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Interleukin-1 receptor type 2 (IL-1R-2) (IL-1RT-2) (IL-1RT2) (CD121 antigen-like family member B) (CDw121b) (IL-1 type II receptor) (Interleukin-1 receptor beta) (IL-1R-beta) (Interleukin-1 receptor type II) (CD antigen CD121b) [Cleaved into: Interleukin-1 receptor type 2, membrane form (mIL-1R2) (mIL-1RII); Interleukin-1 receptor type 2, soluble form (sIL-1R2) (sIL-1RII)]

 IL1R2_HUMAN             Reviewed;         398 AA.
P27930; D3DVJ5; Q6LCE6; Q9UE68;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
10-OCT-2018, entry version 172.
RecName: Full=Interleukin-1 receptor type 2;
Short=IL-1R-2;
Short=IL-1RT-2;
Short=IL-1RT2;
AltName: Full=CD121 antigen-like family member B;
AltName: Full=CDw121b;
AltName: Full=IL-1 type II receptor;
AltName: Full=Interleukin-1 receptor beta;
Short=IL-1R-beta;
AltName: Full=Interleukin-1 receptor type II;
AltName: CD_antigen=CD121b;
Contains:
RecName: Full=Interleukin-1 receptor type 2, membrane form;
Short=mIL-1R2;
Short=mIL-1RII;
Contains:
RecName: Full=Interleukin-1 receptor type 2, soluble form;
Short=sIL-1R2;
Short=sIL-1RII;
Flags: Precursor;
Name=IL1R2; Synonyms=IL1RB;
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 LONG).
TISSUE=B-cell;
PubMed=1833184;
McMahan C.J., Slack J.L., Mosley B., Cosman D., Lupton S.D.,
Brunton L.L., Grubin C.E., Wignall J.M., Jenkins N.A., Brannan C.I.,
Copeland N.G., Huebner K., Croce C.M., Cannizzarro L.A., Benjamin D.,
Dower S.K., Spriggs M.K., Sims J.E.;
"A novel IL-1 receptor, cloned from B cells by mammalian expression,
is expressed in many cell types.";
EMBO J. 10:2821-2832(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), IL1B-BINDING, AND
SUBCELLULAR LOCATION (ISOFORM SHORT).
PubMed=8702856; DOI=10.1074/jbc.271.34.20965;
Liu C., Hart R.P., Liu X.J., Clevenger W., Maki R.A., Souza E.B.;
"Cloning and characterization of an alternatively processed human type
II interleukin-1 receptor mRNA.";
J. Biol. Chem. 271:20965-20972(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Chou H.-H., Takashiba T., Takigawa M., Maeda H., Asahara Y.,
Nishimura F., Arai H., Murayama Y.;
"Complete nucleotide sequence and expression of the human interleukin-
1 receptor type II in human gingival fibroblasts.";
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-181 AND LYS-292.
SeattleSNPs variation discovery resource;
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Ovary;
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).
[8]
FUNCTION, PROTEOLYTIC PROCESSING, AND LIGAND-BINDING.
PubMed=7989776;
Giri J.G., Wells J., Dower S.K., McCall C.E., Guzman R.N., Slack J.,
Bird T.A., Shanebeck K., Grabstein K.H., Sims J.E., Alderson M.R.;
"Elevated levels of shed type II IL-1 receptor in sepsis. Potential
role for type II receptor in regulation of IL-1 responses.";
J. Immunol. 153:5802-5809(1994).
[9]
LIGAND-BINDING.
PubMed=7878046; DOI=10.1073/pnas.92.5.1714;
Symons J.A., Young P.R., Duff G.W.;
"Soluble type II interleukin 1 (IL-1) receptor binds and blocks
processing of IL-1 beta precursor and loses affinity for IL-1 receptor
antagonist.";
Proc. Natl. Acad. Sci. U.S.A. 92:1714-1718(1995).
[10]
PROTEOLYTIC PROCESSING.
