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

 IL6RB_MOUSE             Reviewed;         917 AA.
Q00560; G5E8D2;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
25-OCT-2017, entry version 167.
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=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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=ICR; TISSUE=Macrophage;
PubMed=1602143;
Saito M., Yoshida K., Hibi M., Taga T., Kishimoto T.;
"Molecular cloning of a murine IL-6 receptor-associated signal
transducer, gp130, and its regulated expression in vivo.";
J. Immunol. 148:4066-4071(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8552649; DOI=10.1073/pnas.93.1.407;
Yoshida K., Taga T., Saito M., Suematsu S., Kumanogoh A., Tanaka T.,
Fujiwara H., Hirata M., Yamagami T., Nakahata T., Hirabayashi T.,
Yoneda Y., Tanaka K., Wang W.Z., Mori C., Shiota K., Yoshida N.,
Kishimoto T.;
"Targeted disruption of gp130, a common signal transducer for the
interleukin 6 family of cytokines, leads to myocardial and
hematological disorders.";
Proc. Natl. Acad. Sci. U.S.A. 93:407-411(1996).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9348227; DOI=10.1210/endo.138.11.5534;
Kawasaki K., Gao Y.H., Yokose S., Kaji Y., Nakamura T., Suda T.,
Yoshida K., Taga T., Kishimoto T., Kataoka H., Yuasa T., Norimatsu H.,
Yamaguchi A.;
"Osteoclasts are present in gp130-deficient mice.";
Endocrinology 138:4959-4965(1997).
[6]
SUBUNIT.
PubMed=9920829;
Tanaka M., Hara T., Copeland N.G., Gilbert D.J., Jenkins N.A.,
Miyajima A.;
"Reconstitution of the functional mouse oncostatin M (OSM) receptor:
molecular cloning of the OSM receptor beta subunit.";
Blood 93:804-815(1999).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10377352;
Nakashima K., Wiese S., Yanagisawa M., Arakawa H., Kimura N.,
Hisatsune T., Yoshida K., Kishimoto T., Sendtner M., Taga T.;
"Developmental requirement of gp130 signaling in neuronal survival and
astrocyte differentiation.";
J. Neurosci. 19:5429-5434(1999).
[8]
FUNCTION.
PubMed=10661409; DOI=10.1016/S1074-7613(00)80162-4;
Ohtani T., Ishihara K., Atsumi T., Nishida K., Kaneko Y., Miyata T.,
Itoh S., Narimatsu M., Maeda H., Fukada T., Itoh M., Okano H.,
Hibi M., Hirano T.;
"Dissection of signaling cascades through gp130 in vivo: reciprocal
roles for STAT3- and SHP2-mediated signals in immune responses.";
Immunity 12:95-105(2000).
[9]
INTERACTION WITH INPP5D.
PubMed=17105399; DOI=10.1089/scd.2006.15.641;
Desponts C., Ninos J.M., Kerr W.G.;
"s-SHIP associates with receptor complexes essential for pluripotent
stem cell growth and survival.";
Stem Cells Dev. 15:641-646(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24339143; DOI=10.1002/jbmr.2159;
Johnson R.W., Brennan H.J., Vrahnas C., Poulton I.J., McGregor N.E.,
Standal T., Walker E.C., Koh T.T., Nguyen H., Walsh N.C.,
Forwood M.R., Martin T.J., Sims N.A.;
"The primary function of gp130 signaling in osteoblasts is to maintain
bone formation and strength, rather than promote osteoclast
formation.";
J. Bone Miner. Res. 29:1492-1505(2014).
[14]
FUNCTION.
PubMed=25228504; DOI=10.1530/JOE-14-0424;
Standal T., Johnson R.W., McGregor N.E., Poulton I.J., Ho P.W.,
Martin T.J., Sims N.A.;
"gp130 in late osteoblasts and osteocytes is required for PTH-induced
osteoblast differentiation.";
J. Endocrinol. 223:181-190(2014).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25057188; DOI=10.1523/JNEUROSCI.5161-13.2014;
Malsch P., Andratsch M., Vogl C., Link A.S., Alzheimer C.,
Brierley S.M., Hughes P.A., Kress M.;
"Deletion of interleukin-6 signal transducer gp130 in small sensory
neurons attenuates mechanonociception and down-regulates TRPA1
expression.";
J. Neurosci. 34:9845-9856(2014).
[16]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=26255596; DOI=10.1016/j.bone.2015.08.005;
Johnson R.W., McGregor N.E., Brennan H.J., Crimeen-Irwin B.,
Poulton I.J., Martin T.J., Sims N.A.;
"Glycoprotein130 (Gp130)/interleukin-6 (IL-6) signalling in
osteoclasts promotes bone formation in periosteal and trabecular
bone.";
Bone 81:343-351(2015).
