2104(2003).
[27]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-612, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-43; ASN-83; ASN-227; ASN-383 AND ASN-553.
PubMed=20489211; DOI=10.1074/jbc.C110.129502;
Xu Y., Kershaw N.J., Luo C.S., Soo P., Pocock M.J., Czabotar P.E.,
Hilton D.J., Nicola N.A., Garrett T.P., Zhang J.G.;
"Crystal structure of the entire ectodomain of gp130: insights into
the molecular assembly of the tall cytokine receptor complexes.";
J. Biol. Chem. 285:21214-21218(2010).
[28]
VARIANT [LARGE SCALE ANALYSIS] ILE-415.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[29]
VARIANT GLY-200.
PubMed=25242236; DOI=10.1016/j.cancergen.2014.07.003;
Sun L., Sui L., Cong X., Ma K., Ma X., Huang Y., Fan C., Fu X., Ma K.;
"Low incidence of IL6ST (gp130) mutations in exon 6 in lung cancer of
a Chinese cohort.";
Cancer Genet. 207:291-298(2014).
[30]
VARIANT ARG-148, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=24629561; DOI=10.1016/j.metabol.2014.02.005;
Wonnerth A., Katsaros K.M., Krychtiuk K.A., Speidl W.S., Kaun C.,
Thaler K., Huber K., Wojta J., Maurer G., Seljeflot I., Arnesen H.,
Weiss T.W.;
"Glycoprotein 130 polymorphism predicts soluble glycoprotein 130
levels.";
Metabolism 63:647-653(2014).
-!- FUNCTION: Signal-transducing molecule. The receptor systems for
IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST for
initiating signal transmission. Binding of IL6 to IL6R induces
IL6ST homodimerization and formation of a high-affinity receptor
complex, which activates Janus kinases (PubMed:2261637). That
causes phosphorylation of IL6ST tyrosine residues which in turn
activates STAT3 (PubMed:19915009, PubMed:23294003). Mediates
signals which regulate immune response, hematopoiesis, pain
control and bone metabolism (By similarity). Has a role in
embryonic development (By similarity). Does not bind IL6
(PubMed:2261637). Essential for survival of motor and sensory
neurons and for differentiation of astrocytes (By similarity).
Required for expression of TRPA1 in nociceptive neurons (By
similarity). Required for the maintenance of PTH1R expression in
the osteoblast lineage and for the stimulation of PTH-induced
osteoblast differentiation (By similarity). Required for normal
trabecular bone mass and cortical bone composition (By
similarity). {ECO:0000250|UniProtKB:Q00560,
ECO:0000269|PubMed:19915009, ECO:0000269|PubMed:2261637,
ECO:0000269|PubMed:23294003}.
-!- SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R
and IL6ST (PubMed:12829785). Forms heterodimers composed of LIFR
and IL6ST (type I OSM receptor) which are activated by LIF and OSM
(PubMed:8999038). Also forms heterodimers composed of OSMR and
IL6ST (type II receptor) which are activated by OSM but not by LIF
(PubMed:8999038). Homodimer. The homodimer binds two molecules of
herpes virus 8/HHV-8 protein vIL-6 (PubMed:11238858,
PubMed:11251120). Interacts with HCK (PubMed:9406996). Interacts
with INPP5D/SHIP1 (By similarity). {ECO:0000250|UniProtKB:Q00560,
ECO:0000269|PubMed:11238858, ECO:0000269|PubMed:11251120,
ECO:0000269|PubMed:12829785, ECO:0000269|PubMed:14527405,
ECO:0000269|PubMed:8999038, ECO:0000269|PubMed:9406996}.
-!- INTERACTION:
P26441:CNTF; NbExp=10; IntAct=EBI-1030834, EBI-1050897;
Q2HRC7:K2 (xeno); NbExp=2; IntAct=EBI-1030834, EBI-9007403;
Q9Y2W7:KCNIP3; NbExp=4; IntAct=EBI-1030834, EBI-751501;
P15018:LIF; NbExp=2; IntAct=EBI-1030834, EBI-1037189;
P42227:Stat3 (xeno); NbExp=4; IntAct=EBI-1030834, EBI-602878;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:19915009}; Single-pass type I membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted
{ECO:0000269|PubMed:24629561}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P40189-1; Sequence=Displayed;
Name=2; Synonyms=GP130-RAPS;
IsoId=P40189-2; Sequence=VSP_001684, VSP_001685;
Name=3;
IsoId=P40189-3; Sequence=VSP_043716;
-!- TISSUE SPECIFICITY: Found in all the tissues and cell lines
examined (PubMed:2261637). Expression not restricted to IL6
responsive cells (PubMed:2261637). Expressed in blood serum (at
protein level) (PubMed:24629561). {ECO:0000269|PubMed:2261637,
ECO:0000269|PubMed:24629561}.
