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Low affinity immunoglobulin epsilon Fc receptor (BLAST-2) (C-type lectin domain family 4 member J) (Fc-epsilon-RII) (Immunoglobulin E-binding factor) (Lymphocyte IgE receptor) (CD antigen CD23) [Cleaved into: Low affinity immunoglobulin epsilon Fc receptor membrane-bound form; Low affinity immunoglobulin epsilon Fc receptor soluble form]

 FCER2_HUMAN             Reviewed;         321 AA.
P06734;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
25-OCT-2017, entry version 190.
RecName: Full=Low affinity immunoglobulin epsilon Fc receptor;
AltName: Full=BLAST-2;
AltName: Full=C-type lectin domain family 4 member J;
AltName: Full=Fc-epsilon-RII;
AltName: Full=Immunoglobulin E-binding factor;
AltName: Full=Lymphocyte IgE receptor;
AltName: CD_antigen=CD23;
Contains:
RecName: Full=Low affinity immunoglobulin epsilon Fc receptor membrane-bound form;
Contains:
RecName: Full=Low affinity immunoglobulin epsilon Fc receptor soluble form;
Name=FCER2; Synonyms=CD23A, CLEC4J, FCE2, IGEBF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2949326; DOI=10.1073/pnas.84.3.819;
Ikuta K., Takami M., Kim C.W., Honjo T., Miyoshi T., Tagaya Y.,
Kawabe T., Yodoi J.;
"Human lymphocyte Fc receptor for IgE: sequence homology of its cloned
cDNA with animal lectins.";
Proc. Natl. Acad. Sci. U.S.A. 84:819-823(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2877743; DOI=10.1016/0092-8674(86)90508-8;
Kikutani H., Inui S., Sato R., Barsumian E.L., Owaki H., Yamasaki K.,
Kaisho T., Uchibayashi N., Hardy R.R., Hirano T., Tsunasawa S.,
Sakiyama F., Suemura M., Kishimoto T.;
"Molecular structure of human lymphocyte receptor for immunoglobulin
E.";
Cell 47:657-665(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3034567;
Luedin C., Hofstetter H., Sarfati M., Levy C.A., Suter U., Alaimo D.,
Kilchherr E., Frost H., Delespesse G.;
"Cloning and expression of the cDNA coding for a human lymphocyte IgE
receptor.";
EMBO J. 6:109-114(1987).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=B-cell, and Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2972386; DOI=10.1016/0092-8674(88)90219-X;
Yokota A., Kikutani H., Tanaka T., Sato R., Barsumian E.L.,
Suemura M., Kishimoto T.;
"Two species of human Fc epsilon receptor II (Fc epsilon RII/CD23):
tissue-specific and IL-4-specific regulation of gene expression.";
Cell 55:611-618(1988).
[7]
PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
PubMed=1417742; DOI=10.1042/bj2860819;
Rose K., Turcatti G., Graber P., Pochon S., Regamey P.-O.,
Jansen K.U., Magnenat E., Aubonney N., Bonnefoy J.-Y.;
"Partial characterization of natural and recombinant human soluble
CD23.";
Biochem. J. 286:819-824(1992).
[8]
SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE BY ADAM10.
PubMed=17389606; DOI=10.1074/jbc.M608414200;
Lemieux G.A., Blumenkron F., Yeung N., Zhou P., Williams J.,
Grammer A.C., Petrovich R., Lipsky P.E., Moss M.L., Werb Z.;
"The low affinity IgE receptor (CD23) is cleaved by the
metalloproteinase ADAM10.";
J. Biol. Chem. 282:14836-14844(2007).
[9]
PALMITOYLATION AT CYS-17 AND CYS-18, AND SUBCELLULAR LOCATION.
TISSUE=B-cell;
PubMed=22615937; DOI=10.1371/journal.pone.0037187;
Ivaldi C., Martin B.R., Kieffer-Jaquinod S., Chapel A., Levade T.,
Garin J., Journet A.;
"Proteomic analysis of S-acylated proteins in human B cells reveals
palmitoylation of the immune regulators CD20 and CD23.";
PLoS ONE 7:E37187-E37187(2012).
