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Search results for: IL1RAcP

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#27347163   2016/05/25 To Up

Interleukin-33 in human gliomas: Expression and prognostic significance.

Interleukin-33 (IL-33) is a nuclear and pleiotropic cytokine with regard to its cellular sources and its actions. IL-33 is involved in the pathogenesis of brain diseases. Several factors account for the tumorigenicity of human gliomas, including cytokines and their receptors. The present study assessed the expression and prognostic significance of IL-33 in human astroglial brain tumors. Protein levels of IL-33 were determined by immunohistochemistry using a tissue microarray containing 95 human gliomas. mRNA expression data of IL-33, as well as of its receptors, IL-1 receptor-like 1 protein and IL-1 receptor accessory protein (IL1RAcP), were obtained from The Cancer Genome Atlas database. IL-33 protein was expressed heterogeneously in tumor tissue, but was, however, not detected in normal brain tissue. There was no differential IL-33 protein expression by tumor grade, while IL-33 protein expression was associated with inferior survival in patients with recurrent glioblastomas. Interrogations of the TCGA database indicated that mRNA expression of IL-33 and the IL-33 receptors was heterogeneous, and that IL-33 and IL1RAcP mRNA levels were correlated with the tumor grade. Elevated IL-33 mRNA levels were associated with the inferior survival of glioblastoma patients. Therefore, IL-33 may play an important role in the pathogenesis and prognosis of human gliomas.
Dorothee Gramatzki, Karl Frei, Gieri Cathomas, Holger Moch, Michael Weller, Kirsten Diana Mertz

2580 related Products with: Interleukin-33 in human gliomas: Expression and prognostic significance.

96 wells (1 kit)96 wells (1 kit)10 96 wells (1 kit)5ug0.1 mg10 2 2 2ug2ug5

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#25048602   2014/07/22 To Up

Protein painting reveals solvent-excluded drug targets hidden within native protein-protein interfaces.

Identifying the contact regions between a protein and its binding partners is essential for creating therapies that block the interaction. Unfortunately, such contact regions are extremely difficult to characterize because they are hidden inside the binding interface. Here we introduce protein painting as a new tool that employs small molecules as molecular paints to tightly coat the surface of protein-protein complexes. The molecular paints, which block trypsin cleavage sites, are excluded from the binding interface. Following mass spectrometry, only peptides hidden in the interface emerge as positive hits, revealing the functional contact regions that are drug targets. We use protein painting to discover contact regions between the three-way interaction of IL1β ligand, the receptor IL1RI and the accessory protein IL1RAcP. We then use this information to create peptides and monoclonal antibodies that block the interaction and abolish IL1β cell signalling. The technology is broadly applicable to discover protein interaction drug targets.
Alessandra Luchini, Virginia Espina, Lance A Liotta

2068 related Products with: Protein painting reveals solvent-excluded drug targets hidden within native protein-protein interfaces.

0.1mg0.1 mg1 mg0.05 mg50 0.05 mg0.025 mg100 ug0.1 mg100 1 mg0.05 mg

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#24568840   2014/02/22 To Up

Association of IL33-IL-1 receptor-like 1 (IL1RL1) pathway polymorphisms with wheezing phenotypes and asthma in childhood.

Genome-wide association studies identified IL33 and IL-1 receptor-like 1 (IL1RL1)/IL18R1 as asthma susceptibility loci. IL33 and IL1RL1 constitute a single ligand-receptor pathway.
Olga E Savenije, Jestinah M Mahachie John, Raquel Granell, Marjan Kerkhof, F Nicole Dijk, Johan C de Jongste, Henriëtte A Smit, Bert Brunekreef, Dirkje S Postma, Kristel Van Steen, John Henderson, Gerard H Koppelman

2903 related Products with: Association of IL33-IL-1 receptor-like 1 (IL1RL1) pathway polymorphisms with wheezing phenotypes and asthma in childhood.

100ug Lyophilized100ug100ul100ug100ug Lyophilized100ug100ug100ug Lyophilized100ug100ug100ug100ug

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#21272866   2011/01/26 To Up

Distinct expression of the soluble and the membrane-bound forms of interleukin-1 receptor accessory protein in the endometrium of women with endometriosis.

To investigate interleukin (IL) 1 receptor accessory protein (IL1RAcP) expression in the eutopic endometrium of women with endometriosis.
Sophie Guay, Nadège Michaud, Nathalie Bourcier, Mathieu Leboeuf, Madeleine Lemyre, Jacques Mailloux, Ali Akoum

2863 related Products with: Distinct expression of the soluble and the membrane-bound forms of interleukin-1 receptor accessory protein in the endometrium of women with endometriosis.

96tests1100μg100ul1mg100μg

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#19996325   2009/12/08 To Up

Expression of interleukin 1-like cytokine interleukin 33 and its receptor complex (ST2L and IL1RAcP) in human pancreatic myofibroblasts.

