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Toll-like receptor 4 (CD antigen CD284)

 TLR4_MOUSE              Reviewed;         835 AA.
Q9QUK6; Q9D691; Q9QZF5; Q9Z203;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 161.
RecName: Full=Toll-like receptor 4;
AltName: CD_antigen=CD284;
Flags: Precursor;
Name=Tlr4; Synonyms=Lps;
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 [GENOMIC DNA].
STRAIN=C3H/HeJ;
PubMed=10087992; DOI=10.1006/bcmd.1998.0201;
Poltorak A., Smirnova I., He X., Liu M.-Y., Van Huffel C.,
Birdwell D., Alejos E., Silva M., Du X., Thompson P., Chan E.K.L.,
Ledesma J., Roe B., Clifton S., Vogel S.N., Beutler B.;
"Genetic and physical mapping of the Lps locus: identification of the
Toll-4 receptor as a candidate gene in the critical region.";
Blood Cells Mol. Dis. 24:340-355(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANT LPS-TOLERANT
HIS-712.
STRAIN=C3H/HeJ;
PubMed=9851930; DOI=10.1126/science.282.5396.2085;
Poltorak A., He X., Smirnova I., Liu M.-Y., Van Huffel C., Du X.,
Birdwell D., Alejos E., Silva M., Galanos C., Freudenberg M.,
Ricciardi-Castagnoli P., Layton B., Beutler B.;
"Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations
in Tlr4 gene.";
Science 282:2085-2088(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANT LPS-TOLERANT
HIS-712.
STRAIN=C57BL/6J;
PubMed=9989976; DOI=10.1084/jem.189.4.615;
Qureshi S.T., Lariviere L., Leveque G., Clermont S., Moore K.J.,
Gros P., Malo D.;
"Endotoxin-tolerant mice have mutations in Toll-like receptor 4
(Tlr4).";
J. Exp. Med. 189:615-625(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Macrophage;
PubMed=10548109; DOI=10.1038/44605;
Underhill D.M., Ozinsky A., Hajjar A.M., Stevens A., Wilson C.B.,
Bassetti M., Aderem A.;
"The Toll-like receptor 2 is recruited to macrophage phagosomes and
discriminates between pathogens.";
Nature 401:811-815(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-94; ILE-209;
GLY-219; ILE-254; LEU-423; SER-477; ALA-516; ASP-593; ILE-600;
VAL-607; ILE-637; HIS-761 AND LYS-811.
STRAIN=Various strains;
PubMed=11104518; DOI=10.1186/gb-2000-1-1-research002;
Smirnova I., Poltorak A., Chan E.K.L., McBride C., Beutler B.;
"Phylogenetic variation and polymorphism at the Toll-like receptor 4
locus (TLR4).";
Genome Biol. 1:RESEARCH002.1-RESEARCH002.10(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-154.
STRAIN=C57BL/6J; TISSUE=Skin;
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).
[7]
FUNCTION.
PubMed=10952994; DOI=10.1074/jbc.M007386200;
Rhee S.H., Hwang D.;
"Murine Toll-like receptor 4 confers lipopolysaccharide responsiveness
as determined by activation of NF kappa B and expression of the
inducible cyclooxygenase.";
J. Biol. Chem. 275:34035-34040(2000).
[8]
FUNCTION.
PubMed=17478729; DOI=10.1161/CIRCRESAHA.106.142851;
Kim F., Pham M., Luttrell I., Bannerman D.D., Tupper J., Thaler J.,
Hawn T.R., Raines E.W., Schwartz M.W.;
"Toll-like receptor-4 mediates vascular inflammation and insulin
resistance in diet-induced obesity.";
Circ. Res. 100:1589-1596(2007).
[9]
INTERACTION WITH CNPY3.
PubMed=18780723; DOI=10.1093/intimm/dxn098;
Kiyokawa T., Akashi-Takamura S., Shibata T., Matsumoto F.,
Nishitani C., Kuroki Y., Seto Y., Miyake K.;
"A single base mutation in the PRAT4A gene reveals differential
interaction of PRAT4A with Toll-like receptors.";
Int. Immunol. 20:1407-1415(2008).
