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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)]

 IL4RA_MOUSE             Reviewed;         810 AA.
P16382; O54690; Q60583; Q8CBW5;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
20-JUN-2018, entry version 180.
RecName: Full=Interleukin-4 receptor subunit alpha;
Short=IL-4 receptor subunit alpha;
Short=IL-4R subunit alpha;
Short=IL-4R-alpha;
Short=IL-4RA;
AltName: CD_antigen=CD124;
Contains:
RecName: Full=Soluble interleukin-4 receptor subunit alpha;
Short=Soluble IL-4 receptor subunit alpha;
Short=Soluble IL-4R-alpha;
Short=sIL4Ralpha/prot;
AltName: Full=IL-4-binding protein;
Short=IL4-BP;
Flags: Precursor;
Name=Il4r; Synonyms=Il4ra;
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] (ISOFORMS 1; 2 AND 3), AND PROTEIN SEQUENCE
OF 26-39; 162-179 AND 194-210.
STRAIN=C57BL/6J; TISSUE=T-cell;
PubMed=2805066; DOI=10.1016/0092-8674(89)90295-X;
Mosley B., Beckmann M.P., March C.J., Idzerda R.L., Gimpel S.D.,
VandenBos T., Friend D., Alpert A., Anderson D., Jackson J.,
Wignall J.M., Smith C., Gallis B., Sims J.E., Urdal D., Widmer M.B.,
Cosman D., Park L.S.;
"The murine interleukin-4 receptor: molecular cloning and
characterization of secreted and membrane bound forms.";
Cell 59:335-348(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Mast cell;
PubMed=2405398; DOI=10.1073/pnas.87.3.857;
Harada N., Castle B.E., Gorman D.M., Itoh N., Schreurs J.,
Barrett R.L., Howard M., Miyajima A.;
"Expression cloning of a cDNA encoding the murine interleukin 4
receptor based on ligand binding.";
Proc. Natl. Acad. Sci. U.S.A. 87:857-861(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Sperm;
PubMed=1534014; DOI=10.3109/08977199209011014;
Wrighton N., Campbell L.A., Harada N., Miyajima A., Lee F.;
"The murine interleukin-4 receptor gene: genomic structure, expression
and potential for alternative splicing.";
Growth Factors 6:103-118(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION OF
VARIANT ILE-74.
STRAIN=AKR/J, BALB/cJ, C3H/HeN, C57BL/6J, CB-17/SCID, CBA/J, DBA/2J,
FVB/N, and SJL/J;
PubMed=9348299; DOI=10.1084/jem.186.9.1419;
Schulte T., Kurrle R., Roellinghoff M., Gessner A.;
"Molecular characterization and functional analysis of murine
interleukin 4 receptor allotypes.";
J. Exp. Med. 186:1419-1429(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Diencephalon, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
INTERACTION WITH JAK1 AND SOCS5.
PubMed=12242343; DOI=10.1073/pnas.202477099;
Seki Y., Hayashi K., Matsumoto A., Seki N., Tsukada J., Ransom J.,
Naka T., Kishimoto T., Yoshimura A., Kubo M.;
"Expression of the suppressor of cytokine signaling-5 (SOCS5)
negatively regulates IL-4-dependent STAT6 activation and Th2
differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 99:13003-13008(2002).
[7]
PHOSPHORYLATION, AND INTERACTION WITH PIK3C3.
PubMed=8390454;
Izuhara K., Harada N.;
"Interleukin-4 (IL-4) induces protein tyrosine phosphorylation of the
IL-4 receptor and association of phosphatidylinositol 3-kinase to the
IL-4 receptor in a mouse T cell line, HT2.";
J. Biol. Chem. 268:13097-13102(1993).
[8]
PROTEOLYTIC PROCESSING.
PubMed=8757301;
Blum H., Wolf M., Enssle K., Roellinghoff M., Gessner A.;
"Two distinct stimulus-dependent pathways lead to production of
soluble murine interleukin-4 receptor.";
J. Immunol. 157:1846-1853(1996).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND 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).