PubMed=9395521; DOI=10.1074/jbc.272.50.31764;
Orlando S., Sironi M., Bianchi G., Drummond A.H., Boraschi D.,
Yabes D., Mantovani A.;
"Role of metalloproteases in the release of the IL-1 type II decoy
receptor.";
J. Biol. Chem. 272:31764-31769(1997).
[11]
FUNCTION, AND INTERACTION WITH IL1RAP.
PubMed=9862719;
Lang D., Knop J., Wesche H., Raffetseder U., Kurrle R., Boraschi D.,
Martin M.U.;
"The type II IL-1 receptor interacts with the IL-1 receptor accessory
protein: a novel mechanism of regulation of IL-1 responsiveness.";
J. Immunol. 161:6871-6877(1998).
[12]
FUNCTION AS DECOY RECEPTOR.
PubMed=10975853; DOI=10.4049/jimmunol.165.6.3350;
Neumann D., Kollewe C., Martin M.U., Boraschi D.;
"The membrane form of the type II IL-1 receptor accounts for
inhibitory function.";
J. Immunol. 165:3350-3357(2000).
[13]
FUNCTION AS DECOY RECEPTOR.
PubMed=12530978; DOI=10.1016/S1074-7613(02)00514-9;
Smith D.E., Hanna R., Friend D., Moore H., Chen H., Farese A.M.,
MacVittie T.J., Virca G.D., Sims J.E.;
"The soluble form of IL-1 receptor accessory protein enhances the
ability of soluble type II IL-1 receptor to inhibit IL-1 action.";
Immunity 18:87-96(2003).
[14]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 14-343 IN COMPLEX WITH IL1RAP
AND IL1B, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-112 AND
ASN-219.
PubMed=20802483; DOI=10.1038/ni.1925;
Wang D., Zhang S., Li L., Liu X., Mei K., Wang X.;
"Structural insights into the assembly and activation of IL-1beta with
its receptors.";
Nat. Immunol. 11:905-911(2010).
-!- FUNCTION: Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces
IL1B activities. Serves as a decoy receptor by competetive binding
to IL1B and preventing its binding to IL1R1. Also modulates
cellular response through non-signaling association with IL1RAP
after binding to IL1B. IL1R2 (membrane and secreted forms)
preferentially binds IL1B and poorly IL1A and IL1RN. The secreted
IL1R2 recruits secreted IL1RAP with high affinity; this complex
formation may be the dominant mechanism for neutralization of IL1B
by secreted/soluble receptors. {ECO:0000269|PubMed:10975853,
ECO:0000269|PubMed:12530978, ECO:0000269|PubMed:7989776,
ECO:0000269|PubMed:9862719}.
-!- SUBUNIT: Associates with IL1RAP to form a non-signaling
interleukin-1 receptor complex. {ECO:0000269|PubMed:20802483}.
-!- INTERACTION:
P01583:IL1A; NbExp=4; IntAct=EBI-2831568, EBI-1749782;
-!- SUBCELLULAR LOCATION: Isoform Short: Secreted
{ECO:0000269|PubMed:8702856}.
-!- SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Single-pass
type I membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P27930-1; Sequence=Displayed;
Name=Short;
IsoId=P27930-2; Sequence=VSP_042222;
-!- PTM: A soluble form (sIL1R2) can also be produced by proteolytic
cleavage at the cell surface (shedding) involving a
metalloproteinase; hovever, several sIL1R2 forms ranging from 45
and 60 kDa are reported. {ECO:0000269|PubMed:7989776,
ECO:0000269|PubMed:9395521}.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il1r2/";
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EMBL; X59770; CAA42441.1; -; mRNA.
EMBL; U64094; AAB05878.1; -; mRNA.
EMBL; U74649; AAD00242.1; -; mRNA.
EMBL; AY124010; AAM64221.1; -; Genomic_DNA.
EMBL; AC007165; AAK52072.1; -; Genomic_DNA.
EMBL; CH471127; EAX01800.1; -; Genomic_DNA.