[10]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=20133493; DOI=10.1093/intimm/dxq005;
Tsukamoto H., Fukudome K., Takao S., Tsuneyoshi N., Kimoto M.;
"Lipopolysaccharide-binding protein-mediated Toll-like receptor 4
dimerization enables rapid signal transduction against
lipopolysaccharide stimulation on membrane-associated CD14-expressing
cells.";
Int. Immunol. 22:271-280(2010).
[11]
INTERACTION WITH HSP90B1.
PubMed=20865800; DOI=10.1038/ncomms1070;
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y.,
Hao B., Bona R., Han D., Li Z.;
"Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a
substrate-specific cochaperone.";
Nat. Commun. 1:79-79(2010).
[12]
ERRATUM.
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y.,
Hao B., Bona R., Han D., Li Z.;
Nat. Commun. 3:653-653(2012).
[13]
FUNCTION.
PubMed=20037584; DOI=10.1038/ni.1836;
Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J.,
Halle A., Rayner K.J., Boyer L., Zhong R., Frazier W.A.,
Lacy-Hulbert A., El Khoury J., Golenbock D.T., Moore K.J.;
"CD36 ligands promote sterile inflammation through assembly of a Toll-
like receptor 4 and 6 heterodimer.";
Nat. Immunol. 11:155-161(2010).
[14]
INTERACTION WITH CEACAM1.
PubMed=22496641; DOI=10.1371/journal.ppat.1002597;
Lu R., Pan H., Shively J.E.;
"CEACAM1 negatively regulates IL-1beta production in LPS activated
neutrophils by recruiting SHP-1 to a SYK-TLR4-CEACAM1 complex.";
PLoS Pathog. 8:E1002597-E1002597(2012).
[15]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=23812099; DOI=10.1038/ni.2639;
Sheedy F.J., Grebe A., Rayner K.J., Kalantari P., Ramkhelawon B.,
Carpenter S.B., Becker C.E., Ediriweera H.N., Mullick A.E.,
Golenbock D.T., Stuart L.M., Latz E., Fitzgerald K.A., Moore K.J.;
"CD36 coordinates NLRP3 inflammasome activation by facilitating
intracellular nucleation of soluble ligands into particulate ligands
in sterile inflammation.";
Nat. Immunol. 14:812-820(2013).
[16]
FUNCTION, AND INTERACTION WITH TIRAP AND TICAM2.
PubMed=24380872; DOI=10.1093/intimm/dxt071;
Tanimura N., Saitoh S., Ohto U., Akashi-Takamura S., Fujimoto Y.,
Fukase K., Shimizu T., Miyake K.;
"The attenuated inflammation of MPL is due to the lack of CD14-
dependent tight dimerization of the TLR4/MD2 complex at the plasma
membrane.";
Int. Immunol. 26:307-314(2014).
[17]
INTERACTION WITH SMPDL3B.
PubMed=26095358; DOI=10.1016/j.celrep.2015.05.006;
Heinz L.X., Baumann C.L., Koeberlin M.S., Snijder B., Gawish R.,
Shui G., Sharif O., Aspalter I.M., Mueller A.C., Kandasamy R.K.,
Breitwieser F.P., Pichlmair A., Bruckner M., Rebsamen M., Blueml S.,
Karonitsch T., Fauster A., Colinge J., Bennett K.L., Knapp S.,
Wenk M.R., Superti-Furga G.;
"The lipid-modifying enzyme SMPDL3B negatively regulates innate
immunity.";
Cell Rep. 11:1919-1928(2015).
[18]
INTERACTION WITH WDFY1 AND TICAM1.
PubMed=25736436; DOI=10.15252/embr.201439637;
Hu Y.H., Zhang Y., Jiang L.Q., Wang S., Lei C.Q., Sun M.S., Shu H.B.,
Liu Y.;
"WDFY1 mediates TLR3/4 signaling by recruiting TRIF.";
EMBO Rep. 16:447-455(2015).