[10]
TISSUE SPECIFICITY, AND INTERACTION WITH CLM1.
PubMed=26124135; DOI=10.1073/pnas.1507625112;
Moshkovits I., Karo-Atar D., Itan M., Reichman H., Rozenberg P.,
Morgenstern-Ben-Baruch N., Shik D., Ejarque-Ortiz A., Hershko A.Y.,
Tian L., Coligan J.E., Sayos J., Munitz A.;
"CD300f associates with IL-4 receptor alpha and amplifies IL-4-induced
immune cell responses.";
Proc. Natl. Acad. Sci. U.S.A. 112:8708-8713(2015).
-!- FUNCTION: Receptor for both interleukin 4 and interleukin 13.
Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is
involved in promoting Th2 differentiation. The IL4/IL13 responses
are involved in regulating IgE production and, chemokine and mucus
production at sites of allergic inflammation. In certain cell
types, can signal through activation of insulin receptor
substrates, IRS1/IRS2.
-!- SUBUNIT: The functional IL4 receptor is formed by initial binding
of IL4 to IL4R. Subsequent recruitment to the complex of the
common gamma chain, in immune cells, creates a type I receptor
and, in non-immune cells, of IL13RA1 forms a type II receptor.
IL4R can also interact with the IL13/IL13RA1 complex to form a
similar type II receptor. Interacts with the SH2-containing
phosphatases, PTPN6/SHIP1, PTPN11/SHIP2 and INPP5D/SHIP. Interacts
with JAK3 (By similarity). Interacts with PIK3C3 (PubMed:8390454).
Interacts with JAK1 through a Box 1-containing region; inhibited
by SOCS5 (PubMed:12242343). Interacts with SOCS5; inhibits IL4
signaling (PubMed:12242343). Interacts with CLM1
(PubMed:26124135). {ECO:0000250|UniProtKB:P24394,
ECO:0000269|PubMed:12242343, ECO:0000269|PubMed:26124135,
ECO:0000269|PubMed:8390454}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Membrane;
IsoId=P16382-1; Sequence=Displayed;
Note=Binds IL-4.;
Name=2; Synonyms=Secreted;
IsoId=P16382-2; Sequence=VSP_001675, VSP_001676;
Note=Binds IL-4.;
Name=3;
IsoId=P16382-3; Sequence=VSP_001677;
Note=Lacks the cytoplasmic domain. Binds IL4.;
-!- TISSUE SPECIFICITY: Expressed in both Th1 and Th2 cells.
-!- DOMAIN: The extracellular domain represents the IL4 binding
protein (IL4BP). {ECO:0000250}.
-!- 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.
-!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to
as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This
motif is involved in modulation of cellular responses. The
phosphorylated ITIM motif can bind the SH2 domain of several SH2-
containing phosphatases.
-!- PTM: On IL4 binding, phosphorylated on C-terminal tyrosine
residues. {ECO:0000250|UniProtKB:P24394}.
-!- PTM: Soluble IL4R can also be produced by proteolytic cleavage at
the cell surface (shedding). {ECO:0000269|PubMed:8757301}.
-!- MISCELLANEOUS: The sequences from strains C3H, CBA, DBA/2 and
FVB/N are all identical to the one displayed.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
subfamily. {ECO:0000305}.
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EMBL; M27959; AAA39299.1; -; mRNA.
EMBL; M27960; AAA39300.1; -; mRNA.
EMBL; M29854; AAA39297.1; -; mRNA.
EMBL; M64879; AAB59727.1; -; Genomic_DNA.
EMBL; M64870; AAB59727.1; JOINED; Genomic_DNA.
EMBL; M64871; AAB59727.1; JOINED; Genomic_DNA.
EMBL; M64872; AAB59727.1; JOINED; Genomic_DNA.
EMBL; M64873; AAB59727.1; JOINED; Genomic_DNA.
EMBL; M64874; AAB59727.1; JOINED; Genomic_DNA.
EMBL; M64876; AAB59727.1; JOINED; Genomic_DNA.
