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Interleukin-18 receptor accessory protein (IL-18 receptor accessory protein) (IL-18RAcP) (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)

 I18RA_HUMAN             Reviewed;         599 AA.
O95256; B2RPJ3; Q2QDE5; Q3KPE7; Q3KPE8; Q53TT4; Q53TU5;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
13-NOV-2019, entry version 167.
RecName: Full=Interleukin-18 receptor accessory protein;
Short=IL-18 receptor accessory protein;
Short=IL-18RAcP;
AltName: Full=Accessory protein-like;
Short=AcPL;
AltName: Full=CD218 antigen-like family member B;
AltName: Full=CDw218b;
AltName: Full=IL-1R accessory protein-like {ECO:0000303|PubMed:10653850};
Short=IL-1RAcPL;
AltName: Full=Interleukin-1 receptor 7;
Short=IL-1R-7;
Short=IL-1R7;
AltName: Full=Interleukin-18 receptor accessory protein-like;
AltName: Full=Interleukin-18 receptor beta {ECO:0000303|PubMed:10653850, ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25500532};
Short=IL-18R-beta;
Short=IL-18Rbeta {ECO:0000303|PubMed:10653850, ECO:0000303|PubMed:14528293, ECO:0000303|PubMed:25500532};
AltName: CD_antigen=CD218b;
Flags: Precursor;
Name=IL18RAP {ECO:0000312|HGNC:HGNC:5989}; Synonyms=IL1R7;
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), FUNCTION, SUBUNIT, AND TISSUE
SPECIFICITY.
PubMed=9792649; DOI=10.1074/jbc.273.45.29445;
Born T.L., Thomassen E., Bird T.A., Sims J.E.;
"Cloning of a novel receptor subunit, AcPL, required for interleukin-
18 signaling.";
J. Biol. Chem. 273:29445-29450(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND TISSUE SPECIFICITY.
PubMed=17897836; DOI=10.1016/j.cyto.2007.07.186;
Fiszer D., Rozwadowska N., Rychlewski L., Kosicki W., Kurpisz M.;
"Identification of IL-18RAP mRNA truncated splice variants in human
testis and the other human tissues.";
Cytokine 39:178-183(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K.,
Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y.,
Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M.,
Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.;
"NEDO human cDNA sequencing project focused on splicing variants.";
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
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).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10653850; DOI=10.1093/intimm/12.2.151;
Tominaga K., Yoshimoto T., Torigoe K., Kurimoto M., Matsui K.,
Hada T., Okamura H., Nakanishi K.;
"IL-12 synergizes with IL-18 or IL-1beta for IFN-gamma production from
human T cells.";
Int. Immunol. 12:151-160(2000).
[8]
TISSUE SPECIFICITY, AND INDUCTION BY IFN-ALPHA AND
IL12/INTERLEUKIN-12.
PubMed=10925275; DOI=10.4049/jimmunol.165.4.1933;
Sareneva T., Julkunen I., Matikainen S.;
"IFN-alpha and IL-12 induce IL-18 receptor gene expression in human NK
and T cells.";
J. Immunol. 165:1933-1938(2000).
[9]
TISSUE SPECIFICITY.
PubMed=11046021; DOI=10.4049/jimmunol.165.9.4950;
Debets R., Timans J.C., Churakowa T., Zurawski S., de Waal Malefyt R.,
Moore K.W., Abrams J.S., O'Garra A., Bazan J.F., Kastelein R.A.;
"IL-18 receptors, their role in ligand binding and function: anti-IL-
1RAcPL antibody, a potent antagonist of IL-18.";
J. Immunol. 165:4950-4956(2000).
[10]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=14528293; DOI=10.1038/nsb993;
Kato Z., Jee J., Shikano H., Mishima M., Ohki I., Ohnishi H., Li A.,
Hashimoto K., Matsukuma E., Omoya K., Yamamoto Y., Yoneda T., Hara T.,
Kondo N., Shirakawa M.;
"The structure and binding mode of interleukin-18.";
Nat. Struct. Biol. 10:966-971(2003).
[11]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 15-356, GLYCOSYLATION AT
ASN-119; ASN-152 AND ASN-345, DISULFIDE BONDS, MUTAGENESIS OF LEU-167;
GLU-210; TYR-212; TYR-214; LYS-313 AND 15-GLU--PRO-176, SUBUNIT, AND
FUNCTION.
PubMed=25500532; DOI=10.1038/ncomms6340;
Tsutsumi N., Kimura T., Arita K., Ariyoshi M., Ohnishi H.,
Yamamoto T., Zuo X., Maenaka K., Park E.Y., Kondo N., Shirakawa M.,
Tochio H., Kato Z.;
"The structural basis for receptor recognition of human interleukin-
18.";
Nat. Commun. 5:5340-5340(2014).
