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

Cytokine receptor common subunit beta (CDw131) (GM-CSF/IL-3/IL-5 receptor common beta subunit) (CD antigen CD131)

 IL3RB_HUMAN             Reviewed;         897 AA.
P32927; Q5JZI1; Q6ICE0;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
25-OCT-2017, entry version 184.
RecName: Full=Cytokine receptor common subunit beta;
AltName: Full=CDw131;
AltName: Full=GM-CSF/IL-3/IL-5 receptor common beta subunit;
AltName: CD_antigen=CD131;
Flags: Precursor;
Name=CSF2RB; Synonyms=IL3RB, IL5RB;
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).
PubMed=1702217; DOI=10.1073/pnas.87.24.9655;
Hayashida K., Kitamura T., Gorman D.M., Arai K., Yokota T.,
Miyajima A.;
"Molecular cloning of a second subunit of the receptor for human
granulocyte-macrophage colony-stimulating factor (GM-CSF):
reconstitution of a high-affinity GM-CSF receptor.";
Proc. Natl. Acad. Sci. U.S.A. 87:9655-9659(1990).
[2]
SEQUENCE REVISION TO 454.
Kitamura T.;
Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[5]
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.
[6]
INTERACTION WITH TMEM102.
PubMed=17828305; DOI=10.1038/sj.onc.1210778;
Kao C.J., Chiang Y.J., Chen P.H., Lin K.R., Hwang P.I., Yang-Yen H.F.,
Yen J.J.;
"CBAP interacts with the un-liganded common beta-subunit of the GM-
CSF/IL-3/IL-5 receptor and induces apoptosis via mitochondrial
dysfunction.";
Oncogene 27:1397-1403(2008).
[7]
INVOLVEMENT IN SMDP5.
PubMed=21075760; DOI=10.1136/jmg.2010.082586;
Tanaka T., Motoi N., Tsuchihashi Y., Tazawa R., Kaneko C., Nei T.,
Yamamoto T., Hayashi T., Tagawa T., Nagayasu T., Kuribayashi F.,
Ariyoshi K., Nakata K., Morimoto K.;
"Adult-onset hereditary pulmonary alveolar proteinosis caused by a
single-base deletion in CSF2RB.";
J. Med. Genet. 48:205-209(2011).
[8]
STRUCTURE BY NMR OF 338-438.
PubMed=10736232; DOI=10.1006/jmbi.2000.3610;
Mulhern T.D., Lopez A.F., D'Andrea R.J., Gaunt C., Vandeleur L.,
Vadas M.A., Booker G.W., Bagley C.J.;
"The solution structure of the cytokine-binding domain of the common
beta-chain of the receptors for granulocyte-macrophage colony-
stimulating factor, interleukin-3 and interleukin-5.";
J. Mol. Biol. 297:989-1001(2000).
[9]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 338-438.
PubMed=10753826;
Rossjohn J., McKinstry W.J., Woodcock J.M., McClure B.J., Hercus T.R.,
Parker M.W., Lopez A.F., Bagley C.J.;
"Structure of the activation domain of the GM-CSF/IL-3/IL-5 receptor
common beta-chain bound to an antagonist.";
Blood 95:2491-2498(2000).
[10]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-437.
PubMed=11207369; DOI=10.1016/S0092-8674(01)00213-6;
Carr P.D., Gustin S.E., Church A.P., Murphy J.M., Ford S.C.,
Mann D.A., Woltring D.M., Walker I., Ollis D.L., Young I.G.;
"Structure of the complete extracellular domain of the common beta
subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel
dimer configuration.";
Cell 104:291-300(2001).
[11]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 25-443, DISULFIDE BONDS,
SUBUNIT, AND GLYCOSYLATION AT ASN-58 AND ASN-191.
PubMed=16754968; DOI=10.1107/S1744309106016812;
Carr P.D., Conlan F., Ford S., Ollis D.L., Young I.G.;
"An improved resolution structure of the human beta common receptor
involved in IL-3, IL-5 and GM-CSF signalling which gives better
definition of the high-affinity binding epitope.";
Acta Crystallogr. F 62:509-513(2006).
