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anti-Human TIRAP Antikörper:
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Human Polyclonal TIRAP Primary Antibody für IHC (p), WB - ABIN541436
Takeda, Kaisho, Akira: Toll-like receptors. in Annual review of immunology 2003
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Human Polyclonal TIRAP Primary Antibody für WB - ABIN550244
Vogel, Fitzgerald, Fenton: TLRs: differential adapter utilization by toll-like receptors mediates TLR-specific patterns of gene expression. in Molecular interventions 2004
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Human Polyclonal TIRAP Primary Antibody für ELISA, WB - ABIN268824
Andreakos, Sacre, Smith, Lundberg, Kiriakidis, Stonehouse, Monaco, Feldmann, Foxwell: Distinct pathways of LPS-induced NF-kappa B activation and cytokine production in human myeloid and nonmyeloid cells defined by selective utilization of MyD88 and Mal/TIRAP. in Blood 2004
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Human Polyclonal TIRAP Primary Antibody für IHC, WB - ABIN6688763
Du, Qiao, Chen, Chen, Liu, Lin, Wang, Xie: Toll-Like Receptor 4 Mediates Methamphetamine-Induced Neuroinflammation through Caspase-11 Signaling Pathway in Astrocytes. in Frontiers in molecular neuroscience 2017
Human Polyclonal TIRAP Primary Antibody für ELISA, WB - ABIN547544
Farina, Krumbholz, Giese, Hartmann, Aloisi, Meinl: Preferential expression and function of Toll-like receptor 3 in human astrocytes. in Journal of neuroimmunology 2005
Human Polyclonal TIRAP Primary Antibody für IF (p), IHC (p) - ABIN872309
Rolf, Kariminia, Ivison, Reid, Schultz: Heterodimer-specific TLR2 stimulation results in divergent functional outcomes in B-cell precursor acute lymphoblastic leukemia. in European journal of immunology 2015
Zebrafish Tirap adaptor lacks the phosphatidylinositol 4,5-bisphosphate binding motif, which could partially explain zebrafish insensitivity to lipopolysaccharide, hence its resulting inability to activate downstream Toll-like receptor signaling.
GPR108, an NF-kappaB activator suppressed by TIRAP, negatively regulates TLR-triggered immune responses.
TIRAP is phosphorylated at Thr28 within its phosphoinositide (PI)-binding motif (PBM), which leads to its ubiquitination and degradation. The authors demonstrate that phosphorylation distorts the helical structure of TIRAP PBM, reducing PI interactions and cell membrane targeting.
MAL is not disulfide-bonded and requires glutathionylation of C91 for signaling.
The Mal-Toll/interleukin-1 receptor (TIR) domains AB loop is capable of mediating direct binding to the TIR domains of TLR4 and MyD88 simultaneously.
MAL is multifunctional and integral for the molecular control of bacterial infections as well as inflammatory diseases. [Review]
Data indicate that TcpB (Q8YF5, BtpA/Btp1) interacts with MAL, MyD88, and TLR4 but interferes only with the MAL-TLR4 interaction.
Docking and physicochemical studies indicated that BTK was involved in close contact with Tyr86 and Tyr106 of MAL, whereas PKCdelta may phosphorylate Tyr106 only.
Results show that MAL protein binds to and regulates MYD88.
Here the authors show that MAL TIR domains spontaneously and reversibly form filaments in vitro. They also form cofilaments with TLR4 TIR domains and induce formation of MyD88 assemblies.
The major allele A of rs2511521 located in DRD2 and the minor allele T of rs625413 located in TIRAP are significantly associated with increased risk of food addiction in overweight/obese subjects with low/zero food addiction symptoms.
Combined targeting of UBAP1 and toll-like receptor adaptors TIRAP and MyD88 by Pseudomonas aeruginosa PumA impedes both cytokine and toll-like receptor signalling, highlighting a novel strategy for innate immune evasion.
Epistatic interaction between MyD88 and TIRAP against Helicobacter pylori.
Presence of at least one copy of the TIRAP (2054C > T) variant may be associated with severity of bronchopulmonary dysplasia among preterm neonates.
Chances of malaria caused by Plasmodium falciparum were low in CC genotype carriers in comparison to other genotypes
TIRAP polymorphisms are associated with progression and survival of patients with symptomatic myeloma.
This present meta-analysis suggests TIRAP C539T polymorphism is significantly correlated with reduced risk of TB infection, with stronger effect in European.
The TIRAP S180L and TLR9 -1486 T>C polymorphism showed no association with systemic lupus erythematosus (SLE) risk, but they influenced SLE phenotype.
Evaluated the possible association between TIRAP rs1893352 and rs8177374 (S180L) gene polymorphisms and pulmonary tuberculosis in a sample of Iranian population.
CCL2rs2530797A/A and TIRAPrs8177376A/A were associated to an increase susceptibility to Chagas disease cardiomyopathy.