-!- 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:1602143). That
causes phosphorylation of IL6ST tyrosine residues which in turn
activates STAT3 (PubMed:10661409). Mediates signals which regulate
immune response, hematopoiesis, pain control and bone metabolism
(PubMed:10661409, PubMed:26255596, PubMed:25057188,
PubMed:8552649). Has a role in embryonic development
(PubMed:10661409). Does not bind IL6 (By similarity). Essential
for survival of motor and sensory neurons and for differentiation
of astrocytes (PubMed:10377352). Required for expression of TRPA1
in nociceptive neurons (PubMed:25057188). Required for the
maintenance of PTH1R expression in the osteoblast lineage and for
the stimulation of PTH-induced osteoblast differentiation
(PubMed:25228504). Required for normal trabecular bone mass and
cortical bone composition (PubMed:24339143, PubMed:9348227,
PubMed:26255596). {ECO:0000250|UniProtKB:P40189,
ECO:0000269|PubMed:10377352, ECO:0000269|PubMed:10661409,
ECO:0000269|PubMed:1602143, ECO:0000269|PubMed:24339143,
ECO:0000269|PubMed:25057188, ECO:0000269|PubMed:25228504,
ECO:0000269|PubMed:26255596, ECO:0000269|PubMed:8552649,
ECO:0000269|PubMed:9348227}.
-!- SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R
and IL6ST. Forms heterodimers composed of LIFR and IL6ST (type I
OSM receptor) which are activated by LIF and OSM. Also forms
heterodimers composed of OSMR and IL6ST (type II receptor) which
are activated by OSM but not by LIF. Interacts with HCK (By
similarity). Interacts with INPP5D/SHIP1 (PubMed:17105399).
{ECO:0000250|UniProtKB:P40189, ECO:0000269|PubMed:17105399,
ECO:0000269|PubMed:9920829}.
-!- INTERACTION:
P97378:Il12rb2; NbExp=2; IntAct=EBI-3862992, EBI-6253448;
O35718:Socs3; NbExp=2; IntAct=EBI-3862992, EBI-2659360;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P40189}; Single-pass type I membrane
protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Found in tissues such as brain, heart, thymus,
spleen, kidney, lung and liver. Found in all the cell lines tested
except BaF-B03. Expression not restricted to IL6-responsive cells.
{ECO:0000269|PubMed:1602143}.
-!- DEVELOPMENTAL STAGE: In embryonic stem cells it is found from day
6 of gestation. It reaches a peak on day 8 and gradually declines
during the rest of embryogenesis. {ECO:0000269|PubMed:1602143}.
-!- 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-780 down-regulates cell surface
expression. {ECO:0000250|UniProtKB:P40189}.
-!- PTM: Heavily N-glycosylated. Glycosylation is required for protein
stability and localization in plasma membrane but not for ligand
binding. {ECO:0000250|UniProtKB:P40189}.
-!- DISRUPTION PHENOTYPE: Progressively lethal between E12.5 and birth
(PubMed:8552649). Embryos show hypoplastic ventricular myocardium
without septal and trabecular defect, reduced numbers of
pluripotential and committed hematopoietic progenitors in liver
and reduced differentiated lineages in thymus (PubMed:8552649).
Impaired differentiation of astrocytes and decreased number of
dorsal root ganglion and motor neurons at E18.5 (PubMed:10377352).
Decreased volume of mineralized trabecular bones, while number of
osteoclasts is increased (PubMed:9348227, PubMed:26255596).