[12]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-438 IN COMPLEX WITH CSF2RA
AND CSF2, SUBUNIT, GLYCOSYLATION AT ASN-58 AND ASN-191, AND DISULFIDE
BONDS.
PubMed=18692472; DOI=10.1016/j.cell.2008.05.053;
Hansen G., Hercus T.R., McClure B.J., Stomski F.C., Dottore M.,
Powell J., Ramshaw H., Woodcock J.M., Xu Y., Guthridge M.,
McKinstry W.J., Lopez A.F., Parker M.W.;
"The structure of the GM-CSF receptor complex reveals a distinct mode
of cytokine receptor activation.";
Cell 134:496-507(2008).
[13]
VARIANT THR-603.
PubMed=9410898; DOI=10.1172/JCI119758;
Dirksen U., Nishinakamura R., Groneck P., Hattenhorst U., Nogee L.,
Murray R., Burdach S.;
"Human pulmonary alveolar proteinosis associated with a defect in GM-
CSF/IL-3/IL-5 receptor common beta chain expression.";
J. Clin. Invest. 100:2211-2217(1997).
-!- FUNCTION: High affinity receptor for interleukin-3, interleukin-5
and granulocyte-macrophage colony-stimulating factor.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta
subunit is common to the IL3, IL5 and GM-CSF receptors. The
signaling GM-CSF receptor complex is a dodecamer of two head-to-
head hexamers of two alpha, two beta, and two ligand subunits.
Interacts with TMEM102; this interaction occurs preferentially in
the absence of CSF2. Interacts with LYN (By similarity).
{ECO:0000250}.
-!- INTERACTION:
P04141:CSF2; NbExp=2; IntAct=EBI-1809771, EBI-1809826;
P05113:IL5; NbExp=2; IntAct=EBI-1809771, EBI-2435811;
Q01344:IL5RA; NbExp=3; IntAct=EBI-1809771, EBI-1759442;
P05556:ITGB1; NbExp=5; IntAct=EBI-1809771, EBI-703066;
O60674:JAK2; NbExp=4; IntAct=EBI-1809771, EBI-518647;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P32927-1; Sequence=Displayed;
Name=2;
IsoId=P32927-2; Sequence=VSP_032798;
-!- 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: May be phosphorylated by LYN. {ECO:0000250}.
-!- DISEASE: Pulmonary surfactant metabolism dysfunction 5 (SMDP5)
[MIM:614370]: A rare lung disorder due to impaired surfactant
homeostasis. It is characterized by alveolar filling with
floccular material that stains positive using the periodic acid-
Schiff method and is derived from surfactant phospholipids and
protein components. Excessive lipoproteins accumulation in the
alveoli results in severe respiratory distress.
{ECO:0000269|PubMed:21075760}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M59941; AAA18171.1; -; mRNA.
EMBL; CR456428; CAG30314.1; -; mRNA.
EMBL; AL008637; CAI17999.1; -; Genomic_DNA.
EMBL; AL133392; CAI17999.1; JOINED; Genomic_DNA.
EMBL; AL008637; CAQ10744.1; -; Genomic_DNA.
EMBL; AL133392; CAQ10744.1; JOINED; Genomic_DNA.
EMBL; CH471095; EAW60125.1; -; Genomic_DNA.
EMBL; CH471095; EAW60126.1; -; Genomic_DNA.
CCDS; CCDS13936.1; -. [P32927-1]
PIR; A39255; A39255.
RefSeq; NP_000386.1; NM_000395.2. [P32927-1]
RefSeq; XP_005261397.1; XM_005261340.3. [P32927-2]
UniGene; Hs.592192; -.
PDB; 1C8P; NMR; -; A=338-438.
PDB; 1EGJ; X-ray; 2.80 A; A=338-438.
PDB; 1GH7; X-ray; 3.00 A; A/B=25-437.
PDB; 2GYS; X-ray; 2.70 A; A/B=25-437.
PDB; 2NA8; NMR; -; A=432-473.
PDB; 2NA9; NMR; -; A=432-473.
PDB; 4NKQ; X-ray; 3.30 A; A=25-438.
PDB; 5DWU; X-ray; 3.97 A; A=17-240, B=241-443.
PDBsum; 1C8P; -.
PDBsum; 1EGJ; -.
PDBsum; 1GH7; -.