[19]
X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 27-625 IN COMPLEX WITH LY96,
DISULFIDE BOND, AND GLYCOSYLATION AT ASN-34; ASN-75; ASN-172; ASN-204;
ASN-237; ASN-307; ASN-492; ASN-524 AND ASN-572.
PubMed=17803912; DOI=10.1016/j.cell.2007.08.002;
Kim H.M., Park B.S., Kim J.-I., Kim S.E., Lee J., Oh S.C.,
Enkhbayar P., Matsushima N., Lee H., Yoo O.J., Lee J.-O.;
"Crystal structure of the TLR4-MD-2 complex with bound endotoxin
antagonist Eritoran.";
Cell 130:906-917(2007).
[20]
X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 22-627 IN COMPLEX WITH LY96,
SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-172; ASN-204;
ASN-524 AND ASN-572.
PubMed=22532668; DOI=10.1073/pnas.1201193109;
Ohto U., Fukase K., Miyake K., Shimizu T.;
"Structural basis of species-specific endotoxin sensing by innate
immune receptor TLR4/MD-2.";
Proc. Natl. Acad. Sci. U.S.A. 109:7421-7426(2012).
-!- FUNCTION: Cooperates with LY96 and CD14 to mediate the innate
immune response to bacterial lipopolysaccharide (LPS)
(PubMed:9851930, PubMed:9989976, PubMed:20133493). Acts via MYD88,
TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine
secretion and the inflammatory response (PubMed:24380872). Also
involved in LPS-independent inflammatory responses triggered by
free fatty acids, such as palmitate. In complex with TLR6,
promotes sterile inflammation in monocytes/macrophages in response
to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In
this context, the initial signal is provided by oxLDL- or amyloid-
beta 42-binding to CD36. This event induces the formation of a
heterodimer of TLR4 and TLR6, which is rapidly internalized and
triggers inflammatory response, leading to the NF-kappa-B-
dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88
signaling pathway, and CCL5 cytokine, via TICAM1 signaling
pathway, as well as IL1B secretion. Binds electronegative LDL
(LDL(-)) and mediates the cytokine release induced by LDL(-) (By
similarity). {ECO:0000250|UniProtKB:O00206,
ECO:0000269|PubMed:10952994, ECO:0000269|PubMed:17478729,
ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:20133493,
ECO:0000269|PubMed:23812099, ECO:0000269|PubMed:24380872,
ECO:0000269|PubMed:9851930, ECO:0000269|PubMed:9989976}.
-!- SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a
multi-protein complex containing at least CD14, LY96 and TLR4
(PubMed:24380872). Binding to bacterial LPS leads to
homodimerization (PubMed:20133493, PubMed:24380872,
PubMed:22532668). Interacts with LY96 via the extracellular domain
(PubMed:17803912, PubMed:22532668). Interacts with MYD88 (via the
TIR domain). Interacts with TICAM2 and TIRAP (PubMed:24380872).
Interacts with NOX4 (By similarity). Interacts with CNPY3 and
HSP90B1; this interaction is required for proper folding in the
endoplasmic reticulum (PubMed:18780723, PubMed:20865800).
Interacts with MAP3K21; this interaction leads to negative
regulation of TLR4 signaling (By similarity). Interacts with CD36,
following CD36 stimulation by oxLDL or amyloid-beta 42, and forms
a heterodimer with TLR6. The trimeric complex is internalized and
triggers inflammatory response. LYN kinase activity facilitates
TLR4-TLR6 heterodimerization and signal initiation (By
similarity). Interacts with TICAM1 in response to LPS in a WDFY1-
dependent manner (PubMed:25736436). Interacts with WDFY1 in
response to LPS (PubMed:25736436). Interacts with SMPDL3B
(PubMed:26095358). Interacts with CEACAM1; upon lipopolysaccharide
stimulation, forms a complex including TLR4 and the phosphorylated
form of SYK and CEACAM1, which in turn, recruits PTPN6 that
dephosphorylates SYK, reducing the production of reactive oxygen
species (ROS) and lysosome disruption, which in turn, reduces the
activity of the inflammasome (PubMed:22496641).
