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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.
12-AUG-2020, entry version 187.
RecName: Full=Interleukin-6 receptor subunit beta {ECO:0000305};
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 {ECO:0000303|PubMed:1602143};
AltName: Full=Oncostatin-M receptor subunit alpha;
AltName: CD_antigen=CD130;
Flags: Precursor;
Name=Il6st {ECO:0000312|MGI:MGI:96560};
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]
FUNCTION.
TISSUE=Thymus;
PubMed=9202125; DOI=10.1038/43206;
Starr R., Willson T.A., Viney E.M., Murray L.J.L., Rayner J.R.,
Jenkins B.J., Gonda T.J., Alexander W.S., Metcalf D., Nicola N.A.,
Hilton D.J.;
"A family of cytokine-inducible inhibitors of signaling.";
Nature 387:917-921(1997).
[7]
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).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10377352; DOI=10.1523/jneurosci.19-13-05429.1999;
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).
[9]
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).
[10]
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).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
FUNCTION.
PubMed=25731159; DOI=10.1038/nature14228;
Taniguchi K., Wu L.W., Grivennikov S.I., de Jong P.R., Lian I., Yu F.X.,
Wang K., Ho S.B., Boland B.S., Chang J.T., Sandborn W.J., Hardiman G.,
Raz E., Maehara Y., Yoshimura A., Zucman-Rossi J., Guan K.L., Karin M.;
"A gp130-Src-YAP module links inflammation to epithelial regeneration.";
Nature 519:57-62(2015).
[19]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY OBESITY.
PubMed=28402851; DOI=10.1016/j.celrep.2017.03.043;
Timper K., Denson J.L., Steculorum S.M., Heilinger C., Engstroem-Ruud L.,
Wunderlich C.M., Rose-John S., Wunderlich F.T., Bruening J.C.;
"IL-6 Improves Energy and Glucose Homeostasis in Obesity via Enhanced
Central IL-6 trans-Signaling.";
Cell Rep. 19:267-280(2017).
[20]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=27893700; DOI=10.1038/ni.3632;
Heink S., Yogev N., Garbers C., Herwerth M., Aly L., Gasperi C.,
Husterer V., Croxford A.L., Moeller-Hackbarth K., Bartsch H.S., Sotlar K.,
Krebs S., Regen T., Blum H., Hemmer B., Misgeld T., Wunderlich T.F.,
Hidalgo J., Oukka M., Rose-John S., Schmidt-Supprian M., Waisman A.,
Korn T.;
"Trans-presentation of IL-6 by dendritic cells is required for the priming
of pathogenic TH17 cells.";
Nat. Immunol. 18:74-85(2017).
-!- FUNCTION: Signal-transducing molecule (PubMed:1602143). 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 activate the intracellular JAK-MAPK and JAK-STAT3
signaling pathways (PubMed:1602143, PubMed:10661409). That causes
phosphorylation of IL6ST tyrosine residues which in turn activates
STAT3 (PubMed:10661409). In parallel, the IL6 signaling pathway induces
the expression of two cytokine receptor signaling inhibitors, SOCS1 and
SOCS3, which inhibit JAK and terminate the activity of the IL6
signaling pathway as a negative feedback loop (PubMed:9202125). Also
activates the yes-associated protein 1 (YAP) and NOTCH pathways to
control inflammation-induced epithelial regeneration, independently of
STAT3 (PubMed:25731159). 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). 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:25731159,
ECO:0000269|PubMed:26255596, ECO:0000269|PubMed:8552649,
ECO:0000269|PubMed:9202125, ECO:0000269|PubMed:9348227}.
-!- SUBUNIT: Component of a hexamer of two molecules each of IL6, IL6R and
IL6ST; associates with the complex IL6:IL6R but does not interact with
IL6 (By similarity). 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). Interacts with SRC and
YES (By similarity). {ECO:0000250|UniProtKB:P40189,
ECO:0000269|PubMed:17105399, ECO:0000269|PubMed:9920829}.
-!- INTERACTION:
Q00560; P97378: Il12rb2; NbExp=2; IntAct=EBI-3862992, EBI-6253448;
Q00560; 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: Expression not restricted to IL6-responsive cells.