PDBsum; 2GYS; -.
PDBsum; 2NA8; -.
PDBsum; 2NA9; -.
PDBsum; 4NKQ; -.
PDBsum; 5DWU; -.
ProteinModelPortal; P32927; -.
SMR; P32927; -.
BioGrid; 107826; 15.
CORUM; P32927; -.
DIP; DIP-127N; -.
ELM; P32927; -.
IntAct; P32927; 16.
MINT; MINT-105697; -.
STRING; 9606.ENSP00000384053; -.
ChEMBL; CHEMBL2364169; -.
DrugBank; DB05264; NPI 32101.
DrugBank; DB00020; Sargramostim.
iPTMnet; P32927; -.
PhosphoSitePlus; P32927; -.
BioMuta; CSF2RB; -.
DMDM; 1345923; -.
PaxDb; P32927; -.
PeptideAtlas; P32927; -.
PRIDE; P32927; -.
DNASU; 1439; -.
Ensembl; ENST00000403662; ENSP00000384053; ENSG00000100368. [P32927-1]
Ensembl; ENST00000406230; ENSP00000385271; ENSG00000100368. [P32927-2]
GeneID; 1439; -.
KEGG; hsa:1439; -.
UCSC; uc003aqa.5; human. [P32927-1]
CTD; 1439; -.
DisGeNET; 1439; -.
EuPathDB; HostDB:ENSG00000100368.13; -.
GeneCards; CSF2RB; -.
HGNC; HGNC:2436; CSF2RB.
HPA; HPA078677; -.
MalaCards; CSF2RB; -.
MIM; 138981; gene.
MIM; 614370; phenotype.
neXtProt; NX_P32927; -.
OpenTargets; ENSG00000100368; -.
Orphanet; 264675; Congenital pulmonary alveolar proteinosis.
PharmGKB; PA26939; -.
eggNOG; ENOG410IGEX; Eukaryota.
eggNOG; ENOG4112BQP; LUCA.
GeneTree; ENSGT00510000048963; -.
HOGENOM; HOG000113049; -.
HOVERGEN; HBG052113; -.
InParanoid; P32927; -.
KO; K04738; -.
OMA; CRWADTQ; -.
OrthoDB; EOG091G05K0; -.
PhylomeDB; P32927; -.
TreeFam; TF337996; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-5683826; Surfactant metabolism.
Reactome; R-HSA-5688849; Defective CSF2RB causes pulmonary surfactant metabolism dysfunction 5 (SMDP5).
Reactome; R-HSA-5688890; Defective CSF2RA causes pulmonary surfactant metabolism dysfunction 4 (SMDP4).
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
SignaLink; P32927; -.
SIGNOR; P32927; -.
ChiTaRS; CSF2RB; human.
EvolutionaryTrace; P32927; -.
GenomeRNAi; 1439; -.
PRO; PR:P32927; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100368; -.
CleanEx; HS_CSF2RB; -.
ExpressionAtlas; P32927; baseline and differential.
Genevisible; P32927; HS.
GO; GO:0030526; C:granulocyte macrophage colony-stimulating factor receptor complex; TAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0036016; P:cellular response to interleukin-3; IEA:GOC.
GO; GO:0038156; P:interleukin-3-mediated signaling pathway; IEA:GOC.
GO; GO:0038043; P:interleukin-5-mediated signaling pathway; IEA:GOC.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0007585; P:respiratory gaseous exchange; TAS:ProtInc.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011365; IL3_rcpt_beta.
InterPro; IPR015373; Interferon/interleukin_rcp_dom.
InterPro; IPR015321; TypeI_recpt_CBD.
Pfam; PF09240; IL6Ra-bind; 1.
Pfam; PF09294; Interfer-bind; 1.
PIRSF; PIRSF001956; IL3R_beta_c; 1.
SMART; SM00060; FN3; 2.
SUPFAM; SSF49265; SSF49265; 4.
PROSITE; PS50853; FN3; 2.
PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 897 Cytokine receptor common subunit beta.
/FTId=PRO_0000010862.
TOPO_DOM 17 443 Extracellular. {ECO:0000255}.
TRANSMEM 444 460 Helical. {ECO:0000255}.
TOPO_DOM 461 897 Cytoplasmic. {ECO:0000255}.
