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Interleukin-5 receptor subunit alpha (IL-5 receptor subunit alpha) (IL-5R subunit alpha) (IL-5R-alpha) (IL-5RA) (CDw125) (CD antigen CD125)

 IL5RA_HUMAN             Reviewed;         420 AA.
Q01344; B3IU77; B4E2G0; Q14633; Q15469; Q6ISX9;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 177.
RecName: Full=Interleukin-5 receptor subunit alpha;
Short=IL-5 receptor subunit alpha;
Short=IL-5R subunit alpha;
Short=IL-5R-alpha;
Short=IL-5RA;
AltName: Full=CDw125;
AltName: CD_antigen=CD125;
Flags: Precursor;
Name=IL5RA; Synonyms=IL5R;
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 2).
PubMed=1833065; DOI=10.1016/0092-8674(91)90040-6;
Tavernier J., Devos R., Cornelis S., Tuypens T., van der Heyden J.,
Fiers W., Plaetinck G.;
"A human high affinity interleukin-5 receptor (IL5R) is composed of an
IL5-specific alpha chain and a beta chain shared with the receptor for
GM-CSF.";
Cell 66:1175-1184(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND VARIANT VAL-129.
TISSUE=Peripheral blood;
PubMed=1732409; DOI=10.1084/jem.175.2.341;
Murata Y., Takaki S., Migita M., Kikuchi Y., Tominaga A., Takatsu K.;
"Molecular cloning and expression of the human interleukin 5
receptor.";
J. Exp. Med. 175:341-351(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
PubMed=1495999; DOI=10.1073/pnas.89.15.7041;
Tavernier J., Tuypens T., Plaetinck G., Verhee A., Fiers W., Devos R.;
"Molecular basis of the membrane-anchored and two soluble isoforms of
the human interleukin 5 receptor alpha subunit.";
Proc. Natl. Acad. Sci. U.S.A. 89:7041-7045(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Ishihara K., Yamada M., Hirasawa N., Ohuchi K.;
"Isolation of the variants for human interleukin-5 receptor alpha
subunit.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-129 AND ALA-262.
SeattleSNPs variation discovery resource;
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[8]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 413-420 IN COMPLEX WITH
SDCBP.
PubMed=12842047; DOI=10.1016/S0969-2126(03)00125-4;
Kang B.S., Cooper D.R., Devedjiev Y., Derewenda U., Derewenda Z.S.;
"Molecular roots of degenerate specificity in syntenin's PDZ2 domain:
reassessment of the PDZ recognition paradigm.";
Structure 11:845-853(2003).
[9]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 20-332 IN COMPLEX WITH IL5,
AND DISULFIDE BONDS.
PubMed=22153509; DOI=10.1016/j.str.2011.08.015;
Patino E., Kotzsch A., Saremba S., Nickel J., Schmitz W., Sebald W.,
Mueller T.D.;
"Structure analysis of the IL-5 ligand-receptor complex reveals a
wrench-like architecture for IL-5Ralpha.";
Structure 19:1864-1875(2011).
-!- FUNCTION: This is the receptor for interleukin-5. The alpha chain
binds to IL5.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta
subunit is common to the IL3, IL5 and GM-CSF receptors. Interacts
with SDCBP. {ECO:0000269|PubMed:12842047,
ECO:0000269|PubMed:22153509}.
-!- INTERACTION:
P32927:CSF2RB; NbExp=3; IntAct=EBI-1759442, EBI-1809771;
P05113:IL5; NbExp=4; IntAct=EBI-15957545, EBI-2435811;
O60674:JAK2; NbExp=2; IntAct=EBI-1759442, EBI-518647;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=Membrane-bound;
IsoId=Q01344-1; Sequence=Displayed;
Name=2; Synonyms=Soluble-S1;
IsoId=Q01344-2; Sequence=VSP_001678, VSP_001679;
Name=3; Synonyms=Soluble-S2;
IsoId=Q01344-3; Sequence=VSP_001680, VSP_001681;
Name=4;
IsoId=Q01344-4; Sequence=VSP_046742;
Name=5;
IsoId=Q01344-5; Sequence=VSP_047762;
-!- TISSUE SPECIFICITY: Expressed on eosinophils and basophils.