Conditional knockout from the entire osteoblast lineage or
specifically in osteocytes causes no significant skeletal or
morphological defects but mice show 30% lower trabecular bone
formation rate and larger cortical diameter compared to wild type
(PubMed:24339143, PubMed:26255596). Conditional knockout in
primary nociceptive afferents causes reduced sensitivity to
mechanical stimulation due to reduced sensitivity of nociceptive
neurons and reduces TRPA1 mRNA expression in dorsal root ganglion
neurons (PubMed:25057188). {ECO:0000269|PubMed:10377352,
ECO:0000269|PubMed:24339143, ECO:0000269|PubMed:25057188,
ECO:0000269|PubMed:26255596, ECO:0000269|PubMed:8552649,
ECO:0000269|PubMed:9348227}.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X62646; CAA44515.1; -; mRNA.
EMBL; M83336; AAA37723.1; -; mRNA.
EMBL; AC159196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466568; EDL18412.1; -; Genomic_DNA.
CCDS; CCDS26773.1; -.
PIR; I49699; I49699.
RefSeq; NP_034690.3; NM_010560.3.
UniGene; Mm.4364; -.
PDB; 2BBU; NMR; -; B=750-764.
PDB; 2HMH; X-ray; 2.00 A; B=753-763.
PDB; 4GL9; X-ray; 3.90 A; I/J/K/L=750-764.
PDBsum; 2BBU; -.
PDBsum; 2HMH; -.
PDBsum; 4GL9; -.
ProteinModelPortal; Q00560; -.
SMR; Q00560; -.
BioGrid; 200643; 8.
CORUM; Q00560; -.
DIP; DIP-5782N; -.
IntAct; Q00560; 8.
MINT; MINT-3382082; -.
STRING; 10090.ENSMUSP00000064205; -.
iPTMnet; Q00560; -.
PhosphoSitePlus; Q00560; -.
SwissPalm; Q00560; -.
MaxQB; Q00560; -.
PaxDb; Q00560; -.
PRIDE; Q00560; -.
Ensembl; ENSMUST00000070731; ENSMUSP00000064205; ENSMUSG00000021756.
Ensembl; ENSMUST00000183663; ENSMUSP00000138836; ENSMUSG00000021756.
Ensembl; ENSMUST00000184311; ENSMUSP00000139227; ENSMUSG00000021756.
GeneID; 16195; -.
KEGG; mmu:16195; -.
UCSC; uc007rwg.2; mouse.
CTD; 3572; -.
MGI; MGI:96560; Il6st.
eggNOG; ENOG410IF1N; Eukaryota.
eggNOG; ENOG410YNQ4; LUCA.
GeneTree; ENSGT00550000074436; -.
HOGENOM; HOG000015771; -.
HOVERGEN; HBG052119; -.
InParanoid; Q00560; -.
KO; K05060; -.
OMA; FCFNKRD; -.
OrthoDB; EOG091G01XM; -.
TreeFam; TF338122; -.
Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
Reactome; R-MMU-112411; MAPK1 (ERK2) activation.
Reactome; R-MMU-447115; Interleukin-12 family signaling.
Reactome; R-MMU-6783589; Interleukin-6 family signaling.
Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
Reactome; R-MMU-8984722; Interleukin-35 Signalling.
EvolutionaryTrace; Q00560; -.
PRO; PR:Q00560; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021756; -.
CleanEx; MM_IL6ST; -.
ExpressionAtlas; Q00560; baseline and differential.
Genevisible; Q00560; MM.
GO; GO:0044297; C:cell body; IDA:MGI.
GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; ISO:MGI.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005896; C:interleukin-6 receptor complex; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005900; C:oncostatin-M receptor complex; ISO:MGI.
GO; GO:0004897; F:ciliary neurotrophic factor receptor activity; ISO:MGI.
GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; ISO:MGI.
GO; GO:0019838; F:growth factor binding; ISO:MGI.
GO; GO:0019981; F:interleukin-6 binding; IEA:Ensembl.
GO; GO:0004915; F:interleukin-6 receptor activity; IEA:Ensembl.
GO; GO:0005138; F:interleukin-6 receptor binding; IEA:Ensembl.
GO; GO:0004923; F:leukemia inhibitory factor receptor activity; IEA:Ensembl.
GO; GO:0004924; F:oncostatin-M receptor activity; IEA:Ensembl.
GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; ISO:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0005977; P:glycogen metabolic process; IMP:MGI.
GO; GO:0038154; P:interleukin-11-mediated signaling pathway; IEA:GOC.
GO; GO:0070106; P:interleukin-27-mediated signaling pathway; ISO:MGI.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISO:MGI.
GO; GO:0048861; P:leukemia inhibitory factor signaling pathway; ISO:MGI.
GO; GO:0070104; P:negative regulation of interleukin-6-mediated signaling pathway; ISO:MGI.
GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; ISO:MGI.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
GO; GO:0008593; P:regulation of Notch signaling pathway; IDA:MGI.
GO; GO:0034097; P:response to cytokine; ISO:MGI.
GO; GO:0007165; P:signal transduction; IDA:MGI.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
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; 4.
PROSITE; PS50853; FN3; 5.
PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 917 Interleukin-6 receptor subunit beta.
/FTId=PRO_0000010900.
TOPO_DOM 23 617 Extracellular. {ECO:0000255}.
TRANSMEM 618 639 Helical. {ECO:0000255}.
TOPO_DOM 640 917 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 120 Ig-like C2-type.
DOMAIN 128 221 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 222 322 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 327 417 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 422 515 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 517 611 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 308 312 WSXWS motif.
MOTIF 649 657 Box 1 motif.
COMPBIAS 723 741 Ser-rich.
MOD_RES 659 659 Phosphoserine.
{ECO:0000250|UniProtKB:P40189}.
MOD_RES 665 665 Phosphoserine.
{ECO:0000250|UniProtKB:P40189}.
MOD_RES 780 780 Phosphoserine.
{ECO:0000250|UniProtKB:P40189}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 827 827 Phosphoserine.
{ECO:0000250|UniProtKB:P40189}.
MOD_RES 837 837 Phosphoserine.
{ECO:0000250|UniProtKB:P40189}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 131 131 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 225 225 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 388 388 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 476 476 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 551 551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 54 {ECO:0000250|UniProtKB:P40189}.
DISULFID 48 103 {ECO:0000250|UniProtKB:P40189}.
DISULFID 134 144 {ECO:0000250|UniProtKB:P40189}.
DISULFID 172 180 {ECO:0000250|UniProtKB:P40189}.
DISULFID 456 464 {ECO:0000250|UniProtKB:P40189}.
CONFLICT 756 756 Q -> E (in Ref. 1; CAA44515/AAA37723).
{ECO:0000305}.
SEQUENCE 917 AA; 102451 MW; EDA69AB865E5A6E8 CRC64;
MSAPRIWLAQ ALLFFLTTES IGQLLEPCGY IYPEFPVVQR GSNFTAICVL KEACLQHYYV
NASYIVWKTN HAAVPREQVT VINRTTSSVT FTDVVLPSVQ LTCNILSFGQ IEQNVYGVTM
LSGFPPDKPT NLTCIVNEGK NMLCQWDPGR ETYLETNYTL KSEWATEKFP DCQSKHGTSC
MVSYMPTYYV NIEVWVEAEN ALGKVSSESI NFDPVDKVKP TPPYNLSVTN SEELSSILKL
SWVSSGLGGL LDLKSDIQYR TKDASTWIQV PLEDTMSPRT SFTVQDLKPF TEYVFRIRSI
KDSGKGYWSD WSEEASGTTY EDRPSRPPSF WYKTNPSHGQ EYRSVRLIWK ALPLSEANGK
ILDYEVILTQ SKSVSQTYTV TGTELTVNLT NDRYVASLAA RNKVGKSAAA VLTIPSPHVT
AAYSVVNLKA FPKDNLLWVE WTPPPKPVSK YILEWCVLSE NAPCVEDWQQ EDATVNRTHL
RGRLLESKCY QITVTPVFAT GPGGSESLKA YLKQAAPARG PTVRTKKVGK NEAVLAWDQI
PVDDQNGFIR NYSISYRTSV GKEMVVHVDS SHTEYTLSSL SSDTLYMVRM AAYTDEGGKD
GPEFTFTTPK FAQGEIEAIV VPVCLAFLLT TLLGVLFCFN KRDLIKKHIW PNVPDPSKSH
IAQWSPHTPP RHNFNSKDQM YSDGNFTDVS VVEIEANNKK PCPDDLKSVD LFKKEKVSTE
GHSSGIGGSS CMSSSRPSIS SNEENESAQS TASTVQYSTV VHSGYRHQVP SVQVFSRSES
TQPLLDSEER PEDLQLVDSV DGGDEILPRQ PYFKQNCSQP EACPEISHFE RSNQVLSGNE
EDFVRLKQQQ VSDHISQPYG SEQRRLFQEG STADALGTGA DGQMERFESV GMETTIDEEI
PKSYLPQTVR QGGYMPQ