EMBL; CH471127; EAX01801.1; -; Genomic_DNA.
EMBL; CH471127; EAX01802.1; -; Genomic_DNA.
EMBL; CH471127; EAX01803.1; -; Genomic_DNA.
EMBL; BC039031; AAH39031.1; -; mRNA.
CCDS; CCDS2054.1; -. [P27930-1]
CCDS; CCDS58719.1; -. [P27930-2]
PIR; S17428; S17428.
RefSeq; NP_001248348.1; NM_001261419.1. [P27930-2]
RefSeq; NP_004624.1; NM_004633.3. [P27930-1]
RefSeq; XP_006712797.1; XM_006712734.3. [P27930-1]
RefSeq; XP_011510106.1; XM_011511804.2. [P27930-1]
UniGene; Hs.25333; -.
PDB; 3O4O; X-ray; 3.30 A; C=14-343.
PDBsum; 3O4O; -.
ProteinModelPortal; P27930; -.
SMR; P27930; -.
BioGrid; 113605; 43.
DIP; DIP-61267N; -.
IntAct; P27930; 4.
MINT; P27930; -.
STRING; 9606.ENSP00000330959; -.
iPTMnet; P27930; -.
PhosphoSitePlus; P27930; -.
BioMuta; IL1R2; -.
DMDM; 124310; -.
EPD; P27930; -.
PaxDb; P27930; -.
PeptideAtlas; P27930; -.
PRIDE; P27930; -.
ProteomicsDB; 54427; -.
ProteomicsDB; 54428; -. [P27930-2]
DNASU; 7850; -.
Ensembl; ENST00000332549; ENSP00000330959; ENSG00000115590. [P27930-1]
Ensembl; ENST00000393414; ENSP00000377066; ENSG00000115590. [P27930-1]
Ensembl; ENST00000441002; ENSP00000414611; ENSG00000115590. [P27930-2]
GeneID; 7850; -.
KEGG; hsa:7850; -.
UCSC; uc002tbm.4; human. [P27930-1]
CTD; 7850; -.
DisGeNET; 7850; -.
EuPathDB; HostDB:ENSG00000115590.13; -.
GeneCards; IL1R2; -.
HGNC; HGNC:5994; IL1R2.
HPA; HPA027597; -.
HPA; HPA027598; -.
MIM; 147811; gene.
neXtProt; NX_P27930; -.
OpenTargets; ENSG00000115590; -.
PharmGKB; PA29810; -.
eggNOG; ENOG410IJCQ; Eukaryota.
eggNOG; ENOG410YQDP; LUCA.
GeneTree; ENSGT00760000119071; -.
HOGENOM; HOG000113036; -.
HOVERGEN; HBG052104; -.
InParanoid; P27930; -.
KO; K04387; -.
OMA; RQEYSEN; -.
OrthoDB; EOG091G077L; -.
PhylomeDB; P27930; -.
TreeFam; TF325519; -.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
SIGNOR; P27930; -.
ChiTaRS; IL1R2; human.
EvolutionaryTrace; P27930; -.
GeneWiki; Interleukin_1_receptor,_type_II; -.
GenomeRNAi; 7850; -.
PRO; PR:P27930; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115590; Expressed in 185 organ(s), highest expression level in decidua.
CleanEx; HS_IL1R2; -.
ExpressionAtlas; P27930; baseline and differential.
Genevisible; P27930; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019966; F:interleukin-1 binding; IEA:Ensembl.
GO; GO:0004908; F:interleukin-1 receptor activity; TAS:ProtInc.
GO; GO:0004910; F:interleukin-1, type II, blocking receptor activity; IEA:InterPro.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
GO; GO:0050712; P:negative regulation of interleukin-1 alpha secretion; IEA:Ensembl.
GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; IEA:Ensembl.
GO; GO:0010955; P:negative regulation of protein processing; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR015621; IL-1_rcpt_fam.
InterPro; IPR004074; IL-1_rcpt_I/II-typ.
InterPro; IPR004077; IL-1_rcpt_II-typ.