EMBL; M64877; AAB59727.1; JOINED; Genomic_DNA.
EMBL; M64878; AAB59727.1; JOINED; Genomic_DNA.
EMBL; AF000304; AAB87750.1; -; mRNA.
EMBL; AK034466; BAC28718.1; -; mRNA.
EMBL; AK088086; BAC40137.1; -; mRNA.
CCDS; CCDS40121.1; -. [P16382-1]
PIR; A33380; A33380.
RefSeq; NP_001008700.1; NM_001008700.3. [P16382-1]
UniGene; Mm.233802; -.
ProteinModelPortal; P16382; -.
SMR; P16382; -.
BioGrid; 200638; 3.
DIP; DIP-1168N; -.
STRING; 10090.ENSMUSP00000033004; -.
iPTMnet; P16382; -.
PhosphoSitePlus; P16382; -.
EPD; P16382; -.
PaxDb; P16382; -.
PRIDE; P16382; -.
Ensembl; ENSMUST00000033004; ENSMUSP00000033004; ENSMUSG00000030748. [P16382-1]
Ensembl; ENSMUST00000206846; ENSMUSP00000145824; ENSMUSG00000030748. [P16382-2]
GeneID; 16190; -.
KEGG; mmu:16190; -.
UCSC; uc009jqc.1; mouse. [P16382-1]
CTD; 16190; -.
MGI; MGI:105367; Il4ra.
eggNOG; ENOG410IGBQ; Eukaryota.
eggNOG; ENOG41124QC; LUCA.
GeneTree; ENSGT00510000049182; -.
HOGENOM; HOG000090263; -.
HOVERGEN; HBG052116; -.
InParanoid; P16382; -.
KO; K05071; -.
OMA; ASPCCGC; -.
OrthoDB; EOG091G010H; -.
PhylomeDB; P16382; -.
TreeFam; TF337996; -.
Reactome; R-MMU-6785807; Interleukin-4 and 13 signaling.
PRO; PR:P16382; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030748; -.
CleanEx; MM_IL4RA; -.
ExpressionAtlas; P16382; baseline and differential.
Genevisible; P16382; MM.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
GO; GO:0045626; P:negative regulation of T-helper 1 cell differentiation; IGI:MGI.
GO; GO:0090197; P:positive regulation of chemokine secretion; IMP:BHF-UCL.
GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:MGI.
GO; GO:0043032; P:positive regulation of macrophage activation; IMP:BHF-UCL.
GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:MGI.
GO; GO:1901741; P:positive regulation of myoblast fusion; IMP:MGI.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IGI:MGI.
GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IEA:InterPro.
GO; GO:0042127; P:regulation of cell proliferation; ISO:MGI.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR015319; IL-4_rcpt-alpha_N.
Pfam; PF09238; IL4Ra_N; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 1.
PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000269|PubMed:2805066}.
CHAIN 26 810 Interleukin-4 receptor subunit alpha.
/FTId=PRO_0000010889.
CHAIN 26 ? Soluble interleukin-4 receptor subunit
alpha.
/FTId=PRO_0000010890.
TOPO_DOM 26 233 Extracellular. {ECO:0000255}.
TRANSMEM 234 257 Helical. {ECO:0000255}.
TOPO_DOM 258 810 Cytoplasmic. {ECO:0000255}.
DOMAIN 126 224 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 441 557 Required for IRS1 activation and IL4-
induced cell growth. {ECO:0000250}.
REGION 557 653 Required for IL4-induced gene expression.
{ECO:0000250}.
MOTIF 213 217 WSXWS motif.
MOTIF 263 271 Box 1 motif.
MOTIF 707 712 ITIM motif.
COMPBIAS 376 381 Poly-Glu.
COMPBIAS 527 530 Poly-Glu.
MOD_RES 165 165 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 500 500 Phosphotyrosine.
{ECO:0000250|UniProtKB:P24394}.
MOD_RES 575 575 Phosphotyrosine.
{ECO:0000250|UniProtKB:P24394}.