Found in tissues such as brain, heart, thymus, spleen, kidney, lung and
liver. Found in all the cell lines tested except BaF-B03. Expressed
paraventricular nucleus of the hypothalamus (PubMed:28402851).
{ECO:0000269|PubMed:1602143, ECO:0000269|PubMed:28402851}.
-!- 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}.
-!- INDUCTION: In paraventricular nucleus of the hypothalamus, expression
is enhanced by obesity. {ECO:0000269|PubMed:28402851}.
-!- 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 12.5 dpc 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 18.5 dpc (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.
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.
PDB; 6C5X; X-ray; 3.10 A; G=754-763.
PDBsum; 2BBU; -.
PDBsum; 2HMH; -.
PDBsum; 4GL9; -.
PDBsum; 6C5X; -.
SMR; Q00560; -.
BioGRID; 200643; 13.
CORUM; Q00560; -.
DIP; DIP-5782N; -.
IntAct; Q00560; 8.
MINT; Q00560; -.
STRING; 10090.ENSMUSP00000138836; -.
GlyConnect; 2412; 2 N-Linked glycans (1 site).
GlyGen; Q00560; 9 sites.
iPTMnet; Q00560; -.
PhosphoSitePlus; Q00560; -.
SwissPalm; Q00560; -.
jPOST; Q00560; -.
MaxQB; Q00560; -.
PaxDb; Q00560; -.
PRIDE; Q00560; -.
Antibodypedia; 2448; 751 antibodies.
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; ENOG502QXEG; Eukaryota.
GeneTree; ENSGT00940000159608; -.
InParanoid; Q00560; -.
KO; K05060; -.
OMA; YLITVYP; -.
OrthoDB; 144839at2759; -.
TreeFam; TF338122; -.
Reactome; R-MMU-1059683; Interleukin-6 signaling.
Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
Reactome; R-MMU-112411; MAPK1 (ERK2) activation.
Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
Reactome; R-MMU-8984722; Interleukin-35 Signalling.
Reactome; R-MMU-9020956; Interleukin-27 signaling.
BioGRID-ORCS; 16195; 2 hits in 20 CRISPR screens.
ChiTaRS; Il6st; mouse.
EvolutionaryTrace; Q00560; -.
PRO; PR:Q00560; -.
Proteomes; UP000000589; Chromosome 13.
RNAct; Q00560; protein.
Bgee; ENSMUSG00000021756; Expressed in fibroblast and 301 other tissues.
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:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005896; C:interleukin-6 receptor complex; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
GO; GO:0005900; C:oncostatin-M receptor complex; ISO:MGI.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0004897; F:ciliary neurotrophic factor receptor activity; ISO:MGI.
GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; ISO:MGI.
GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
GO; GO:0019838; F:growth factor binding; ISO:MGI.
GO; GO:0042802; F:identical protein 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:0051481; P:negative regulation of cytosolic calcium ion concentration; 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 population proliferation; IGI:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; 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.
GO; GO:0006642; P:triglyceride mobilization; ISO:MGI.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 6.
IDEAL; IID50222; -.