-!- INDUCTION: LIF and OSM activate the type I OSM receptor while only
OSM can activate the type II OSM receptor.
{ECO:0000269|PubMed:8999038}.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- PTM: Phosphorylation of Ser-782 down-regulates cell surface
expression. {ECO:0000269|PubMed:10811661}.
-!- PTM: Heavily N-glycosylated (PubMed:11098061, PubMed:16335952,
PubMed:19159218, PubMed:19139490, PubMed:11251120). Glycosylation
is required for protein stability and localization in plasma
membrane but not for ligand binding (PubMed:19915009).
{ECO:0000269|PubMed:11098061, ECO:0000269|PubMed:11251120,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19915009}.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
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EMBL; M57230; AAA59155.1; -; mRNA.
EMBL; AB015706; BAA78112.1; -; mRNA.
EMBL; AB102802; BAD89393.1; -; mRNA.
EMBL; EF064722; ABK41905.1; -; Genomic_DNA.
EMBL; AC008914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC016596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471123; EAW54936.1; -; Genomic_DNA.
CCDS; CCDS3971.1; -. [P40189-1]
CCDS; CCDS47209.1; -. [P40189-2]
CCDS; CCDS54856.1; -. [P40189-3]
PIR; A36337; A36337.
RefSeq; NP_001177910.1; NM_001190981.1. [P40189-3]
RefSeq; NP_002175.2; NM_002184.3. [P40189-1]
RefSeq; NP_786943.1; NM_175767.2. [P40189-2]
UniGene; Hs.532082; -.
UniGene; Hs.706627; -.
PDB; 1BJ8; NMR; -; A=219-325.
PDB; 1BQU; X-ray; 2.00 A; A/B=122-333.
PDB; 1I1R; X-ray; 2.40 A; A=23-325.
PDB; 1N2Q; Model; -; A/B=23-324.
PDB; 1P9M; X-ray; 3.65 A; A=23-321.
PDB; 1PVH; X-ray; 2.50 A; A/C=123-323.
PDB; 3L5H; X-ray; 3.60 A; A=24-612.
PDB; 3L5I; X-ray; 1.90 A; A=323-612.
PDB; 3L5J; X-ray; 3.04 A; A/B=323-610.
PDBsum; 1BJ8; -.
PDBsum; 1BQU; -.
PDBsum; 1I1R; -.
PDBsum; 1N2Q; -.
PDBsum; 1P9M; -.
PDBsum; 1PVH; -.
PDBsum; 3L5H; -.
PDBsum; 3L5I; -.
PDBsum; 3L5J; -.
ProteinModelPortal; P40189; -.
SMR; P40189; -.
BioGrid; 109786; 31.
CORUM; P40189; -.
DIP; DIP-95N; -.
IntAct; P40189; 20.
MINT; MINT-130473; -.
STRING; 9606.ENSP00000338799; -.
ChEMBL; CHEMBL3124734; -.
GuidetoPHARMACOLOGY; 2317; -.
iPTMnet; P40189; -.
PhosphoSitePlus; P40189; -.
SwissPalm; P40189; -.
UniCarbKB; P40189; -.
BioMuta; IL6ST; -.
DMDM; 215273999; -.
EPD; P40189; -.
MaxQB; P40189; -.
PaxDb; P40189; -.
PeptideAtlas; P40189; -.
PRIDE; P40189; -.
DNASU; 3572; -.
Ensembl; ENST00000336909; ENSP00000338799; ENSG00000134352. [P40189-1]
Ensembl; ENST00000381287; ENSP00000370687; ENSG00000134352. [P40189-2]
Ensembl; ENST00000381294; ENSP00000370694; ENSG00000134352. [P40189-3]
Ensembl; ENST00000381298; ENSP00000370698; ENSG00000134352. [P40189-1]
Ensembl; ENST00000502326; ENSP00000462158; ENSG00000134352. [P40189-1]
Ensembl; ENST00000522633; ENSP00000435399; ENSG00000134352. [P40189-2]
GeneID; 3572; -.
KEGG; hsa:3572; -.
UCSC; uc003jqq.4; human. [P40189-1]
CTD; 3572; -.
DisGeNET; 3572; -.
EuPathDB; HostDB:ENSG00000134352.19; -.