InterPro; IPR013151; Immunoglobulin.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF00047; ig; 1.
PRINTS; PR01539; INTRLEUKN1R2.
PRINTS; PR01536; INTRLKN1R12F.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 13 {ECO:0000255}.
CHAIN 14 398 Interleukin-1 receptor type 2, membrane
form.
/FTId=PRO_0000015439.
CHAIN 14 ? Interleukin-1 receptor type 2, soluble
form.
/FTId=PRO_0000415348.
TOPO_DOM 14 343 Extracellular. {ECO:0000255}.
TRANSMEM 344 369 Helical. {ECO:0000255}.
TOPO_DOM 370 398 Cytoplasmic. {ECO:0000255}.
DOMAIN 18 124 Ig-like C2-type 1.
DOMAIN 134 223 Ig-like C2-type 2.
DOMAIN 237 349 Ig-like C2-type 3.
REGION 329 343 Contains proteolytic cleavage site.
{ECO:0000305}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20802483}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20802483}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 116 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20802483}.
DISULFID 50 108 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20802483}.
DISULFID 152 207 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20802483}.
DISULFID 258 326 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20802483}.
VAR_SEQ 297 398 Missing (in isoform Short).
{ECO:0000303|PubMed:8702856}.
/FTId=VSP_042222.
VARIANT 181 181 E -> K (in dbSNP:rs28385682).
{ECO:0000269|Ref.4}.
/FTId=VAR_019132.
VARIANT 292 292 E -> K (in dbSNP:rs3218976).
{ECO:0000269|Ref.4}.
/FTId=VAR_019133.
CONFLICT 123 123 L -> F (in Ref. 2; AAD00242).
{ECO:0000305}.
CONFLICT 171 171 K -> R (in Ref. 2; AAD00242).
{ECO:0000305}.
CONFLICT 199 199 L -> Q (in Ref. 2; AAD00242).
{ECO:0000305}.
STRAND 29 33 {ECO:0000244|PDB:3O4O}.
STRAND 38 41 {ECO:0000244|PDB:3O4O}.
STRAND 47 49 {ECO:0000244|PDB:3O4O}.
STRAND 70 73 {ECO:0000244|PDB:3O4O}.
STRAND 82 84 {ECO:0000244|PDB:3O4O}.
STRAND 86 89 {ECO:0000244|PDB:3O4O}.
STRAND 92 98 {ECO:0000244|PDB:3O4O}.
STRAND 104 107 {ECO:0000244|PDB:3O4O}.
STRAND 110 112 {ECO:0000244|PDB:3O4O}.
STRAND 115 126 {ECO:0000244|PDB:3O4O}.
HELIX 130 132 {ECO:0000244|PDB:3O4O}.
HELIX 133 136 {ECO:0000244|PDB:3O4O}.
STRAND 138 143 {ECO:0000244|PDB:3O4O}.
STRAND 148 151 {ECO:0000244|PDB:3O4O}.
TURN 156 158 {ECO:0000244|PDB:3O4O}.
STRAND 161 163 {ECO:0000244|PDB:3O4O}.
STRAND 170 173 {ECO:0000244|PDB:3O4O}.
STRAND 181 185 {ECO:0000244|PDB:3O4O}.
STRAND 189 196 {ECO:0000244|PDB:3O4O}.
HELIX 199 201 {ECO:0000244|PDB:3O4O}.
STRAND 203 210 {ECO:0000244|PDB:3O4O}.
STRAND 219 229 {ECO:0000244|PDB:3O4O}.
STRAND 260 265 {ECO:0000244|PDB:3O4O}.
STRAND 271 279 {ECO:0000244|PDB:3O4O}.
STRAND 281 285 {ECO:0000244|PDB:3O4O}.
STRAND 287 289 {ECO:0000244|PDB:3O4O}.
STRAND 301 303 {ECO:0000244|PDB:3O4O}.
STRAND 305 308 {ECO:0000244|PDB:3O4O}.