-!- 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.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il5ra/";
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EMBL; M75914; AAA36110.1; -; mRNA.
EMBL; X61176; CAA43483.1; -; mRNA.
EMBL; X62156; CAA44081.1; -; mRNA.
EMBL; M96651; AAA59151.1; -; mRNA.
EMBL; M96652; AAA59152.1; -; mRNA.
EMBL; AB288090; BAG49562.1; -; mRNA.
EMBL; AK304256; BAG65122.1; -; mRNA.
EMBL; AY642135; AAT45457.1; -; Genomic_DNA.
EMBL; AC022002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC024060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS2559.1; -. [Q01344-1]
CCDS; CCDS2560.1; -. [Q01344-2]
CCDS; CCDS46739.1; -. [Q01344-3]
CCDS; CCDS58813.1; -. [Q01344-4]
PIR; A40267; A40267.
RefSeq; NP_000555.2; NM_000564.4. [Q01344-1]
RefSeq; NP_001230028.1; NM_001243099.1. [Q01344-4]
RefSeq; NP_783851.1; NM_175724.2. [Q01344-3]
RefSeq; NP_783852.1; NM_175725.2. [Q01344-2]
RefSeq; NP_783853.1; NM_175726.3. [Q01344-1]
RefSeq; NP_783854.1; NM_175727.2. [Q01344-3]
RefSeq; NP_783855.1; NM_175728.2. [Q01344-2]
UniGene; Hs.68876; -.
PDB; 1OBX; X-ray; 1.35 A; B=413-420.
PDB; 1OBZ; X-ray; 1.69 A; P=413-420.
PDB; 3QT2; X-ray; 2.55 A; A/B=20-335.
PDB; 3VA2; X-ray; 2.70 A; C=21-335.
PDBsum; 1OBX; -.
PDBsum; 1OBZ; -.
PDBsum; 3QT2; -.
PDBsum; 3VA2; -.
ProteinModelPortal; Q01344; -.
SMR; Q01344; -.
BioGrid; 109782; 15.
DIP; DIP-3510N; -.
ELM; Q01344; -.
IntAct; Q01344; 5.
STRING; 9606.ENSP00000256452; -.
ChEMBL; CHEMBL3580483; -.
GuidetoPHARMACOLOGY; 1706; -.
iPTMnet; Q01344; -.
PhosphoSitePlus; Q01344; -.
BioMuta; IL5RA; -.
DMDM; 116242525; -.
MaxQB; Q01344; -.
PaxDb; Q01344; -.
PeptideAtlas; Q01344; -.
PRIDE; Q01344; -.
Ensembl; ENST00000256452; ENSP00000256452; ENSG00000091181. [Q01344-1]
Ensembl; ENST00000311981; ENSP00000309196; ENSG00000091181. [Q01344-2]
Ensembl; ENST00000383846; ENSP00000373358; ENSG00000091181. [Q01344-2]
Ensembl; ENST00000430514; ENSP00000400400; ENSG00000091181. [Q01344-3]
Ensembl; ENST00000438560; ENSP00000390753; ENSG00000091181. [Q01344-4]
Ensembl; ENST00000446632; ENSP00000412209; ENSG00000091181. [Q01344-1]
Ensembl; ENST00000456302; ENSP00000392059; ENSG00000091181. [Q01344-3]
GeneID; 3568; -.
KEGG; hsa:3568; -.
UCSC; uc010hbs.4; human. [Q01344-1]
CTD; 3568; -.
DisGeNET; 3568; -.
EuPathDB; HostDB:ENSG00000091181.19; -.
GeneCards; IL5RA; -.
HGNC; HGNC:6017; IL5RA.
MIM; 147851; gene.
neXtProt; NX_Q01344; -.
OpenTargets; ENSG00000091181; -.
PharmGKB; PA29834; -.
eggNOG; ENOG410IJ36; Eukaryota.
eggNOG; ENOG4111ZG2; LUCA.
GeneTree; ENSGT00530000063295; -.
HOGENOM; HOG000070224; -.
HOVERGEN; HBG052117; -.
InParanoid; Q01344; -.
KO; K05067; -.
OMA; ACWFPRT; -.
OrthoDB; EOG091G0B29; -.
PhylomeDB; Q01344; -.
TreeFam; TF331549; -.