GeneCards; IL6ST; -.
HGNC; HGNC:6021; IL6ST.
HPA; CAB025784; -.
HPA; HPA010558; -.
MIM; 600694; gene.
neXtProt; NX_P40189; -.
OpenTargets; ENSG00000134352; -.
PharmGKB; PA29837; -.
eggNOG; ENOG410IF1N; Eukaryota.
eggNOG; ENOG410YNQ4; LUCA.
GeneTree; ENSGT00550000074436; -.
HOGENOM; HOG000015771; -.
HOVERGEN; HBG052119; -.
InParanoid; P40189; -.
KO; K05060; -.
OMA; FCFNKRD; -.
OrthoDB; EOG091G01XM; -.
PhylomeDB; P40189; -.
TreeFam; TF338122; -.
Reactome; R-HSA-110056; MAPK3 (ERK1) activation.
Reactome; R-HSA-112411; MAPK1 (ERK2) activation.
Reactome; R-HSA-447115; Interleukin-12 family signaling.
Reactome; R-HSA-6783589; Interleukin-6 family signaling.
Reactome; R-HSA-6788467; IL-6-type cytokine receptor ligand interactions.
Reactome; R-HSA-8984722; Interleukin-35 Signalling.
SignaLink; P40189; -.
SIGNOR; P40189; -.
ChiTaRS; IL6ST; human.
EvolutionaryTrace; P40189; -.
GeneWiki; Glycoprotein_130; -.
GenomeRNAi; 3572; -.
PRO; PR:P40189; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000134352; -.
CleanEx; HS_IL6ST; -.
ExpressionAtlas; P40189; baseline and differential.
Genevisible; P40189; HS.
GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; IDA:BHF-UCL.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005896; C:interleukin-6 receptor complex; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005900; C:oncostatin-M receptor complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004897; F:ciliary neurotrophic factor receptor activity; IDA:BHF-UCL.
GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; IPI:BHF-UCL.
GO; GO:0019838; F:growth factor binding; IPI:BHF-UCL.
GO; GO:0019970; F:interleukin-11 binding; IEA:Ensembl.
GO; GO:0004921; F:interleukin-11 receptor activity; IEA:Ensembl.
GO; GO:0045509; F:interleukin-27 receptor activity; IC:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; TAS:BHF-UCL.
GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0005977; P:glycogen metabolic process; IEA:Ensembl.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0070106; P:interleukin-27-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0048861; P:leukemia inhibitory factor signaling pathway; IDA:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:BHF-UCL.
GO; GO:0070104; P:negative regulation of interleukin-6-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0002675; P:positive regulation of acute inflammatory response; IC:BHF-UCL.
GO; GO:0002821; P:positive regulation of adaptive immune response; IC:BHF-UCL.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; IEA:Ensembl.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; TAS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:BHF-UCL.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; TAS:BHF-UCL.
GO; GO:0008593; P:regulation of Notch signaling pathway; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IDA:BHF-UCL.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR003961; FN3_dom.
InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR010457; IgC2-like_lig-bd.
InterPro; IPR015321; TypeI_recpt_CBD.
Pfam; PF00041; fn3; 2.
Pfam; PF09240; IL6Ra-bind; 1.
Pfam; PF06328; Lep_receptor_Ig; 1.
SMART; SM00060; FN3; 5.
SUPFAM; SSF49265; SSF49265; 5.
PROSITE; PS50853; FN3; 4.
PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host-virus interaction; Immunoglobulin domain; Membrane;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 22
CHAIN 23 918 Interleukin-6 receptor subunit beta.
/FTId=PRO_0000010899.
TOPO_DOM 23 619 Extracellular. {ECO:0000255}.
TRANSMEM 620 641 Helical. {ECO:0000255}.
TOPO_DOM 642 918 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 120 Ig-like C2-type.
DOMAIN 125 216 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 224 324 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 329 424 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 426 517 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 518 613 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 310 314 WSXWS motif.
MOTIF 651 659 Box 1 motif.
COMPBIAS 725 755 Ser-rich.
MOD_RES 661 661 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 667 667 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 782 782 Phosphoserine.
{ECO:0000269|PubMed:10811661}.
MOD_RES 789 789 Phosphoserine.
{ECO:0000250|UniProtKB:Q00560}.
MOD_RES 829 829 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 839 839 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211}.
CARBOHYD 131 131 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11098061}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11098061}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:20489211}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:16335952}.
CARBOHYD 383 383 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:20489211}.
CARBOHYD 390 390 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 553 553 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211}.