MOD_RES 603 603 Phosphotyrosine.
{ECO:0000250|UniProtKB:P24394}.
MOD_RES 631 631 Phosphotyrosine.
{ECO:0000250|UniProtKB:P24394}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 163 163 N-linked (GlcNAc...) asparagine.
DISULFID 34 44 {ECO:0000250}.
DISULFID 75 87 {ECO:0000250}.
VAR_SEQ 225 230 HFQLPL -> PSNENL (in isoform 2).
{ECO:0000303|PubMed:2805066}.
/FTId=VSP_001675.
VAR_SEQ 231 810 Missing (in isoform 2).
{ECO:0000303|PubMed:2805066}.
/FTId=VSP_001676.
VAR_SEQ 258 810 Missing (in isoform 3).
{ECO:0000303|PubMed:2805066}.
/FTId=VSP_001677.
VARIANT 59 59 C -> R (in strain: BALB/c, AKR/J and SJL/
J).
VARIANT 74 74 T -> I (in strain: BALB/c, AKR/J and SJL/
J; reduced IL4-neutralizing capacity of
soluble form).
{ECO:0000269|PubMed:9348299}.
VARIANT 193 193 M -> T (in strain: BALB/c, AKR/J and SJL/
J).
VARIANT 334 334 L -> P (in strain: BALB/c, AKR/J and SJL/
J).
VARIANT 374 374 N -> S (in strain: BALB/c, AKR/J and SJL/
J).
VARIANT 382 382 I -> M (in strain: BALB/c, AKR/J and SJL/
J).
VARIANT 472 472 G -> D (in strain: BALB/c, AKR/J and SJL/
J).
VARIANT 626 626 D -> G (in strain: BALB/c, AKR/J and SJL/
J).
CONFLICT 436 436 S -> C (in Ref. 5; BAC28718).
{ECO:0000305}.
SEQUENCE 810 AA; 87627 MW; 536B9E01E938FF6D CRC64;
MGRLCTKFLT SVGCLILLLV TGSGSIKVLG EPTCFSDYIR TSTCEWFLDS AVDCSSQLCL
HYRLMFFEFS ENLTCIPRNS ASTVCVCHME MNRPVQSDRY QMELWAEHRQ LWQGSFSPSG
NVKPLAPDNL TLHTNVSDEW LLTWNNLYPS NNLLYKDLIS MVNISREDNP AEFIVYNVTY
KEPRLSFPIN ILMSGVYYTA RVRVRSQILT GTWSEWSPSI TWYNHFQLPL IQRLPLGVTI
SCLCIPLFCL FCYFSITKIK KIWWDQIPTP ARSPLVAIII QDAQVPLWDK QTRSQESTKY
PHWKTCLDKL LPCLLKHRVK KKTDFPKAAP TKSLQSPGKA GWCPMEVSRT VLWPENVSVS
VVRCMELFEA PVQNVEEEED EIVKEDLSMS PENSGGCGFQ ESQADIMARL TENLFSDLLE
AENGGLGQSA LAESCSPLPS GSGQASVSWA CLPMGPSEEA TCQVTEQPSH PGPLSGSPAQ
SAPTLACTQV PLVLADNPAY RSFSDCCSPA PNPGELAPEQ QQADHLEEEE PPSPADPHSS
GPPMQPVESW EQILHMSVLQ HGAAAGSTPA PAGGYQEFVQ AVKQGAAQDP GVPGVRPSGD
PGYKAFSSLL SSNGIRGDTA AAGTDDGHGG YKPFQNPVPN QSPSSVPLFT FGLDTELSPS
PLNSDPPKSP PECLGLELGL KGGDWVKAPP PADQVPKPFG DDLGFGIVYS SLTCHLCGHL
KQHHSQEEGG QSPIVASPGC GCCYDDRSPS LGSLSGALES CPEGIPPEAN LMSAPKTPSN
LSGEGKGPGH SPVPSQTTEV PVGALGIAVS


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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
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 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
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
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
U2031m CLIA 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
U2031r CLIA 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
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


 

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