-!- FUNCTION: Within the IL18 receptor complex, does not mediate IL18-
binding, but involved in IL18-dependent signal transduction,
leading to NF-kappa-B and JNK activation (PubMed:9792649,
PubMed:14528293, PubMed:25500532). May play a role in IL18-
mediated IFNG synthesis from T-helper 1 (Th1) cells (Probable).
{ECO:0000269|PubMed:14528293, ECO:0000269|PubMed:25500532,
ECO:0000269|PubMed:9792649, ECO:0000305|PubMed:10653850}.
-!- SUBUNIT: Forms a ternary complex with IL18 and IL18R1
(PubMed:14528293, PubMed:25500532). Within this complex, IL18R1 is
involved in ligand-binding and IL18RAP in signaling leading to NF-
kappa-B and JNK activation (Probable).
{ECO:0000269|PubMed:14528293, ECO:0000269|PubMed:25500532,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14528293};
Single-pass type I membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O95256-1; Sequence=Displayed;
Name=2;
IsoId=O95256-2; Sequence=VSP_056295;
Note=No experimental confirmation available.;
Name=3; Synonyms=IL-18RAPshort {ECO:0000303|PubMed:17897836};
IsoId=O95256-3; Sequence=VSP_059116, VSP_059117;
Name=4;
IsoId=O95256-4; Sequence=VSP_059114, VSP_059115;
-!- TISSUE SPECIFICITY: Detected in adrenal gland, bone marrow, brain,
fetal brain, fetal liver, heart, kidney, lung, liver, peripheral
blood leukocytes, placenta, prostate, salivary gland, skeletal
muscle, spinal cord, testis, thymus, thyroid, trachea and uterus
(PubMed:17897836). Strongly expressed in peripheral blood
leukocytes and spleen and, to a lesser extent, in colon
(PubMed:9792649). Specifically coexpressed with IL18R1 in T-helper
1 (Th1)cells (PubMed:10925275, PubMed:11046021, PubMed:10653850).
{ECO:0000269|PubMed:10653850, ECO:0000269|PubMed:10925275,
ECO:0000269|PubMed:11046021, ECO:0000269|PubMed:17897836,
ECO:0000269|PubMed:9792649}.
-!- INDUCTION: Induced by IFN-alpha and IL12/interleukin-12 in natural
killer (NK) cells and T-cells. {ECO:0000269|PubMed:10925275}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:25500532}.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF077346; AAC72196.1; -; mRNA.
EMBL; DQ116957; AAZ52551.1; -; mRNA.
EMBL; AC007278; AAY15080.1; -; Genomic_DNA.
EMBL; AC007248; AAY15049.1; -; Genomic_DNA.
EMBL; CH471127; EAX01791.1; -; Genomic_DNA.
EMBL; AK300026; BAG61837.1; -; mRNA.
EMBL; BC069630; AAH69630.1; -; mRNA.
EMBL; BC106764; AAI06765.1; -; mRNA.
EMBL; BC106765; AAI06766.1; -; mRNA.
EMBL; BC137474; AAI37475.1; -; mRNA.
EMBL; BC137475; AAI37476.1; -; mRNA.
CCDS; CCDS2061.1; -. [O95256-1]
RefSeq; NP_003844.1; NM_003853.3. [O95256-1]
RefSeq; XP_011510389.1; XM_011512087.2. [O95256-2]
RefSeq; XP_011510390.1; XM_011512088.2. [O95256-2]
PDB; 3WO4; X-ray; 3.10 A; C=15-356.
PDBsum; 3WO4; -.
SMR; O95256; -.
BioGrid; 114335; 3.
IntAct; O95256; 4.
STRING; 9606.ENSP00000264260; -.
iPTMnet; O95256; -.
PhosphoSitePlus; O95256; -.
BioMuta; IL18RAP; -.
PaxDb; O95256; -.
PeptideAtlas; O95256; -.
PRIDE; O95256; -.
ProteomicsDB; 50750; -. [O95256-1]
ProteomicsDB; 61717; -.
Ensembl; ENST00000264260; ENSP00000264260; ENSG00000115607. [O95256-1]
Ensembl; ENST00000409369; ENSP00000387201; ENSG00000115607. [O95256-2]
GeneID; 8807; -.
KEGG; hsa:8807; -.
UCSC; uc002tbx.4; human. [O95256-1]
CTD; 8807; -.
DisGeNET; 8807; -.
GeneCards; IL18RAP; -.
HGNC; HGNC:5989; IL18RAP.
HPA; CAB025270; -.
MIM; 604509; gene.
neXtProt; NX_O95256; -.
OpenTargets; ENSG00000115607; -.
PharmGKB; PA29805; -.
eggNOG; ENOG410IGUG; Eukaryota.
eggNOG; ENOG410Y9SN; LUCA.