{ECO:0000250|UniProtKB:O00206, ECO:0000269|PubMed:17803912,
ECO:0000269|PubMed:18780723, ECO:0000269|PubMed:20133493,
ECO:0000269|PubMed:20865800, ECO:0000269|PubMed:22496641,
ECO:0000269|PubMed:22532668, ECO:0000269|PubMed:24380872,
ECO:0000269|PubMed:25736436, ECO:0000269|PubMed:26095358}.
-!- INTERACTION:
Q9JHF9:Ly96; NbExp=8; IntAct=EBI-1534575, EBI-1534566;
Q3U0V2:Tradd; NbExp=3; IntAct=EBI-1534575, EBI-1544032;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20133493};
Single-pass type I membrane protein {ECO:0000269|PubMed:20133493}.
Note=Upon complex formation with CD36 and TLR6, internalized
through dynamin-dependent endocytosis.
{ECO:0000250|UniProtKB:O00206}.
-!- TISSUE SPECIFICITY: Highly expressed in heart, spleen, lung and
muscle. Lower levels are found in liver and kidney. Expressed in
macrophages. {ECO:0000269|PubMed:23812099}.
-!- DOMAIN: The TIR domain mediates interaction with NOX4.
{ECO:0000250|UniProtKB:O00206}.
-!- POLYMORPHISM: Interstrain analyzes reveals that TLR4 is a
polymorphic protein and that the extracellular domain is far more
variable than the cytoplasmic domain, which is variable at the C-
terminal. {ECO:0000305|PubMed:11104518}.
-!- DISEASE: Note=The protein is encoded by the Lps locus, an
important susceptibility locus, influencing the propensity to
develop a disseminated Gram-negative infection.
{ECO:0000269|PubMed:9851930, ECO:0000269|PubMed:9989976}.
-!- DISRUPTION PHENOTYPE: Animals with a double knockout of APOE and
TLR4, fed a Western diet for 12 weeks, have less aortic plaque
formation than single APOE knockout mice. They also show lower
serum concentrations of IL1A, ILB and IL18.
{ECO:0000269|PubMed:23812099}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
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EMBL; AF095353; AAC99411.1; -; mRNA.
EMBL; AF110133; AAD29272.1; -; mRNA.
EMBL; AF185285; AAF04278.1; -; mRNA.
EMBL; AF177767; AAF05317.1; -; Genomic_DNA.
EMBL; AK014533; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS18271.1; -.
RefSeq; NP_067272.1; NM_021297.3.
UniGene; Mm.38049; -.
PDB; 2Z64; X-ray; 2.84 A; A=27-625.
PDB; 3VQ1; X-ray; 2.70 A; A/B=22-627.
PDB; 3VQ2; X-ray; 2.48 A; A/B=22-627.
PDB; 5IJB; X-ray; 2.91 A; A/B=26-544.
PDB; 5IJC; X-ray; 2.57 A; A/B=26-544.
PDB; 5IJD; X-ray; 2.70 A; A/B=26-544.
PDBsum; 2Z64; -.
PDBsum; 3VQ1; -.
PDBsum; 3VQ2; -.
PDBsum; 5IJB; -.
PDBsum; 5IJC; -.
PDBsum; 5IJD; -.
ProteinModelPortal; Q9QUK6; -.
SMR; Q9QUK6; -.
BioGrid; 204224; 24.
DIP; DIP-38573N; -.
IntAct; Q9QUK6; 10.
STRING; 10090.ENSMUSP00000045770; -.
BindingDB; Q9QUK6; -.
ChEMBL; CHEMBL1795167; -.
iPTMnet; Q9QUK6; -.
PhosphoSitePlus; Q9QUK6; -.
MaxQB; Q9QUK6; -.
PaxDb; Q9QUK6; -.
PRIDE; Q9QUK6; -.