[10]
3D-STRUCTURE MODELING OF LECTIN DOMAIN.
PubMed=8142907;
Padlan E.A., Helm B.A.;
"Modeling of the lectin-homology domains of the human and murine low-
affinity Fc epsilon receptor (Fc epsilon RII/CD23).";
Receptor 3:325-341(1993).
[11]
3D-STRUCTURE MODELING OF 173-285.
PubMed=8745401; DOI=10.1002/pro.5560050207;
Bajorath J., Aruffo A.;
"Structure-based modeling of the ligand binding domain of the human
cell surface receptor CD23 and comparison of two independently derived
molecular models.";
Protein Sci. 5:240-247(1996).
[12]
STRUCTURE BY NMR OF 156-298, DISULFIDE BONDS, AND SUBUNIT.
PubMed=16172256; DOI=10.1084/jem.20050811;
Hibbert R.G., Teriete P., Grundy G.J., Beavil R.L., Reljic R.,
Holers V.M., Hannan J.P., Sutton B.J., Gould H.J., McDonnell J.M.;
"The structure of human CD23 and its interactions with IgE and CD21.";
J. Exp. Med. 202:751-760(2005).
[13]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 150-321 ALONE AND IN COMPLEX
WITH CALCIUM, AND DISULFIDE BONDS.
PubMed=16765898; DOI=10.1016/j.str.2006.03.017;
Wurzburg B.A., Tarchevskaya S.S., Jardetzky T.S.;
"Structural changes in the lectin domain of CD23, the low-affinity IgE
receptor, upon calcium binding.";
Structure 14:1049-1058(2006).
[14]
VARIANT PHE-316.
PubMed=23424103; DOI=10.1002/ana.23832;
Hersheson J., Mencacci N.E., Davis M., Macdonald N., Trabzuni D.,
Ryten M., Pittman A., Paudel R., Kara E., Fawcett K., Plagnol V.,
Bhatia K.P., Medlar A.J., Stanescu H.C., Hardy J., Kleta R.,
Wood N.W., Houlden H.;
"Mutations in the autoregulatory domain of beta-tubulin 4a cause
hereditary dystonia.";
Ann. Neurol. 73:546-553(2013).
-!- FUNCTION: Low-affinity receptor for immunoglobulin E (IgE) and
CR2/CD21. Has essential roles in the regulation of IgE production
and in the differentiation of B-cells (it is a B-cell-specific
antigen).
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:16172256,
ECO:0000269|PubMed:16765898}.
-!- INTERACTION:
P17544:ATF7; NbExp=3; IntAct=EBI-10199985, EBI-765623;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
protein. Cell membrane; Lipid-anchor. Secreted. Note=Also exists
as a soluble excreted form, sCD23.
-!- PTM: N- and O-glycosylated.
-!- PTM: The secreted form sCD23 is produced by ADAM10-mediated
ectodomain shedding.
-!- MISCELLANEOUS: There are two kinds of Fc receptors for IgE, which
differ in both structure and function: high affinity receptors on
basophils and mast cells and low affinity receptors on lymphocytes
and monocytes.
-!- SEQUENCE CAUTION:
Sequence=AAA52433.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=CD23;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_221";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FCER2ID44222ch19p13.html";
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EMBL; M15059; AAA52434.1; -; mRNA.
EMBL; M14766; AAA52435.1; -; mRNA.
EMBL; X04772; CAA28465.1; -; mRNA.
EMBL; AC008763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014108; AAH14108.1; -; mRNA.
EMBL; BC062591; AAH62591.1; -; mRNA.
EMBL; M23562; AAA52433.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS12184.1; -.
PIR; A26067; LNHUER.
RefSeq; NP_001193948.2; NM_001207019.2.
RefSeq; NP_001207429.1; NM_001220500.1.
RefSeq; NP_001993.2; NM_002002.4.