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U0046r CLIA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Oncostatin-M receptor sub 96T
E0046r ELISA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Oncostatin-M receptor su 96T
20-272-190538 CD130 ( gp130 ) - Mouse monoclonal [B - T2] to CD130 ( gp130 ); IL-6R-beta; Interleukin-6 signal transducer; Membrane glycoprotein 130; gp130; Oncostatin-M receptor alpha subunit; CD130 antigen; CDw13 0.05 mg
E0046h ELISA CDw130,gp130,Homo sapiens,Human,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,IL6ST,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 13 96T
U0046h CLIA CDw130,gp130,Homo sapiens,Human,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,IL6ST,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130 96T
U0046m CLIA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Mouse,Mus musculus,Oncost 96T
E0046m ELISA gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Mouse,Mus musculus,Oncos 96T
E0046m ELISA kit gp130,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,Il6st,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprotein 130,Mouse,Mus musculus, 96T
E0046h ELISA kit CDw130,gp130,Homo sapiens,Human,IL-6 receptor subunit beta,IL-6R subunit beta,IL-6RB,IL-6R-beta,IL6ST,Interleukin-6 receptor subunit beta,Interleukin-6 signal transducer,Membrane glycoprote 96T
20-272-190537 CD130 ( gp130 ) ( FITC ) - Mouse monoclonal [B - R3] to CD130 ( gp130 ) ( FITC ); IL-6R-beta; Interleukin-6 signal transducer; Membrane glycoprotein 130; gp130; Oncostatin-M receptor alpha subunit; CD 0.5 ml
U1761h CLIA Homo sapiens,Human,IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,OSMR,OSMRB 96T
E1761h ELISA kit Homo sapiens,Human,IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,OSMR,OSMRB 96T
E1761h ELISA Homo sapiens,Human,IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,OSMR,OSMRB 96T
E1761r ELISA kit IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb,Rat,Rattus norvegicus 96T
E1761m ELISA kit IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Mouse,Mus musculus,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb 96T
E1761m ELISA IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Mouse,Mus musculus,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb 96T
U1761m CLIA IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Mouse,Mus musculus,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb 96T
U1761r CLIA IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb,Rat,Rattus norvegicus 96T
E1761r ELISA IL-31 receptor subunit beta,IL-31R subunit beta,IL-31RB,IL-31R-beta,Interleukin-31 receptor subunit beta,Oncostatin-M-specific receptor subunit beta,Osmr,Osmrb,Rat,Rattus norvegicus 96T
U1837h CLIA High affinity IL-2 receptor subunit beta,Homo sapiens,Human,IL-2 receptor subunit beta,IL-2R subunit beta,IL2RB,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,p75 96T
E1837h ELISA kit High affinity IL-2 receptor subunit beta,Homo sapiens,Human,IL-2 receptor subunit beta,IL-2R subunit beta,IL2RB,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,p75 96T
U1837h CLIA kit High affinity IL-2 receptor subunit beta,Homo sapiens,Human,IL-2 receptor subunit beta,IL-2R subunit beta,IL2RB,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,p75 96T
E1837h ELISA High affinity IL-2 receptor subunit beta,Homo sapiens,Human,IL-2 receptor subunit beta,IL-2R subunit beta,IL2RB,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,p75 96T
U1837r CLIA kit High affinity IL-2 receptor subunit beta,IL-2 receptor subunit beta,IL-2R subunit beta,Il2rb,IL-2RB,Interleukin-2 receptor subunit beta,p70-75,Rat,Rattus norvegicus 96T


 

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