Ensembl; ENSMUST00000048096; ENSMUSP00000045770; ENSMUSG00000039005.
GeneID; 21898; -.
KEGG; mmu:21898; -.
UCSC; uc008thv.1; mouse.
CTD; 7099; -.
MGI; MGI:96824; Tlr4.
eggNOG; KOG4641; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000119006; -.
HOGENOM; HOG000037951; -.
HOVERGEN; HBG018823; -.
InParanoid; Q9QUK6; -.
KO; K10160; -.
OMA; EDWVRNE; -.
OrthoDB; EOG091G01RC; -.
PhylomeDB; Q9QUK6; -.
TreeFam; TF351113; -.
Reactome; R-MMU-140534; Ligand-dependent caspase activation.
Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-MMU-166166; MyD88-independent TLR4 cascade.
Reactome; R-MMU-2562578; TRIF-mediated programmed cell death.
Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-MMU-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
Reactome; R-MMU-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-MMU-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
EvolutionaryTrace; Q9QUK6; -.
PRO; PR:Q9QUK6; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000039005; -.
CleanEx; MM_TLR4; -.
ExpressionAtlas; Q9QUK6; baseline and differential.
Genevisible; Q9QUK6; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
GO; GO:0046696; C:lipopolysaccharide receptor complex; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
GO; GO:0001875; F:lipopolysaccharide receptor activity; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0002218; P:activation of innate immune response; IMP:MGI.
GO; GO:0000187; P:activation of MAPK activity; IMP:BHF-UCL.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; NAS:UniProtKB.
GO; GO:0014002; P:astrocyte development; IMP:MGI.
GO; GO:0002322; P:B cell proliferation involved in immune response; IMP:MGI.
GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
GO; GO:0071223; P:cellular response to lipoteichoic acid; IMP:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; IGI:ARUK-UCL.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:MGI.
GO; GO:0032497; P:detection of lipopolysaccharide; ISO:MGI.
GO; GO:0007252; P:I-kappaB phosphorylation; IMP:MGI.
GO; GO:0045087; P:innate immune response; TAS:BHF-UCL.
GO; GO:0032609; P:interferon-gamma production; IGI:MGI.
GO; GO:0050702; P:interleukin-1 beta secretion; IDA:UniProtKB.
GO; GO:0060729; P:intestinal epithelial structure maintenance; IMP:BHF-UCL.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
GO; GO:0042116; P:macrophage activation; ISS:UniProtKB.
GO; GO:0045576; P:mast cell activation; NAS:UniProtKB.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IGI:ARUK-UCL.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:BHF-UCL.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IMP:BHF-UCL.
GO; GO:0032707; P:negative regulation of interleukin-23 production; IMP:BHF-UCL.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:BHF-UCL.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:BHF-UCL.
GO; GO:0002537; P:nitric oxide production involved in inflammatory response; IMP:MGI.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
GO; GO:0032722; P:positive regulation of chemokine production; IDA:BHF-UCL.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IGI:ARUK-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
GO; GO:0050729; P:positive regulation of inflammatory response; IGI:ARUK-UCL.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:BHF-UCL.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; IMP:MGI.
GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:BHF-UCL.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; ISO:MGI.
GO; GO:0045362; P:positive regulation of interleukin-1 biosynthetic process; NAS:UniProtKB.
GO; GO:0032732; P:positive regulation of interleukin-1 production; IDA:BHF-UCL.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:BHF-UCL.
GO; GO:0045084; P:positive regulation of interleukin-12 biosynthetic process; ISO:MGI.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
GO; GO:0045368; P:positive regulation of interleukin-13 biosynthetic process; NAS:UniProtKB.
GO; GO:0045410; P:positive regulation of interleukin-6 biosynthetic process; NAS:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; ISO:MGI.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
GO; GO:0050671; P:positive regulation of lymphocyte proliferation; IMP:MGI.
GO; GO:0043032; P:positive regulation of macrophage activation; IGI:ARUK-UCL.
GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:MGI.
GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IMP:MGI.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:MGI.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
GO; GO:0070430; P:positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway; IDA:MGI.
GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IDA:MGI.
GO; GO:1903223; P:positive regulation of oxidative stress-induced neuron death; IGI:ARUK-UCL.
GO; GO:0010572; P:positive regulation of platelet activation; IMP:BHF-UCL.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:ARUK-UCL.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; ISO:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0002730; P:regulation of dendritic cell cytokine production; IDA:MGI.
GO; GO:0050727; P:regulation of inflammatory response; IMP:BHF-UCL.
GO; GO:0009617; P:response to bacterium; IMP:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IEA:InterPro.
GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; IGI:ARUK-UCL.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 3.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027168; TLR4.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR44568; PTHR44568; 1.
Pfam; PF13855; LRR_8; 2.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 8.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52058; SSF52058; 2.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disease mutation;
Disulfide bond; Glycoprotein; Immunity; Inflammatory response;
Innate immunity; Leucine-rich repeat; Membrane; Polymorphism;
Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 835 Toll-like receptor 4.
/FTId=PRO_0000034723.
TOPO_DOM 26 638 Extracellular. {ECO:0000255}.
TRANSMEM 639 659 Helical. {ECO:0000255}.
TOPO_DOM 660 835 Cytoplasmic. {ECO:0000255}.
REPEAT 54 75 LRR 1.
REPEAT 78 99 LRR 2.
REPEAT 102 123 LRR 3.
REPEAT 126 147 LRR 4.
REPEAT 150 171 LRR 5.
REPEAT 175 198 LRR 6.
REPEAT 204 224 LRR 7.
REPEAT 226 247 LRR 8.
REPEAT 248 269 LRR 9.
REPEAT 329 349 LRR 10.
REPEAT 350 370 LRR 11.
REPEAT 372 392 LRR 12.
REPEAT 398 420 LRR 13.
REPEAT 421 442 LRR 14.
REPEAT 446 467 LRR 15.
REPEAT 470 490 LRR 16.
REPEAT 495 516 LRR 17.
REPEAT 519 540 LRR 18.
REPEAT 543 564 LRR 19.
DOMAIN 576 627 LRRCT.
DOMAIN 670 816 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17803912}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17803912}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17803912}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17803912}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17803912}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17803912}.
CARBOHYD 492 492 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17803912}.
CARBOHYD 495 495 N-linked (GlcNAc...) asparagine.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17803912}.
CARBOHYD 572 572 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17803912}.
CARBOHYD 575 575 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 613 613 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 621 621 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 39 {ECO:0000269|PubMed:17803912}.
DISULFID 280 304 {ECO:0000269|PubMed:17803912}.
DISULFID 388 389 {ECO:0000269|PubMed:17803912}.
DISULFID 580 606 {ECO:0000269|PubMed:17803912}.
DISULFID 582 625 {ECO:0000269|PubMed:17803912}.
VARIANT 94 94 D -> N (in strain: KK/HLJ).
{ECO:0000269|PubMed:11104518}.
VARIANT 209 209 M -> I (in strain: A/J, BALB/cJ, P/J,
SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK).
{ECO:0000269|PubMed:11104518}.
VARIANT 219 219 D -> G (in strain: SEA/GNJ).
{ECO:0000269|PubMed:11104518}.
VARIANT 254 254 V -> I (in strain: A/J, BALB/cJ and SEA/
GNJ). {ECO:0000269|PubMed:11104518}.
VARIANT 423 423 Q -> L (in strain: SEA/GNJ).
{ECO:0000269|PubMed:11104518}.
VARIANT 477 477 A -> S (in strain: P/J).
{ECO:0000269|PubMed:11104518}.
VARIANT 516 516 T -> A (in strain: LP/J).
{ECO:0000269|PubMed:11104518}.
VARIANT 593 593 E -> D (in strain: A/J, BALB/cJ, P/J,
SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK).
{ECO:0000269|PubMed:11104518}.
VARIANT 600 600 N -> I (in strain: KK/HLJ).
{ECO:0000269|PubMed:11104518}.