RefSeq; XP_005272519.1; XM_005272462.4.
UniGene; Hs.465778; -.
PDB; 1HLI; Model; -; A=173-285.
PDB; 1KJE; Model; -; A=173-285.
PDB; 1T8C; NMR; -; A=156-298.
PDB; 1T8D; NMR; -; A=156-298.
PDB; 2H2R; X-ray; 1.50 A; A/B=150-321.
PDB; 2H2T; X-ray; 1.30 A; B=150-321.
PDB; 4EZM; X-ray; 3.10 A; G/H/I/J/K/L=156-298.
PDB; 4G96; X-ray; 2.25 A; A/B/C/D=156-298.
PDB; 4G9A; X-ray; 2.00 A; A/B/C/D=156-298.
PDB; 4GI0; X-ray; 2.27 A; A/B/C=156-298.
PDB; 4GJ0; X-ray; 1.95 A; A/B/C/D=156-298.
PDB; 4GJX; X-ray; 2.80 A; A/B/C/D/E/F/G/H=156-298.
PDB; 4GK1; X-ray; 2.24 A; A/B/C/D/E/F/G=156-298.
PDB; 4GKO; X-ray; 3.30 A; G/H/I/J/K/L=156-298.
PDB; 4J6J; X-ray; 1.90 A; A/B/C/D=156-298.
PDB; 4J6K; X-ray; 2.30 A; A/B/C/D/E/F/G/H=156-298.
PDB; 4J6L; X-ray; 3.15 A; A/B/C/D/E/F/G/H=156-298.
PDB; 4J6M; X-ray; 2.48 A; A/B/C/D/E/F/G/H=156-298.
PDB; 4J6N; X-ray; 2.85 A; A/B=156-298.
PDB; 4J6P; X-ray; 1.90 A; A/B/C/D=156-298.
PDB; 4J6Q; X-ray; 2.54 A; A=156-298.
PDB; 4KI1; X-ray; 3.20 A; E/F/G/H=156-298.
PDB; 5LGK; X-ray; 3.50 A; E/F=165-284.
PDBsum; 1HLI; -.
PDBsum; 1KJE; -.
PDBsum; 1T8C; -.
PDBsum; 1T8D; -.
PDBsum; 2H2R; -.
PDBsum; 2H2T; -.
PDBsum; 4EZM; -.
PDBsum; 4G96; -.
PDBsum; 4G9A; -.
PDBsum; 4GI0; -.
PDBsum; 4GJ0; -.
PDBsum; 4GJX; -.
PDBsum; 4GK1; -.
PDBsum; 4GKO; -.
PDBsum; 4J6J; -.
PDBsum; 4J6K; -.
PDBsum; 4J6L; -.
PDBsum; 4J6M; -.
PDBsum; 4J6N; -.
PDBsum; 4J6P; -.
PDBsum; 4J6Q; -.
PDBsum; 4KI1; -.
PDBsum; 5LGK; -.
ProteinModelPortal; P06734; -.
SMR; P06734; -.
BioGrid; 108502; 4.
CORUM; P06734; -.
IntAct; P06734; 1.
STRING; 9606.ENSP00000264072; -.
BindingDB; P06734; -.
ChEMBL; CHEMBL2940; -.
GuidetoPHARMACOLOGY; 2935; -.
PhosphoSitePlus; P06734; -.
SwissPalm; P06734; -.
BioMuta; FCER2; -.
DMDM; 119862; -.
MaxQB; P06734; -.
PaxDb; P06734; -.
PeptideAtlas; P06734; -.
PRIDE; P06734; -.
DNASU; 2208; -.
Ensembl; ENST00000346664; ENSP00000264072; ENSG00000104921.
Ensembl; ENST00000597921; ENSP00000471974; ENSG00000104921.
GeneID; 2208; -.
KEGG; hsa:2208; -.
UCSC; uc002mhm.3; human.
CTD; 2208; -.
DisGeNET; 2208; -.
EuPathDB; HostDB:ENSG00000104921.14; -.
GeneCards; FCER2; -.