STRAND 325 330 {ECO:0000244|PDB:3O4O}.
STRAND 333 335 {ECO:0000244|PDB:3O4O}.
SEQUENCE 398 AA; 45421 MW; 2C2A03ADA6F3AC5B CRC64;
MLRLYVLVMG VSAFTLQPAA HTGAARSCRF RGRHYKREFR LEGEPVALRC PQVPYWLWAS
VSPRINLTWH KNDSARTVPG EEETRMWAQD GALWLLPALQ EDSGTYVCTT RNASYCDKMS
IELRVFENTD AFLPFISYPQ ILTLSTSGVL VCPDLSEFTR DKTDVKIQWY KDSLLLDKDN
EKFLSVRGTT HLLVHDVALE DAGYYRCVLT FAHEGQQYNI TRSIELRIKK KKEETIPVII
SPLKTISASL GSRLTIPCKV FLGTGTPLTT MLWWTANDTH IESAYPGGRV TEGPRQEYSE
NNENYIEVPL IFDPVTREDL HMDFKCVVHN TLSFQTLRTT VKEASSTFSW GIVLAPLSLA
FLVLGGIWMH RRCKHRTGKA DGLTVLWPHH QDFQSYPK


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U0066m CLIA CD121 antigen-like family member B,Il1r2,Il-1r2,IL-1R-2,Il1rb,IL-1R-beta,IL-1RT2,IL-1RT-2,Interleukin-1 receptor beta,Interleukin-1 receptor type 2,Interleukin-1 receptor type II,Mouse,Mus muscul 96T
E0066m ELISA CD121 antigen-like family member B,Il1r2,Il-1r2,IL-1R-2,Il1rb,IL-1R-beta,IL-1RT2,IL-1RT-2,Interleukin-1 receptor beta,Interleukin-1 receptor type 2,Interleukin-1 receptor type II,Mouse,Mus muscu 96T
U0066r CLIA CD121 antigen-like family member B,Il1r2,Il-1r2,IL-1R-2,Il1rb,IL-1R-beta,IL-1RT2,IL-1RT-2,Interleukin-1 receptor beta,Interleukin-1 receptor type 2,Interleukin-1 receptor type II,Rat,Rattus norve 96T
E0066r ELISA kit CD121 antigen-like family member B,Il1r2,Il-1r2,IL-1R-2,Il1rb,IL-1R-beta,IL-1RT2,IL-1RT-2,Interleukin-1 receptor beta,Interleukin-1 receptor type 2,Interleukin-1 receptor type II,Rat,Rattus 96T
E0066m ELISA kit CD121 antigen-like family member B,Il1r2,Il-1r2,IL-1R-2,Il1rb,IL-1R-beta,IL-1RT2,IL-1RT-2,Interleukin-1 receptor beta,Interleukin-1 receptor type 2,Interleukin-1 receptor type II,Mouse,Mus 96T
E0065m ELISA CD121 antigen-like family member A,Il1r1,Il-1r1,IL-1R-1,Il1ra,IL-1R-alpha,IL-1RT1,IL-1RT-1,Interleukin-1 receptor alpha,Interleukin-1 receptor type 1,Interleukin-1 receptor type I,Mouse,Mus musc 96T
U0065r CLIA CD121 antigen-like family member A,Il1r1,IL-1R-1,Il1ra,IL-1R-alpha,IL-1RT1,IL-1RT-1,Interleukin-1 receptor alpha,Interleukin-1 receptor type 1,Interleukin-1 receptor type I,p80,Rat,Rattus norvegi 96T
U0065m CLIA CD121 antigen-like family member A,Il1r1,Il-1r1,IL-1R-1,Il1ra,IL-1R-alpha,IL-1RT1,IL-1RT-1,Interleukin-1 receptor alpha,Interleukin-1 receptor type 1,Interleukin-1 receptor type I,Mouse,Mus muscu 96T
E0065r ELISA CD121 antigen-like family member A,Il1r1,IL-1R-1,Il1ra,IL-1R-alpha,IL-1RT1,IL-1RT-1,Interleukin-1 receptor alpha,Interleukin-1 receptor type 1,Interleukin-1 receptor type I,p80,Rat,Rattus norveg 96T