VARIANT 607 607 A -> V (in strain: P/J).
{ECO:0000269|PubMed:11104518}.
VARIANT 637 637 V -> I (in strain: P/J).
{ECO:0000269|PubMed:11104518}.
VARIANT 712 712 P -> H (in Lps-tolerant mice).
{ECO:0000269|PubMed:9851930,
ECO:0000269|PubMed:9989976}.
VARIANT 761 761 R -> H (in strain: A/J, BALB/cJ, SODL/EI,
SEA/GNJ, NZW/LACJ and VM/DK).
{ECO:0000269|PubMed:11104518}.
VARIANT 811 811 N -> K (in strain: P/J).
{ECO:0000269|PubMed:11104518}.
CONFLICT 87 154 CEIETIEDKAWHGLHHLSNLILTGNPIQSFSPGSFSGLTSL
ENLVAVETKLASLESFPIGQLITLKKL -> EMNTESKSSE
AHALALSHILSPCQPSRRKLRVKLGSLSYQRAEEGVRSSEI
GYSCLHVDTRHDINAVD (in Ref. 6).
{ECO:0000305}.
STRAND 29 32 {ECO:0000244|PDB:3VQ2}.
TURN 33 35 {ECO:0000244|PDB:3VQ2}.
STRAND 36 38 {ECO:0000244|PDB:3VQ2}.
STRAND 40 42 {ECO:0000244|PDB:2Z64}.
STRAND 49 51 {ECO:0000244|PDB:5IJD}.
STRAND 57 59 {ECO:0000244|PDB:3VQ2}.
TURN 70 75 {ECO:0000244|PDB:3VQ2}.
STRAND 81 83 {ECO:0000244|PDB:3VQ2}.
TURN 94 99 {ECO:0000244|PDB:3VQ2}.
STRAND 105 107 {ECO:0000244|PDB:3VQ2}.
TURN 118 121 {ECO:0000244|PDB:5IJC}.
STRAND 129 131 {ECO:0000244|PDB:3VQ2}.
STRAND 140 143 {ECO:0000244|PDB:3VQ2}.
STRAND 153 155 {ECO:0000244|PDB:3VQ2}.
HELIX 168 171 {ECO:0000244|PDB:3VQ2}.
STRAND 178 180 {ECO:0000244|PDB:3VQ2}.
TURN 191 194 {ECO:0000244|PDB:3VQ2}.
HELIX 195 199 {ECO:0000244|PDB:3VQ2}.
STRAND 206 208 {ECO:0000244|PDB:3VQ2}.
TURN 219 224 {ECO:0000244|PDB:3VQ2}.
STRAND 226 234 {ECO:0000244|PDB:3VQ2}.
HELIX 239 247 {ECO:0000244|PDB:3VQ2}.
TURN 248 251 {ECO:0000244|PDB:3VQ2}.
STRAND 253 260 {ECO:0000244|PDB:3VQ2}.
HELIX 273 276 {ECO:0000244|PDB:3VQ2}.
HELIX 279 281 {ECO:0000244|PDB:3VQ2}.
STRAND 282 289 {ECO:0000244|PDB:3VQ2}.
HELIX 297 300 {ECO:0000244|PDB:3VQ2}.
HELIX 303 305 {ECO:0000244|PDB:3VQ2}.
STRAND 309 315 {ECO:0000244|PDB:3VQ2}.
STRAND 331 337 {ECO:0000244|PDB:3VQ2}.
STRAND 353 358 {ECO:0000244|PDB:3VQ2}.
STRAND 375 377 {ECO:0000244|PDB:3VQ2}.
STRAND 380 382 {ECO:0000244|PDB:2Z64}.
STRAND 383 388 {ECO:0000244|PDB:3VQ2}.
HELIX 391 394 {ECO:0000244|PDB:3VQ2}.
STRAND 401 403 {ECO:0000244|PDB:3VQ2}.
STRAND 408 412 {ECO:0000244|PDB:3VQ2}.