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-912526; Interleukin receptor SHC signaling.
SignaLink; Q01344; -.
SIGNOR; Q01344; -.
ChiTaRS; IL5RA; human.
EvolutionaryTrace; Q01344; -.
GeneWiki; Interleukin_5_receptor_alpha_subunit; -.
GenomeRNAi; 3568; -.
PRO; PR:Q01344; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000091181; -.
CleanEx; HS_IL5RA; -.
ExpressionAtlas; Q01344; baseline and differential.
Genevisible; Q01344; HS.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004914; F:interleukin-5 receptor activity; TAS:ProtInc.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0032674; P:regulation of interleukin-5 production; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003532; Short_hematopoietin_rcpt_2_CS.
InterPro; IPR015321; TypeI_recpt_CBD.
Pfam; PF09240; IL6Ra-bind; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 2.
PROSITE; PS01356; HEMATOPO_REC_S_F2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Membrane; Polymorphism; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 20
CHAIN 21 420 Interleukin-5 receptor subunit alpha.
/FTId=PRO_0000010893.
TOPO_DOM 21 342 Extracellular. {ECO:0000255}.
TRANSMEM 343 362 Helical. {ECO:0000255}.
TOPO_DOM 363 420 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 123 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 241 334 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 322 326 WSXWS motif.
MOTIF 371 379 Box 1 motif.
CARBOHYD 35 35 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 131 131 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 216 216 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 134 155 {ECO:0000269|PubMed:22153509}.
DISULFID 182 196 {ECO:0000269|PubMed:22153509}.
DISULFID 269 316 {ECO:0000269|PubMed:22153509}.
VAR_SEQ 123 331 Missing (in isoform 5).
{ECO:0000303|Ref.4}.
/FTId=VSP_047762.
VAR_SEQ 333 335 NDE -> FSR (in isoform 2).
{ECO:0000303|PubMed:1833065}.
/FTId=VSP_001678.
VAR_SEQ 333 333 N -> K (in isoform 3).
{ECO:0000303|PubMed:1495999,
ECO:0000303|PubMed:1732409}.
/FTId=VSP_001680.
VAR_SEQ 334 420 Missing (in isoform 3).
{ECO:0000303|PubMed:1495999,
ECO:0000303|PubMed:1732409}.
/FTId=VSP_001681.
VAR_SEQ 336 420 Missing (in isoform 2).
{ECO:0000303|PubMed:1833065}.
/FTId=VSP_001679.
VAR_SEQ 365 420 CHLWIKLFPPIPAPKSNIKDLFVTTNYEKAGSSETEIEVIC
YIEKPGVETLEDSVF -> KLGPVRRKLKSSVI (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046742.
VARIANT 129 129 I -> V (in dbSNP:rs2290610).
{ECO:0000269|PubMed:1732409,
ECO:0000269|Ref.6}.
/FTId=VAR_020654.
VARIANT 262 262 V -> A (in dbSNP:rs17879690).
{ECO:0000269|Ref.6}.
/FTId=VAR_020655.
CONFLICT 212 212 A -> S (in Ref. 1; AAA36110 and 2;
AAA59151/AAA59152). {ECO:0000305}.
STRAND 34 42 {ECO:0000244|PDB:3QT2}.
STRAND 45 51 {ECO:0000244|PDB:3QT2}.
STRAND 59 61 {ECO:0000244|PDB:3QT2}.
STRAND 64 73 {ECO:0000244|PDB:3QT2}.
STRAND 75 87 {ECO:0000244|PDB:3QT2}.
STRAND 94 103 {ECO:0000244|PDB:3QT2}.
STRAND 108 110 {ECO:0000244|PDB:3QT2}.
STRAND 114 118 {ECO:0000244|PDB:3QT2}.
STRAND 122 124 {ECO:0000244|PDB:3VA2}.
HELIX 125 127 {ECO:0000244|PDB:3QT2}.
STRAND 130 140 {ECO:0000244|PDB:3QT2}.
STRAND 144 146 {ECO:0000244|PDB:3QT2}.
STRAND 149 158 {ECO:0000244|PDB:3QT2}.
STRAND 168 175 {ECO:0000244|PDB:3QT2}.
STRAND 178 181 {ECO:0000244|PDB:3QT2}.