GeneTree; ENSGT00960000186586; -.
HOGENOM; HOG000060101; -.
InParanoid; O95256; -.
KO; K05174; -.
OMA; PTVTWRG; -.
OrthoDB; 985064at2759; -.
PhylomeDB; O95256; -.
TreeFam; TF325519; -.
Reactome; R-HSA-9012546; Interleukin-18 signaling.
GeneWiki; IL18RAP; -.
GenomeRNAi; 8807; -.
Pharos; O95256; -.
PRO; PR:O95256; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115607; Expressed in 112 organ(s), highest expression level in bone marrow.
ExpressionAtlas; O95256; baseline and differential.
Genevisible; O95256; HS.
GO; GO:0045092; C:interleukin-18 receptor complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042008; F:interleukin-18 receptor activity; IDA:UniProtKB.
GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0032609; P:interferon-gamma production; IEA:Ensembl.
GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0032635; P:interleukin-6 production; IEA:Ensembl.
GO; GO:0042119; P:neutrophil activation; IEA:Ensembl.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0035744; P:T-helper 1 cell cytokine production; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR041416; Ig_6.
InterPro; IPR003599; Ig_sub.
InterPro; IPR015621; IL-1_rcpt_fam.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF13895; Ig_2; 1.
Pfam; PF18452; Ig_6; 1.
Pfam; PF01582; TIR; 1.
SMART; SM00409; IG; 2.
SMART; SM00255; TIR; 1.
SUPFAM; SSF48726; SSF48726; 2.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain;
Inflammatory response; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 599 Interleukin-18 receptor accessory
protein.
/FTId=PRO_0000042185.
TOPO_DOM 20 356 Extracellular. {ECO:0000255}.
TRANSMEM 357 377 Helical. {ECO:0000255}.
TOPO_DOM 378 599 Cytoplasmic. {ECO:0000255}.
DOMAIN 149 235 Ig-like C2-type 1.
DOMAIN 251 353 Ig-like C2-type 2.
DOMAIN 406 562 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
CARBOHYD 21 21 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532}.
DISULFID 46 126 {ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532}.
DISULFID 155 180 {ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532}.
DISULFID 175 221 {ECO:0000244|PDB:3WO4,
ECO:0000269|PubMed:25500532}.
DISULFID 180 221 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 273 337 {ECO:0000244|PDB:3WO4,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:25500532}.
VAR_SEQ 1 142 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056295.
VAR_SEQ 118 126 VNNSGSYIC -> LGHIFVDPR (in isoform 4).
{ECO:0000269|PubMed:17897836}.
/FTId=VSP_059114.
VAR_SEQ 127 599 Missing (in isoform 4).
{ECO:0000269|PubMed:17897836}.
/FTId=VSP_059115.
VAR_SEQ 133 149 SPYDVACCVKMILEVKP -> YDPNTFLSENISKSSII
(in isoform 3).
{ECO:0000269|PubMed:17897836}.
/FTId=VSP_059116.
VAR_SEQ 150 599 Missing (in isoform 3).
{ECO:0000269|PubMed:17897836}.
/FTId=VSP_059117.
VARIANT 350 350 V -> I (in dbSNP:rs11465716).
/FTId=VAR_034005.
MUTAGEN 15 176 Missing: Impairs IL18 receptor signaling
via NF-kappa-B.
{ECO:0000269|PubMed:25500532}.
MUTAGEN 167 167 L->A: Decreases binding to the preformed
binary complex of IL18 and IL18R1.
{ECO:0000269|PubMed:25500532}.
MUTAGEN 210 210 E->A: Decreases binding to the preformed
binary complex of IL18 and IL18R1.
Impairs IL18 receptor signaling via NF-
kappa-B; when associated with A-212 and
A-214. {ECO:0000269|PubMed:25500532}.
MUTAGEN 212 212 Y->A: Abolishes binding to the preformed
binary complex of IL18 and IL18R1.
Impairs IL18 receptor signaling via NF-
kappa-B; when associated with A-210 and
A-214. {ECO:0000269|PubMed:25500532}.
MUTAGEN 214 214 Y->A: Decreases binding to the preformed
binary complex of IL18 and IL18R1.
Impairs IL18 receptor signaling via NF-
kappa-B; when associated with A-210 and
A-212. {ECO:0000269|PubMed:25500532}.
MUTAGEN 313 313 K->A: Decreases binding to the preformed
binary complex of IL18 and IL18R1.
Decreases IL18 receptor signaling via NF-
kappa-B. {ECO:0000269|PubMed:25500532}.
STRAND 32 36 {ECO:0000244|PDB:3WO4}.
STRAND 41 44 {ECO:0000244|PDB:3WO4}.
STRAND 110 115 {ECO:0000244|PDB:3WO4}.
STRAND 117 120 {ECO:0000244|PDB:3WO4}.