HGNC; HGNC:3612; FCER2.
HPA; CAB002624; -.
HPA; HPA008928; -.
MIM; 151445; gene.
neXtProt; NX_P06734; -.
OpenTargets; ENSG00000104921; -.
PharmGKB; PA28058; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00760000118924; -.
HOGENOM; HOG000089951; -.
HOVERGEN; HBG051599; -.
InParanoid; P06734; -.
KO; K06468; -.
OMA; GQWNDAF; -.
OrthoDB; EOG091G0KN3; -.
PhylomeDB; P06734; -.
TreeFam; TF333341; -.
Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SIGNOR; P06734; -.
EvolutionaryTrace; P06734; -.
GeneWiki; CD23; -.
GenomeRNAi; 2208; -.
PMAP-CutDB; P06734; -.
PRO; PR:P06734; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104921; -.
CleanEx; HS_FCER2; -.
ExpressionAtlas; P06734; baseline and differential.
Genevisible; P06734; HS.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
GO; GO:0005178; F:integrin binding; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl.
GO; GO:0051712; P:positive regulation of killing of cells of other organism; IDA:BHF-UCL.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
CDD; cd03590; CLECT_DC-SIGN_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR033989; CD209-like_CTLD.
InterPro; IPR016187; CTDL_fold.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
3D-structure; Calcium; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
IgE-binding protein; Lectin; Lipoprotein; Membrane; Metal-binding;
Palmitate; Polymorphism; Receptor; Reference proteome; Repeat;
Secreted; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 321 Low affinity immunoglobulin epsilon Fc
receptor membrane-bound form.
/FTId=PRO_0000017391.
CHAIN 150 321 Low affinity immunoglobulin epsilon Fc
receptor soluble form.
/FTId=PRO_0000017392.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.
TRANSMEM 22 47 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 48 321 Extracellular. {ECO:0000255}.
REPEAT 69 89
REPEAT 90 110
REPEAT 111 131
DOMAIN 162 284 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
METAL 249 249 Calcium. {ECO:0000269|PubMed:16765898}.
METAL 251 251 Calcium. {ECO:0000269|PubMed:16765898}.
METAL 269 269 Calcium. {ECO:0000269|PubMed:16765898}.
METAL 270 270 Calcium. {ECO:0000269|PubMed:16765898}.
SITE 149 150 Cleavage.
LIPID 17 17 S-palmitoyl cysteine.
{ECO:0000269|PubMed:22615937}.
LIPID 18 18 S-palmitoyl cysteine.
{ECO:0000269|PubMed:22615937}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 160 288
DISULFID 163 174
DISULFID 191 282
DISULFID 259 273
VARIANT 62 62 R -> W (in dbSNP:rs2228137).
/FTId=VAR_035387.
VARIANT 284 284 R -> Q (in dbSNP:rs8102872).
/FTId=VAR_035388.
VARIANT 316 316 S -> F. {ECO:0000269|PubMed:23424103}.
/FTId=VAR_069800.
CONFLICT 269 269 N -> T (in Ref. 3; CAA28465).
{ECO:0000305}.
STRAND 159 162 {ECO:0000244|PDB:2H2R}.
STRAND 164 166 {ECO:0000244|PDB:1T8C}.
STRAND 168 170 {ECO:0000244|PDB:2H2T}.
STRAND 173 182 {ECO:0000244|PDB:2H2T}.
HELIX 184 193 {ECO:0000244|PDB:2H2T}.
STRAND 196 198 {ECO:0000244|PDB:4J6N}.
HELIX 204 211 {ECO:0000244|PDB:2H2T}.
STRAND 215 217 {ECO:0000244|PDB:1T8C}.
STRAND 219 226 {ECO:0000244|PDB:2H2T}.
TURN 227 230 {ECO:0000244|PDB:2H2T}.
STRAND 231 234 {ECO:0000244|PDB:2H2T}.
TURN 247 252 {ECO:0000244|PDB:4GK1}.
STRAND 253 256 {ECO:0000244|PDB:4J6N}.