E0065m ELISA kit CD121 antigen-like family member A,Il1r1,Il-1r1,IL-1R-1,Il1ra,IL-1R-alpha,IL-1RT1,IL-1RT-1,Interleukin-1 receptor alpha,Interleukin-1 receptor type 1,Interleukin-1 receptor type I,Mouse,Mus 96T
E0065r ELISA kit CD121 antigen-like family member A,Il1r1,IL-1R-1,Il1ra,IL-1R-alpha,IL-1RT1,IL-1RT-1,Interleukin-1 receptor alpha,Interleukin-1 receptor type 1,Interleukin-1 receptor type I,p80,Rat,Rattus n 96T
E0065h ELISA kit CD121 antigen-like family member A,Homo sapiens,Human,IL1R,IL1R1,IL-1R-1,IL1RA,IL-1R-alpha,IL1RT1,IL-1RT1,IL-1RT-1,Interleukin-1 receptor alpha,Interleukin-1 receptor type 1,Interleukin-1 r 96T
E0065h ELISA CD121 antigen-like family member A,Homo sapiens,Human,IL1R,IL1R1,IL-1R-1,IL1RA,IL-1R-alpha,IL1RT1,IL-1RT1,IL-1RT-1,Interleukin-1 receptor alpha,Interleukin-1 receptor type 1,Interleukin-1 recept 96T
U0065h CLIA CD121 antigen-like family member A,Homo sapiens,Human,IL1R,IL1R1,IL-1R-1,IL1RA,IL-1R-alpha,IL1RT1,IL-1RT1,IL-1RT-1,Interleukin-1 receptor alpha,Interleukin-1 receptor type 1,Interleukin-1 recepto 96T
20-321-175031 INTERLEUKIN-1 RECEPTOR TYPE I (p80) - MONOCLONAL ANTIBODY TO MOUSE INTERLEUKIN-1 RECEPTOR TYPE I (p80); IL-1R-1; p80; CD121a antigen Monoclonal 0.1 mg
20-321-175030 INTERLEUKIN-1 RECEPTOR TYPE I (p80) - MONOCLONAL ANTIBODY TO MOUSE INTERLEUKIN-1 RECEPTOR TYPE I (p80); IL-1R-1; p80; CD121a antigen Monoclonal 0.1 mg
20-321-175029 INTERLEUKIN-1 RECEPTOR TYPE I (p80) - MONOCLONAL ANTIBODY TO MOUSE INTERLEUKIN-1 RECEPTOR TYPE I (p80); IL-1R-1; p80; CD121a antigen Monoclonal 0.1 mg
20-321-175028 INTERLEUKIN-1 RECEPTOR TYPE I (p80) - MONOCLONAL ANTIBODY TO MOUSE INTERLEUKIN-1 RECEPTOR TYPE I (p80); IL-1R-1; p80; CD121a antigen Monoclonal 0.1 mg
E2006h ELISA kit CDw128b,C-X-C chemokine receptor type 2,CXCR2,CXC-R2,CXCR-2,GRO_MGSA receptor,High affinity interleukin-8 receptor B,Homo sapiens,Human,IL-8 receptor type 2,IL-8R B,IL8RB 96T
U2006h CLIA CDw128b,C-X-C chemokine receptor type 2,CXCR2,CXC-R2,CXCR-2,GRO_MGSA receptor,High affinity interleukin-8 receptor B,Homo sapiens,Human,IL-8 receptor type 2,IL-8R B,IL8RB 96T
U2006h CLIA kit CDw128b,C-X-C chemokine receptor type 2,CXCR2,CXC-R2,CXCR-2,GRO_MGSA receptor,High affinity interleukin-8 receptor B,Homo sapiens,Human,IL-8 receptor type 2,IL-8R B,IL8RB 96T


 

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