Interleukin 33 (IL33) is a cytokine belonging to the IL1 family and it binds to a complex of the ST2L/IL1 receptor accessory protein (IL1RAcP). To define the role of IL33 in fibrogenesis of the pancreas, the expression of IL33, ST2L and IL1RAcP was examined in chronic pancreatitis tissues. The effects of IL33 on the functions of human pancreatic myofibroblasts were also investigated.
Atsushi Nishida, Akira Andoh, Hirotsugu Imaeda, Osamu Inatomi, Hisanori Shiomi, Yoshihide Fujiyama

2135 related Products with: Expression of interleukin 1-like cytokine interleukin 33 and its receptor complex (ST2L and IL1RAcP) in human pancreatic myofibroblasts.

96 wells (1 kit)96 wells (1 kit)96 wells (1 kit)96T500 100ul96tests2ug1 mg1 kit(96 Wells)2

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#15849357   2005/04/22 To Up

Interactive sites in the MyD88 Toll/interleukin (IL) 1 receptor domain responsible for coupling to the IL1beta signaling pathway.

Myeloid differentiation factor MyD88 is the essential adaptor protein that integrates and transduces intracellular signals generated by multiple Toll-like receptors including receptor complex for interleukin (IL) 1beta, a key inflammatory cytokine. IL1beta receptor complex interacts with MyD88 via the Toll/IL1 receptor (TIR) domain. Here we report structure-function studies that help define the MyD88 TIR domain binding sites involved in IL1beta-induced protein-protein interactions. The MyD88 TIR domain, employed as a dominant negative inhibitor of IL1beta signaling to screen MyD88 TIR mutants, lost its suppressing activity upon truncation of its Box 3. Accordingly, mutations of Box 3 residues 285-286 reversed the dominant negative effect of the MyD88 TIR domain on IL1beta-induced and NFkappaB-dependent reporter gene activity and IL6 production. Moreover, mutations of residues 171 in helix alphaA, 195-197 in Box 2, and 275 in betaE-strand had similar functional effects. Strikingly, only mutations of residues 195-197 eliminated the TIR-TIR interaction of MyD88 and IL1 receptor accessory protein (IL1RAcP), whereas substitution of neighboring canonical Pro200 by His was without effect. Mutations in Box 2 and 3 prevented homotypic MyD88 oligomerization via TIR domain. Based on this structure-function analysis, a three-dimensional docking model of TIR-TIR interaction between MyD88 and IL1RAcP was developed.
Chunsheng Li, Jozef Zienkiewicz, Jacek Hawiger

1385 related Products with: Interactive sites in the MyD88 Toll/interleukin (IL) 1 receptor domain responsible for coupling to the IL1beta signaling pathway.

2 Pieces/Box2 Pieces/Box100ug100ug 100ul100ug2 Pieces/Box100ug

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#12368275   2002/10/03 To Up

Characterization of signaling pathways activated by the interleukin 1 (IL-1) receptor homologue T1/ST2. A role for Jun N-terminal kinase in IL-4 induction.

T1/ST2 is a member of the interleukin (IL)-1 receptor superfamily, possessing three immunoglobulin domains extracellularly and a Toll/IL1R (TIR) domain intracellularly. The ligand for T1/ST2 is not known. T1/ST2 is expressed on Type 2 T helper (Th2) cells, and its role appears to be in the regulation of Th2 cell function. Here, we have investigated T1/ST2 signal transduction, using either transient overexpression of T1/ST2 or a cross-linking monoclonal antibody to activate cells. We demonstrate that T1/ST2 does not activate the transcription factor NF-kappaB when overexpressed in murine thymoma EL4 cells, or in the mast cell line P815 treated with the anti-T1/ST2 antibody. However, a chimera comprising the extracellular domain of the type 1 IL-1 receptor and the intracellular domain of T1/ST2 activates NF-kappaB both by overexpression and in response to IL-1. This artificial activation requires the IL1RAcP recruited via the extracellular portion (IL1R1) of the chimera. T1/ST2 is, however, able to activate the transcription factor activator protein-1 (AP-1), increase phosphorylation of c-Jun, and activate the MAP kinases c-Jun N-terminal kinase (JNK), p42/p44 and p38. Anti-T1/ST2 also induces the selective expression of IL-4 but not IFN-gamma in naive T cells. Importantly, this effect is blocked by prior treatment with the JNK inhibitor SP600125 confirming that JNK as a key effector in T1/ST2 signaling. The lack of effect on NF-kappaB when T1/ST2 is homodimerized identifies T1/ST2 as the first member of the IL-1 receptor superfamily so far studied that is apparently unable to activate NF-kappaB, consistent with evidence indicating the lack of a role for NF-kappaB in Th2 cell function.
Elizabeth K Brint, Katherine A Fitzgerald, Philip Smith, Anthony J Coyle, Jose-Carlos Gutierrez-Ramos, Padraic G Fallon, Luke A J O'Neill

1040 related Products with: Characterization of signaling pathways activated by the interleukin 1 (IL-1) receptor homologue T1/ST2. A role for Jun N-terminal kinase in IL-4 induction.

100ul100ug200ul100ug100ug400Tests100ug100ug Lyophilized100ug Lyophilized100ug Lyophilized100ul100ug

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