STRAND 424 426 {ECO:0000244|PDB:3VQ2}.
STRAND 430 434 {ECO:0000244|PDB:3VQ2}.
TURN 435 443 {ECO:0000244|PDB:3VQ2}.
STRAND 449 451 {ECO:0000244|PDB:3VQ2}.
TURN 462 467 {ECO:0000244|PDB:3VQ2}.
STRAND 473 475 {ECO:0000244|PDB:3VQ2}.
HELIX 482 484 {ECO:0000244|PDB:3VQ2}.
TURN 489 492 {ECO:0000244|PDB:5IJD}.
STRAND 498 500 {ECO:0000244|PDB:3VQ2}.
TURN 511 516 {ECO:0000244|PDB:3VQ2}.
STRAND 522 524 {ECO:0000244|PDB:3VQ2}.
STRAND 532 534 {ECO:0000244|PDB:2Z64}.
HELIX 535 537 {ECO:0000244|PDB:3VQ2}.
TURN 538 540 {ECO:0000244|PDB:3VQ2}.
STRAND 546 548 {ECO:0000244|PDB:3VQ2}.
STRAND 557 559 {ECO:0000244|PDB:3VQ2}.
HELIX 561 563 {ECO:0000244|PDB:3VQ2}.
STRAND 570 572 {ECO:0000244|PDB:3VQ2}.
HELIX 582 584 {ECO:0000244|PDB:3VQ1}.
HELIX 585 588 {ECO:0000244|PDB:3VQ2}.
TURN 589 593 {ECO:0000244|PDB:3VQ2}.
STRAND 594 600 {ECO:0000244|PDB:3VQ2}.
HELIX 601 603 {ECO:0000244|PDB:3VQ2}.
STRAND 608 610 {ECO:0000244|PDB:2Z64}.
HELIX 616 618 {ECO:0000244|PDB:2Z64}.
SEQUENCE 835 AA; 95519 MW; 9C83B59F9A220C17 CRC64;
MMPPWLLART LIMALFFSCL TPGSLNPCIE VVPNITYQCM DQKLSKVPDD IPSSTKNIDL
SFNPLKILKS YSFSNFSELQ WLDLSRCEIE TIEDKAWHGL HHLSNLILTG NPIQSFSPGS
FSGLTSLENL VAVETKLASL ESFPIGQLIT LKKLNVAHNF IHSCKLPAYF SNLTNLVHVD
LSYNYIQTIT VNDLQFLREN PQVNLSLDMS LNPIDFIQDQ AFQGIKLHEL TLRGNFNSSN
IMKTCLQNLA GLHVHRLILG EFKDERNLEI FEPSIMEGLC DVTIDEFRLT YTNDFSDDIV
KFHCLANVSA MSLAGVSIKY LEDVPKHFKW QSLSIIRCQL KQFPTLDLPF LKSLTLTMNK
GSISFKKVAL PSLSYLDLSR NALSFSGCCS YSDLGTNSLR HLDLSFNGAI IMSANFMGLE
ELQHLDFQHS TLKRVTEFSA FLSLEKLLYL DISYTNTKID FDGIFLGLTS LNTLKMAGNS
FKDNTLSNVF ANTTNLTFLD LSKCQLEQIS WGVFDTLHRL QLLNMSHNNL LFLDSSHYNQ
LYSLSTLDCS FNRIETSKGI LQHFPKSLAF FNLTNNSVAC ICEHQKFLQW VKEQKQFLVN
VEQMTCATPV EMNTSLVLDF NNSTCYMYKT IISVSVVSVI VVSTVAFLIY HFYFHLILIA
GCKKYSRGES IYDAFVIYSS QNEDWVRNEL VKNLEEGVPR FHLCLHYRDF IPGVAIAANI
IQEGFHKSRK VIVVVSRHFI QSRWCIFEYE IAQTWQFLSS RSGIIFIVLE KVEKSLLRQQ
VELYRLLSRN TYLEWEDNPL GRHIFWRRLK NALLDGKASN PEQTAEEEQE TATWT


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