STRAND 122 126 {ECO:0000244|PDB:3WO4}.
STRAND 141 149 {ECO:0000244|PDB:3WO4}.
STRAND 154 157 {ECO:0000244|PDB:3WO4}.
STRAND 161 166 {ECO:0000244|PDB:3WO4}.
STRAND 171 174 {ECO:0000244|PDB:3WO4}.
HELIX 176 178 {ECO:0000244|PDB:3WO4}.
TURN 180 183 {ECO:0000244|PDB:3WO4}.
STRAND 189 193 {ECO:0000244|PDB:3WO4}.
STRAND 203 210 {ECO:0000244|PDB:3WO4}.
HELIX 213 215 {ECO:0000244|PDB:3WO4}.
STRAND 217 224 {ECO:0000244|PDB:3WO4}.
STRAND 233 243 {ECO:0000244|PDB:3WO4}.
STRAND 252 255 {ECO:0000244|PDB:3WO4}.
STRAND 258 263 {ECO:0000244|PDB:3WO4}.
STRAND 269 278 {ECO:0000244|PDB:3WO4}.
STRAND 286 293 {ECO:0000244|PDB:3WO4}.
STRAND 296 299 {ECO:0000244|PDB:3WO4}.
STRAND 306 310 {ECO:0000244|PDB:3WO4}.
STRAND 312 325 {ECO:0000244|PDB:3WO4}.
HELIX 328 331 {ECO:0000244|PDB:3WO4}.
STRAND 333 341 {ECO:0000244|PDB:3WO4}.
STRAND 344 354 {ECO:0000244|PDB:3WO4}.
SEQUENCE 599 AA; 68310 MW; 54807DA3E05462F1 CRC64;
MLCLGWIFLW LVAGERIKGF NISGCSTKKL LWTYSTRSEE EFVLFCDLPE PQKSHFCHRN
RLSPKQVPEH LPFMGSNDLS DVQWYQQPSN GDPLEDIRKS YPHIIQDKCT LHFLTPGVNN
SGSYICRPKM IKSPYDVACC VKMILEVKPQ TNASCEYSAS HKQDLLLGST GSISCPSLSC
QSDAQSPAVT WYKNGKLLSV ERSNRIVVDE VYDYHQGTYV CDYTQSDTVS SWTVRAVVQV
RTIVGDTKLK PDILDPVEDT LEVELGKPLT ISCKARFGFE RVFNPVIKWY IKDSDLEWEV
SVPEAKSIKS TLKDEIIERN IILEKVTQRD LRRKFVCFVQ NSIGNTTQSV QLKEKRGVVL
LYILLGTIGT LVAVLAASAL LYRHWIEIVL LYRTYQSKDQ TLGDKKDFDA FVSYAKWSSF
PSEATSSLSE EHLALSLFPD VLENKYGYSL CLLERDVAPG GVYAEDIVSI IKRSRRGIFI
LSPNYVNGPS IFELQAAVNL ALDDQTLKLI LIKFCYFQEP ESLPHLVKKA LRVLPTVTWR
GLKSVPPNSR FWAKMRYHMP VKNSQGFTWN QLRITSRIFQ WKGLSRTETT GRSSQPKEW


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E91655Hu ELISA Kit for Interleukin 18 Receptor Accessory Protein (IL18RAP) 96T/Kit
201-20-2761 IL1RAPL1{interleukin 1 receptor accessory protein-like 1}rabbit.pAb 0.2ml
CD72 Human Interleukin-18 receptor accessory protein IL18RAP (C-Fc-His tag) 50
CSB-EL011623RA Rat Interleukin-1 receptor accessory protein(IL1RAP) ELISA kit 96T
CC08 Human Interleukin-1 Receptor Accessory Protein IL-1RAcP 50
IL1RL2 IL1RAPL2 Gene interleukin 1 receptor accessory protein-like 2
E97819Hu ELISA Kit for Interleukin 1 Receptor Accessory Protein (IL1RAP) 96T/Kit
IL1RL1 IL1RAPL1 Gene interleukin 1 receptor accessory protein-like 1
C033 Human Interleukin-1 Receptor Accessory Protein IL-1RAcP l0
CB99 Human Interleukin-18 receptor accessory protein IL18RAP (C-His tag) 50
E97819Mu ELISA Kit for Interleukin 1 Receptor Accessory Protein (IL1RAP) 96T/Kit
CC35 Human Interleukin-18 receptor accessory protein IL18RAP (C-His tag) l0
IL1A IL18RAP Gene interleukin 18 receptor accessory protein
CB99 Human Interleukin-18 receptor accessory protein IL18RAP (C-Fc-His tag) l0
CSB-EL011624RA Rat Interleukin-1 receptor accessory protein-like 1(IL1RAPL1) ELISA kit 96T