TIRAP rs81777374 is associated with resistance to pulmonary tuberculosis.
TIRAP plays a functional role in transducing LPS signaling from TLR-4 to downstream effector molecules involved in NF-kappaB activation, and TIRAP promotes apoptotic signaling
TIARP independently down-regulated CXCL2 and IL-6 production by fibroblast-like synoviocytes, and the expression of chemokine receptors (CXCR1 and CXCR2) in neutrophils, with resultant reduction of neutrophil migration into arthritic joints.
Our key findings provide novel insights into the mechanism of action of heterotrimeric complex (PKCdelta-TIRAP-p38) in proinflammatory cytokine expression, which controls the development of the inflammatory trigger in stimulated macrophages.
Results suggest that TIR domain-containing adaptor protein positively regulated BV2 microglial M1 polarization through toll-like receptor 4 -mediated Transforming Growth Factor-Beta-Activated Kinase 1/I-Kappa-B Kinase /Nuclear Factor of Kappa Light Polypeptide Gene Enhancer in B-Cells (TAK1/IKK/NF-kappaB), mitogen-activated protein kinases and Akt signalling pathways.
The adapter Mal (encoded by TIRAP) has appeared crucial for the cytokine production by Ly6C(lo) but not by Ly6C(hi) monocytes. The protein Mal was necessary to induce cytokine synthesis by Ly6C(lo) monocytes after triggering TLR2 or TLR9.
genetic polymorphism is associated with interferon-gamma signaling and susceptibility to infections
TIRAP/Mal deficiency significantly inhibited the activity of titanium particles with adherent bacterial debris to stimulate in vivo osteolysis and in vitro cytokine mRNAs and secretion.
A critical role for the TLR signaling adapter Mal in alveolar macrophage-mediated protection against Bordetella pertussis.
The D-helix peptide, 2R9, also potently inhibited TLR4, TLR7, and TLR9, but not TLR3 or TNF-alpha signaling. Cell imaging, co-immunoprecipitation, and in vitro studies demonstrated that 2R9 preferentially targets TIRAP.
MyD88 adaptor-like (Mal) functions in the epithelial barrier and contributes to intestinal integrity via protein kinase C.
our data reveal a differential, but inflammation-independent, requirement for Mal and MyD88 during TLR2-promoted gastric tumourigenesis.
Mal is essential for the maintenance of intestinal homeostasis and expression of Mal in nonhematopoietic cells prevents chronic intestinal inflammation that may predispose to colon neoplasia.
Study reports that, in response to natural activators of innate immunity, the sorting adaptor TIRAP regulates TLR signaling from the plasma membrane and endosomes.
TIRAP plays a central role in regulating the effects of lipopolysaccharides or lipoteichoic acid on chlorpromazine-induced hepatotoxicity.
PIP5Kalpha promotes TLR4-associated microglial inflammation by mediating PIP(2)-dependent recruitment of TIRAP to the plasma membrane
PTEN deletion impeded Mal localization at the plasma membrane and suppressed Mal-TLR5 interaction. These results suggest that, by controlling Mal recruitment, PTEN regulates TLR5-induced inflammatory responses.
Toll-like receptor signal adaptor protein MyD88 is required for sustained endotoxin-induced acute hypoferremic response in mice.
findings support that ozone-induced airway hyperresponsiveness is dependent on the HA-TLR4-MyD88-TIRAP signaling pathway
the effect of TLR2 on drug-metabolizing enzyme genes in hepatocytes was mediated by TIRAP, whereas TIRAP was not involved in mediating the effects of TLR2 on cytokine expression in the liver
Long-term exposure of murine airway to IL-1beta induces up- and down-regulation of mRNA expression for Toll-IL-1 receptor signal molecules.[Toll-IL-1 receptor]
The innate immune system recognizes microbial pathogens through Toll-like receptors (TLRs), which identify pathogen-associated molecular patterns. Different TLRs recognize different pathogen-associated molecular patterns and all TLRs have a Toll-interleukin 1 receptor (TIR) domain, which is responsible for signal transduction. The protein encoded by this gene is a TIR adaptor protein involved in the TLR4 signaling pathway of the immune system. It activates NF-kappa-B, MAPK1, MAPK3 and JNK, which then results in cytokine secretion and the inflammatory response. Alternative splicing of this gene results in several transcript variants\; however, not all variants have been fully described.
MyD88 adapter-like protein
, Toll-interleukin 1 receptor domain-containing adaptor protein
, toll/interleukin-1 receptor domain-containing adapter protein
, TIR domain-containing adaptor protein
, Toll-like receptor adaptor protein
, adapter protein wyatt
, adaptor protein Wyatt
, toll-interleukin 1 receptor domain-containing adaptor protein
, TIR domain-containing adapter protein
, Toll-like receptor 4 adaptor protein
, myD88 adapter-like protein