CARBOHYD 564 564 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11098061}.
DISULFID 28 54 {ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211}.
DISULFID 48 103 {ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211}.
DISULFID 134 144 {ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211}.
DISULFID 172 182 {ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211}.
DISULFID 458 466 {ECO:0000269|PubMed:11098061,
ECO:0000269|PubMed:20489211}.
VAR_SEQ 325 329 RPSKA -> NIASF (in isoform 2).
{ECO:0000303|PubMed:10880057}.
/FTId=VSP_001684.
VAR_SEQ 330 918 Missing (in isoform 2).
{ECO:0000303|PubMed:10880057}.
/FTId=VSP_001685.
VAR_SEQ 423 483 Missing (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_043716.
VARIANT 8 8 L -> V (in dbSNP:rs1063560).
{ECO:0000269|PubMed:10880057,
ECO:0000269|PubMed:2261637}.
/FTId=VAR_047782.
VARIANT 148 148 G -> R (polymorphism; associated with
increased levels of soluble IL6RB in
blood serum; dbSNP:rs2228044).
{ECO:0000269|PubMed:24629561}.
/FTId=VAR_047783.
VARIANT 200 200 A -> G (found in patient with lung
cancer; unknown pathological
significance; dbSNP:rs199905033).
{ECO:0000269|PubMed:25242236}.
/FTId=VAR_074654.
VARIANT 397 397 L -> V (in dbSNP:rs2228043).
/FTId=VAR_047784.
VARIANT 415 415 T -> I (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036165.
VARIANT 454 454 I -> T (in dbSNP:rs2228046).
/FTId=VAR_047785.
VARIANT 499 499 V -> I (in dbSNP:rs34417936).
/FTId=VAR_047786.
MUTAGEN 172 172 C->S: Induces ligand-independent
activation.
{ECO:0000269|PubMed:23294003}.
MUTAGEN 186 190 Missing: Induces ligand-independent
activation.
{ECO:0000269|PubMed:23294003}.
MUTAGEN 189 189 V->G: Does not induce ligand-independent
activation.
{ECO:0000269|PubMed:23294003}.
MUTAGEN 190 190 Y->G: Does not induce ligand-independent
activation.
{ECO:0000269|PubMed:23294003}.
MUTAGEN 215 215 D->G: Induces ligand-independent
activation.
{ECO:0000269|PubMed:23294003}.
MUTAGEN 252 252 V->G: Induces ligand-independent
activation.
{ECO:0000269|PubMed:23294003}.
MUTAGEN 782 782 S->A: Increases cell surface expression.
{ECO:0000269|PubMed:10811661}.
STRAND 28 35 {ECO:0000244|PDB:1I1R}.
STRAND 37 39 {ECO:0000244|PDB:1I1R}.
STRAND 44 50 {ECO:0000244|PDB:1I1R}.
HELIX 52 58 {ECO:0000244|PDB:1I1R}.
HELIX 62 64 {ECO:0000244|PDB:1I1R}.
STRAND 65 69 {ECO:0000244|PDB:1I1R}.
HELIX 76 78 {ECO:0000244|PDB:1I1R}.
STRAND 80 83 {ECO:0000244|PDB:1I1R}.
STRAND 86 91 {ECO:0000244|PDB:1I1R}.
STRAND 97 107 {ECO:0000244|PDB:1I1R}.
TURN 108 110 {ECO:0000244|PDB:1I1R}.
STRAND 111 123 {ECO:0000244|PDB:1I1R}.
STRAND 130 137 {ECO:0000244|PDB:1BQU}.
STRAND 143 147 {ECO:0000244|PDB:1BQU}.
STRAND 157 164 {ECO:0000244|PDB:1BQU}.
STRAND 176 178 {ECO:0000244|PDB:1PVH}.
STRAND 181 183 {ECO:0000244|PDB:1BQU}.
STRAND 194 202 {ECO:0000244|PDB:1BQU}.
STRAND 205 208 {ECO:0000244|PDB:1BQU}.
STRAND 212 214 {ECO:0000244|PDB:1BQU}.
HELIX 216 218 {ECO:0000244|PDB:1BQU}.
STRAND 219 221 {ECO:0000244|PDB:1BQU}.
STRAND 226 231 {ECO:0000244|PDB:1BQU}.
STRAND 234 238 {ECO:0000244|PDB:1I1R}.
STRAND 240 245 {ECO:0000244|PDB:1BQU}.
HELIX 248 251 {ECO:0000244|PDB:1BQU}.