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; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1..22
/evidence="ECO:0000255"
CHAIN 23..917
/note="Interleukin-6 receptor subunit beta"
/id="PRO_0000010900"
TOPO_DOM 23..617
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 618..639
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 640..917
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 26..120
/note="Ig-like C2-type"
DOMAIN 128..221
/note="Fibronectin type-III 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 222..322
/note="Fibronectin type-III 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 327..417
/note="Fibronectin type-III 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 422..515
/note="Fibronectin type-III 4"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 517..611
/note="Fibronectin type-III 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
MOTIF 308..312
/note="WSXWS motif"
MOTIF 649..657
/note="Box 1 motif"
COMPBIAS 723..741
/note="Ser-rich"
MOD_RES 659
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P40189"
MOD_RES 665
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P40189"
MOD_RES 780
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P40189"
MOD_RES 787
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 827
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P40189"
MOD_RES 837
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P40189"
CARBOHYD 43
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 61
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 83
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 131
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 157
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 225
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973"
CARBOHYD 388
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 476
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 551
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 28..54
/evidence="ECO:0000250|UniProtKB:P40189"
DISULFID 48..103
/evidence="ECO:0000250|UniProtKB:P40189"
DISULFID 134..144
/evidence="ECO:0000250|UniProtKB:P40189"
DISULFID 172..180
/evidence="ECO:0000250|UniProtKB:P40189"
DISULFID 456..464
/evidence="ECO:0000250|UniProtKB:P40189"
CONFLICT 756
/note="Q -> E (in Ref. 1; CAA44515/AAA37723)"
/evidence="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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Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP1566: Citrate cycle (TCA cycle)
WP566: canonical wnt - zebrafish
WP2292: Chemokine signaling pathway
WP258: TGF-beta Receptor Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP2272: Pathogenic Escherichia coli infection
WP809: TGF-beta Receptor Signaling Pathway
WP362: TGF-beta Receptor Signaling Pathway
WP1367: TGF-beta Receptor Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP244: Alpha 6 Beta 4 signaling pathway
WP215: noncanonical wnt pathway
WP210: Cytoplasmic Ribosomal Proteins
WP537: Translation Factors
WP1434: Osteopontin Signaling
WP433: tRNA Synthetases
WP1225: estrogen signalling
WP1835: Interferon alpha/beta signaling
WP1571: EBV LMP1 signaling
WP1904: RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways
WP1224: EBV LMP1 signaling
WP219: Cytoplasmic tRNA Synthetases

Related Genes :
[Il6st] 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)
[IL6ST] 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)
[Il6st] 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)
[IL6R] Interleukin-6 receptor subunit alpha (IL-6 receptor subunit alpha) (IL-6R subunit alpha) (IL-6R-alpha) (IL-6RA) (IL-6R 1) (Membrane glycoprotein 80) (gp80) (CD antigen CD126) [Cleaved into: Soluble interleukin-6 receptor subunit alpha (sIL6R)]
[IL31RA CRL3 GPL UNQ6368/PRO21073/PRO21384] Interleukin-31 receptor subunit alpha (IL-31 receptor subunit alpha) (IL-31R subunit alpha) (IL-31R-alpha) (IL-31RA) (Cytokine receptor-like 3) (GLM-R) (hGLM-R) (Gp130-like monocyte receptor) (Gp130-like receptor) (ZcytoR17)
[OSMR OSMRB] Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB)
[Osmr Osmrb] Oncostatin-M-specific receptor subunit beta (Interleukin-31 receptor subunit beta) (IL-31 receptor subunit beta) (IL-31R subunit beta) (IL-31R-beta) (IL-31RB)