STRAND 259 262 {ECO:0000244|PDB:2H2T}.
TURN 264 266 {ECO:0000244|PDB:1T8C}.
STRAND 268 271 {ECO:0000244|PDB:2H2T}.
STRAND 277 285 {ECO:0000244|PDB:2H2T}.
STRAND 287 289 {ECO:0000244|PDB:2H2R}.
STRAND 291 294 {ECO:0000244|PDB:1T8C}.
SEQUENCE 321 AA; 36469 MW; F86708C0E6515B87 CRC64;
MEEGQYSEIE ELPRRRCCRR GTQIVLLGLV TAALWAGLLT LLLLWHWDTT QSLKQLEERA
ARNVSQVSKN LESHHGDQMA QKSQSTQISQ ELEELRAEQQ RLKSQDLELS WNLNGLQADL
SSFKSQELNE RNEASDLLER LREEVTKLRM ELQVSSGFVC NTCPEKWINF QRKCYYFGKG
TKQWVHARYA CDDMEGQLVS IHSPEEQDFL TKHASHTGSW IGLRNLDLKG EFIWVDGSHV
DYSNWAPGEP TSRSQGEDCV MMRGSGRWND AFCDRKLGAW VCDRLATCTP PASEGSAESM
GPDSRPDPDG RLPTPSAPLH S


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18-272-196580 CD23 - Rabbit polyclonal to CD23; Lymphocyte IgE receptor; Fc-epsilon-RII; BLAST-2; Immunoglobulin E-binding factor; CD23 antigen Polyclonal 0.5 ml
20-272-191417 CD23 - Mouse monoclonal [1B12] to CD23; Lymphocyte IgE receptor; Fc-epsilon-RII; BLAST-2; Immunoglobulin E-binding factor; CD23 antigen Monoclonal 0.5 ml
20-272-190181 CD23 - Mouse monoclonal [LT23] to CD23; Lymphocyte IgE receptor; Fc-epsilon-RII; BLAST-2; Immunoglobulin E-binding factor; CD23 antigen Monoclonal 0.1 mg
20-272-191325 CD23 - Rabbit monoclonal [SP23] to CD23; Lymphocyte IgE receptor; Fc-epsilon-RII; BLAST-2; Immunoglobulin E-binding factor; CD23 antigen Monoclonal 0.5 ml
E1891h ELISA kit APY,Fc epsilon receptor I beta-chain,FCER1B,FcERI,High affinity immunoglobulin epsilon receptor subunit beta,Homo sapiens,Human,IgE Fc receptor subunit beta,IGER,Membrane-spanning 4-domains 96T
U1891h CLIA kit APY,Fc epsilon receptor I beta-chain,FCER1B,FcERI,High affinity immunoglobulin epsilon receptor subunit beta,Homo sapiens,Human,IgE Fc receptor subunit beta,IGER,Membrane-spanning 4-domains 96T
U1891h CLIA APY,Fc epsilon receptor I beta-chain,FCER1B,FcERI,High affinity immunoglobulin epsilon receptor subunit beta,Homo sapiens,Human,IgE Fc receptor subunit beta,IGER,Membrane-spanning 4-domains subfa 96T
E1891h ELISA APY,Fc epsilon receptor I beta-chain,FCER1B,FcERI,High affinity immunoglobulin epsilon receptor subunit beta,Homo sapiens,Human,IgE Fc receptor subunit beta,IGER,Membrane-spanning 4-domains subf 96T
20-272-191412 CD23. prediluted - Mouse monoclonal [MHM6] to CD23. prediluted; Lymphocyte IgE receptor; Fc-epsilon-RII; BLAST-2; Immunoglobulin E-binding factor; CD23 antigen Monoclonal 6 ml
EIAAB14647 FCE1A,Fc-epsilon RI-alpha,FCER1A,FcERI,High affinity immunoglobulin epsilon receptor subunit alpha,Homo sapiens,Human,IgE Fc receptor subunit alpha


 

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