STRAND 255 263 {ECO:0000244|PDB:1BQU}.
HELIX 274 277 {ECO:0000244|PDB:1BQU}.
STRAND 282 286 {ECO:0000244|PDB:1BQU}.
STRAND 291 303 {ECO:0000244|PDB:1BQU}.
STRAND 317 321 {ECO:0000244|PDB:1BQU}.
HELIX 325 331 {ECO:0000244|PDB:1BQU}.
STRAND 332 338 {ECO:0000244|PDB:3L5I}.
STRAND 345 351 {ECO:0000244|PDB:3L5I}.
HELIX 356 359 {ECO:0000244|PDB:3L5I}.
STRAND 363 372 {ECO:0000244|PDB:3L5I}.
STRAND 378 391 {ECO:0000244|PDB:3L5I}.
STRAND 396 406 {ECO:0000244|PDB:3L5I}.
STRAND 412 416 {ECO:0000244|PDB:3L5I}.
STRAND 428 435 {ECO:0000244|PDB:3L5I}.
STRAND 438 444 {ECO:0000244|PDB:3L5I}.
STRAND 452 460 {ECO:0000244|PDB:3L5I}.
STRAND 462 464 {ECO:0000244|PDB:3L5I}.
STRAND 469 474 {ECO:0000244|PDB:3L5I}.
STRAND 478 481 {ECO:0000244|PDB:3L5I}.
STRAND 491 500 {ECO:0000244|PDB:3L5I}.
STRAND 508 515 {ECO:0000244|PDB:3L5I}.
STRAND 525 530 {ECO:0000244|PDB:3L5I}.
STRAND 535 539 {ECO:0000244|PDB:3L5I}.
HELIX 544 547 {ECO:0000244|PDB:3L5I}.
STRAND 553 560 {ECO:0000244|PDB:3L5I}.
STRAND 566 571 {ECO:0000244|PDB:3L5I}.
STRAND 575 579 {ECO:0000244|PDB:3L5I}.
STRAND 587 596 {ECO:0000244|PDB:3L5I}.
STRAND 599 602 {ECO:0000244|PDB:3L5I}.
STRAND 606 609 {ECO:0000244|PDB:3L5I}.
SEQUENCE 918 AA; 103537 MW; 6510A4409FFCF08C CRC64;
MLTLQTWLVQ ALFIFLTTES TGELLDPCGY ISPESPVVQL HSNFTAVCVL KEKCMDYFHV
NANYIVWKTN HFTIPKEQYT IINRTASSVT FTDIASLNIQ LTCNILTFGQ LEQNVYGITI
ISGLPPEKPK NLSCIVNEGK KMRCEWDGGR ETHLETNFTL KSEWATHKFA DCKAKRDTPT
SCTVDYSTVY FVNIEVWVEA ENALGKVTSD HINFDPVYKV KPNPPHNLSV INSEELSSIL
KLTWTNPSIK SVIILKYNIQ YRTKDASTWS QIPPEDTAST RSSFTVQDLK PFTEYVFRIR
CMKEDGKGYW SDWSEEASGI TYEDRPSKAP SFWYKIDPSH TQGYRTVQLV WKTLPPFEAN
GKILDYEVTL TRWKSHLQNY TVNATKLTVN LTNDRYLATL TVRNLVGKSD AAVLTIPACD
FQATHPVMDL KAFPKDNMLW VEWTTPRESV KKYILEWCVL SDKAPCITDW QQEDGTVHRT
YLRGNLAESK CYLITVTPVY ADGPGSPESI KAYLKQAPPS KGPTVRTKKV GKNEAVLEWD
QLPVDVQNGF IRNYTIFYRT IIGNETAVNV DSSHTEYTLS SLTSDTLYMV RMAAYTDEGG
KDGPEFTFTT PKFAQGEIEA IVVPVCLAFL LTTLLGVLFC FNKRDLIKKH IWPNVPDPSK
SHIAQWSPHT PPRHNFNSKD QMYSDGNFTD VSVVEIEAND KKPFPEDLKS LDLFKKEKIN
TEGHSSGIGG SSCMSSSRPS ISSSDENESS QNTSSTVQYS TVVHSGYRHQ VPSVQVFSRS
ESTQPLLDSE ERPEDLQLVD HVDGGDGILP RQQYFKQNCS QHESSPDISH FERSKQVSSV
NEEDFVRLKQ QISDHISQSC GSGQMKMFQE VSAADAFGPG TEGQVERFET VGMEAATDEG
MPKSYLPQTV RQGGYMPQ


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