DOMAIN 133 240 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 339 436 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 425 429 WSXWS motif.
MOTIF 474 482 Box 1 motif.
MOD_RES 766 766 Phosphotyrosine.
{ECO:0000250|UniProtKB:P26955}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16754968,
ECO:0000269|PubMed:18692472}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16754968,
ECO:0000269|PubMed:18692472}.
CARBOHYD 346 346 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 45
DISULFID 75 96
DISULFID 86 91
DISULFID 250 260
DISULFID 289 306
VAR_SEQ 285 285 G -> GSAVLLR (in isoform 2).
{ECO:0000303|PubMed:15461802}.
/FTId=VSP_032798.
VARIANT 249 249 E -> Q (in dbSNP:rs16845).
/FTId=VAR_042521.
VARIANT 603 603 P -> T (in dbSNP:rs1801122).
{ECO:0000269|PubMed:9410898}.
/FTId=VAR_014801.
VARIANT 647 647 G -> V (in dbSNP:rs1801115).
/FTId=VAR_014802.
VARIANT 652 652 V -> M (in dbSNP:rs1801114).
/FTId=VAR_014803.
VARIANT 696 696 P -> S (in dbSNP:rs16997517).
/FTId=VAR_042522.
HELIX 28 32 {ECO:0000244|PDB:2GYS}.
STRAND 34 37 {ECO:0000244|PDB:2GYS}.
STRAND 39 50 {ECO:0000244|PDB:2GYS}.
HELIX 51 54 {ECO:0000244|PDB:2GYS}.
STRAND 59 66 {ECO:0000244|PDB:2GYS}.
STRAND 69 72 {ECO:0000244|PDB:2GYS}.
STRAND 75 77 {ECO:0000244|PDB:2GYS}.
STRAND 88 99 {ECO:0000244|PDB:2GYS}.
STRAND 108 117 {ECO:0000244|PDB:2GYS}.
STRAND 121 126 {ECO:0000244|PDB:2GYS}.
HELIX 127 129 {ECO:0000244|PDB:2GYS}.
STRAND 137 144 {ECO:0000244|PDB:2GYS}.
STRAND 147 153 {ECO:0000244|PDB:2GYS}.
STRAND 162 164 {ECO:0000244|PDB:4NKQ}.
HELIX 166 168 {ECO:0000244|PDB:2GYS}.
STRAND 169 177 {ECO:0000244|PDB:2GYS}.
HELIX 182 184 {ECO:0000244|PDB:1GH7}.
STRAND 186 197 {ECO:0000244|PDB:2GYS}.
TURN 199 201 {ECO:0000244|PDB:2GYS}.
STRAND 207 216 {ECO:0000244|PDB:2GYS}.
STRAND 218 221 {ECO:0000244|PDB:1GH7}.
STRAND 233 236 {ECO:0000244|PDB:2GYS}.
STRAND 246 252 {ECO:0000244|PDB:2GYS}.
STRAND 254 265 {ECO:0000244|PDB:2GYS}.
HELIX 266 269 {ECO:0000244|PDB:2GYS}.
STRAND 274 279 {ECO:0000244|PDB:2GYS}.
STRAND 292 295 {ECO:0000244|PDB:2GYS}.
TURN 298 300 {ECO:0000244|PDB:2GYS}.
STRAND 301 309 {ECO:0000244|PDB:2GYS}.
TURN 313 315 {ECO:0000244|PDB:2GYS}.
STRAND 318 325 {ECO:0000244|PDB:2GYS}.
STRAND 330 333 {ECO:0000244|PDB:2GYS}.
HELIX 334 336 {ECO:0000244|PDB:2GYS}.
STRAND 337 339 {ECO:0000244|PDB:1GH7}.
STRAND 344 348 {ECO:0000244|PDB:2GYS}.
STRAND 350 352 {ECO:0000244|PDB:1GH7}.
STRAND 355 359 {ECO:0000244|PDB:2GYS}.
STRAND 365 367 {ECO:0000244|PDB:1C8P}.
STRAND 370 377 {ECO:0000244|PDB:2GYS}.
STRAND 379 381 {ECO:0000244|PDB:2GYS}.
HELIX 383 385 {ECO:0000244|PDB:1GH7}.