STRAND 185 187 {ECO:0000244|PDB:3QT2}.
STRAND 193 200 {ECO:0000244|PDB:3QT2}.
STRAND 209 218 {ECO:0000244|PDB:3QT2}.
STRAND 227 232 {ECO:0000244|PDB:3QT2}.
HELIX 233 236 {ECO:0000244|PDB:3QT2}.
STRAND 243 250 {ECO:0000244|PDB:3QT2}.
STRAND 253 259 {ECO:0000244|PDB:3QT2}.
STRAND 262 265 {ECO:0000244|PDB:3QT2}.
HELIX 267 269 {ECO:0000244|PDB:3QT2}.
STRAND 270 278 {ECO:0000244|PDB:3QT2}.
TURN 279 281 {ECO:0000244|PDB:3QT2}.
STRAND 284 297 {ECO:0000244|PDB:3QT2}.
STRAND 304 312 {ECO:0000244|PDB:3QT2}.
TURN 314 316 {ECO:0000244|PDB:3QT2}.
STRAND 329 331 {ECO:0000244|PDB:3QT2}.
SEQUENCE 420 AA; 47685 MW; 4E0A5F2838B9C4FE CRC64;
MIIVAHVLLI LLGATEILQA DLLPDEKISL LPPVNFTIKV TGLAQVLLQW KPNPDQEQRN
VNLEYQVKIN APKEDDYETR ITESKCVTIL HKGFSASVRT ILQNDHSLLA SSWASAELHA
PPGSPGTSIV NLTCTTNTTE DNYSRLRSYQ VSLHCTWLVG TDAPEDTQYF LYYRYGSWTE
ECQEYSKDTL GRNIACWFPR TFILSKGRDW LAVLVNGSSK HSAIRPFDQL FALHAIDQIN
PPLNVTAEIE GTRLSIQWEK PVSAFPIHCF DYEVKIHNTR NGYLQIEKLM TNAFISIIDD
LSKYDVQVRA AVSSMCREAG LWSEWSQPIY VGNDEHKPLR EWFVIVIMAT ICFILLILSL
ICKICHLWIK LFPPIPAPKS NIKDLFVTTN YEKAGSSETE IEVICYIEKP GVETLEDSVF


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U2031h CLIA 582J2.1,Homo sapiens,Human,IL-4 receptor subunit alpha,IL4R,IL-4R subunit alpha,IL4RA,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha 96T
E0229b ELISA kit Bos taurus,Bovine,IL-2 receptor subunit alpha,IL-2R subunit alpha,IL2RA,IL-2-RA,IL2-RA,Interleukin-2 receptor subunit alpha,p55,TAC antigen 96T
E0229b ELISA Bos taurus,Bovine,IL-2 receptor subunit alpha,IL-2R subunit alpha,IL2RA,IL-2-RA,IL2-RA,Interleukin-2 receptor subunit alpha,p55,TAC antigen 96T
U0229b CLIA Bos taurus,Bovine,IL-2 receptor subunit alpha,IL-2R subunit alpha,IL2RA,IL-2-RA,IL2-RA,Interleukin-2 receptor subunit alpha,p55,TAC antigen 96T
E2031m ELISA kit IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Mouse,Mus musculus 96T
U2031r CLIA IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Rat,Rattus norvegicus 96T
E2031m ELISA IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Mouse,Mus musculus 96T
E1815r ELISA IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Rat,Rattus norvegicus 96T
U1815m CLIA kit IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Mouse,Mus musculus 96T
U1815r CLIA kit IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Rat,Rattus norvegicus 96T
E2031r ELISA IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Rat,Rattus norvegicus 96T
E1815r ELISA kit IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Rat,Rattus norvegicus 96T
U1815m CLIA IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Mouse,Mus musculus 96T
E2031r ELISA kit IL-4 receptor subunit alpha,Il4r,IL-4R subunit alpha,Il4ra,IL-4RA,IL-4R-alpha,Interleukin-4 receptor subunit alpha,Rat,Rattus norvegicus 96T
U1815r CLIA IL-6 receptor subunit alpha,Il6r,IL-6R 1,IL-6R subunit alpha,Il6ra,IL-6RA,IL-6R-alpha,Interleukin-6 receptor subunit alpha,Rat,Rattus norvegicus 96T


 

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