[Il12rb2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[IL12RB1 IL12R IL12RB] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12RB1) (IL-12 receptor beta component) (CD antigen CD212)
[Il12rb1 Il12rb] Interleukin-12 receptor subunit beta-1 (IL-12 receptor subunit beta-1) (IL-12R subunit beta-1) (IL-12R-beta-1) (IL-12 receptor beta component) (CD antigen CD212)
[IL2RB IL15RB] Interleukin-2 receptor subunit beta (IL-2 receptor subunit beta) (IL-2R subunit beta) (IL-2RB) (High affinity IL-2 receptor subunit beta) (Interleukin-15 receptor subunit beta) (p70-75) (p75) (CD antigen CD122)
[IL18RAP IL1R7] Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (EC 3.2.2.6) (Accessory protein-like) (AcPL) (CD218 antigen-like family member B) (CDw218b) (IL-1R accessory protein-like) (IL-1RAcPL) (Interleukin-1 receptor 7) (IL-1R-7) (IL-1R7) (Interleukin-18 receptor accessory protein-like) (Interleukin-18 receptor beta) (IL-18R-beta) (IL-18Rbeta) (CD antigen CD218b)
[Il11ra1 Etl2 Il11ra] Interleukin-11 receptor subunit alpha-1 (IL-11 receptor subunit alpha-1) (IL-11R subunit alpha-1) (IL-11R-alpha-1) (IL-11RA1) (Enhancer trap locus homolog 2) (Etl-2) (Novel cytokine receptor 1) (NR-1) (NR1) [Cleaved into: Soluble interleukin-11 receptor subunit alpha (sIL-11R) (sIL-11RA) (sIL11RA)]
[IL12RB2] Interleukin-12 receptor subunit beta-2 (IL-12 receptor subunit beta-2) (IL-12R subunit beta-2) (IL-12R-beta-2) (IL-12RB2)
[Il3ra Sut-1] Interleukin-3 receptor subunit alpha (IL-3 receptor subunit alpha) (IL-3R subunit alpha) (IL-3R-alpha) (IL-3RA) (Interleukin-3 receptor class II alpha chain) (CD antigen CD123)
[Il4r Il4ra] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[Il27ra Tccr Wsx1] Interleukin-27 receptor subunit alpha (IL-27 receptor subunit alpha) (IL-27R subunit alpha) (IL-27R-alpha) (IL-27RA) (Type I T-cell cytokine receptor) (TCCR) (WSX-1)
[Il1rap] Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-33 receptot beta chain)
[IL1R1 IL1R IL1RA IL1RT1] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[Il7r] Interleukin-7 receptor subunit alpha (IL-7 receptor subunit alpha) (IL-7R subunit alpha) (IL-7R-alpha) (IL-7RA) (CD antigen CD127)
[IL6 IFNB2] Interleukin-6 (IL-6) (B-cell stimulatory factor 2) (BSF-2) (CTL differentiation factor) (CDF) (Hybridoma growth factor) (Interferon beta-2) (IFN-beta-2)
[IL10RB CRFB4 D21S58 D21S66] Interleukin-10 receptor subunit beta (IL-10 receptor subunit beta) (IL-10R subunit beta) (IL-10RB) (Cytokine receptor class-II member 4) (Cytokine receptor family 2 member 4) (CRF2-4) (Interleukin-10 receptor subunit 2) (IL-10R subunit 2) (IL-10R2) (CD antigen CDw210b)
[Il1r1 Il1ra] Interleukin-1 receptor type 1 (IL-1R-1) (IL-1RT-1) (IL-1RT1) (EC 3.2.2.6) (CD121 antigen-like family member A) (Interleukin-1 receptor alpha) (IL-1R-alpha) (Interleukin-1 receptor type I) (p80) (CD antigen CD121a) [Cleaved into: Interleukin-1 receptor type 1, membrane form (mIL-1R1) (mIL-1RI); Interleukin-1 receptor type 1, soluble form (sIL-1R1) (sIL-1RI)]
[Il2rg] Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)
[IL11RA] Interleukin-11 receptor subunit alpha (IL-11 receptor subunit alpha) (IL-11R subunit alpha) (IL-11R-alpha) (IL-11RA) [Cleaved into: Soluble interleukin-11 receptor subunit alpha (sIL-11R) (sIL-11RA) (sIL11RA)]
[IL4R IL4RA 582J2.1] Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]
[IL10RA IL10R] Interleukin-10 receptor subunit alpha (IL-10 receptor subunit alpha) (IL-10R subunit alpha) (IL-10RA) (CDw210a) (Interleukin-10 receptor subunit 1) (IL-10R subunit 1) (IL-10R1) (CD antigen CD210)
[IL13RA1 IL13R IL13RA] Interleukin-13 receptor subunit alpha-1 (IL-13 receptor subunit alpha-1) (IL-13R subunit alpha-1) (IL-13R-alpha-1) (IL-13RA1) (Cancer/testis antigen 19) (CT19) (CD antigen CD213a1)
[IL18R1 IL1RRP] Interleukin-18 receptor 1 (IL-18R-1) (IL-18R1) (EC 3.2.2.6) (CD218 antigen-like family member A) (CDw218a) (IL1 receptor-related protein) (IL-1Rrp) (IL1R-rp) (Interleukin-18 receptor alpha) (IL-18R-alpha) (IL-18Ralpha) (CD antigen CD218a)
[Il6 Il-6] Interleukin-6 (IL-6) (B-cell hybridoma growth factor) (Interleukin HP-1)

Bibliography :
No related Items