STRAND 388 393 {ECO:0000244|PDB:2GYS}.
STRAND 395 398 {ECO:0000244|PDB:2GYS}.
STRAND 405 407 {ECO:0000244|PDB:1GH7}.
STRAND 409 416 {ECO:0000244|PDB:2GYS}.
STRAND 418 420 {ECO:0000244|PDB:1GH7}.
STRAND 432 436 {ECO:0000244|PDB:1EGJ}.
HELIX 442 466 {ECO:0000244|PDB:2NA8}.
SEQUENCE 897 AA; 97336 MW; 3398E37FDB8F393A CRC64;
MVLAQGLLSM ALLALCWERS LAGAEETIPL QTLRCYNDYT SHITCRWADT QDAQRLVNVT
LIRRVNEDLL EPVSCDLSDD MPWSACPHPR CVPRRCVIPC QSFVVTDVDY FSFQPDRPLG
TRLTVTLTQH VQPPEPRDLQ ISTDQDHFLL TWSVALGSPQ SHWLSPGDLE FEVVYKRLQD
SWEDAAILLS NTSQATLGPE HLMPSSTYVA RVRTRLAPGS RLSGRPSKWS PEVCWDSQPG
DEAQPQNLEC FFDGAAVLSC SWEVRKEVAS SVSFGLFYKP SPDAGEEECS PVLREGLGSL
HTRHHCQIPV PDPATHGQYI VSVQPRRAEK HIKSSVNIQM APPSLNVTKD GDSYSLRWET
MKMRYEHIDH TFEIQYRKDT ATWKDSKTET LQNAHSMALP ALEPSTRYWA RVRVRTSRTG
YNGIWSEWSE ARSWDTESVL PMWVLALIVI FLTIAVLLAL RFCGIYGYRL RRKWEEKIPN
PSKSHLFQNG SAELWPPGSM SAFTSGSPPH QGPWGSRFPE LEGVFPVGFG DSEVSPLTIE
DPKHVCDPPS GPDTTPAASD LPTEQPPSPQ PGPPAASHTP EKQASSFDFN GPYLGPPHSR
SLPDILGQPE PPQEGGSQKS PPPGSLEYLC LPAGGQVQLV PLAQAMGPGQ AVEVERRPSQ
GAAGSPSLES GGGPAPPALG PRVGGQDQKD SPVAIPMSSG DTEDPGVASG YVSSADLVFT
PNSGASSVSL VPSLGLPSDQ TPSLCPGLAS GPPGAPGPVK SGFEGYVELP PIEGRSPRSP
RNNPVPPEAK SPVLNPGERP ADVSPTSPQP EGLLVLQQVG DYCFLPGLGP GPLSLRSKPS
SPGPGPEIKN LDQAFQVKKP PGQAVPQVPV IQLFKALKQQ DYLSLPPWEV NKPGEVC


Related products :

Catalog number Product name Quantity
CSB-EL006047MO Mouse Cytokine receptor common subunit beta(CSF2RB) ELISA kit 96T
CSB-EL006047HU Human Cytokine receptor common subunit beta(CSF2RB) ELISA kit 96T
CSB-EL006047HU Human Cytokine receptor common subunit beta(CSF2RB) ELISA kit SpeciesHuman 96T
CSB-EL006047MO Mouse Cytokine receptor common subunit beta(CSF2RB) ELISA kit SpeciesMouse 96T
IL3RB_MOUSE ELISA Kit FOR Cytokine receptor common subunit beta; organism: Mouse; gene name: Csf2rb 96T
IL3RB_HUMAN ELISA Kit FOR Cytokine receptor common subunit beta; organism: Human; gene name: CSF2RB 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
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
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
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
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
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
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 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
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
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 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
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
U1837m CLIA High affinity IL-2 receptor subunit beta,IL-2 receptor subunit beta,IL-2R subunit beta,Il2rb,IL-2RB,Interleukin-2 receptor subunit beta,Mouse,Mus musculus,p70-75 96T
E1837m ELISA 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,Mouse,Mus musculus,p70-75 96T
E1837r ELISA 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
U1837r CLIA 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
U1837m 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,Mouse,Mus musculus,p70-75 96T


 

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