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anti-Human LY96 Antibodies:
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Human Polyclonal LY96 Primary Antibody for IHC (p), IHC - ABIN252602
Kunda, Cavicchia, Acosta: Lipopolysaccharides and trophic factors regulate the LPS receptor complex in nodose and trigeminal neurons. in Neuroscience 2014
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Human Monoclonal LY96 Primary Antibody for FACS - ABIN2192087
Pugin, Stern-Voeffray, Daubeuf, Matthay, Elson, Dunn-Siegrist: Soluble MD-2 activity in plasma from patients with severe sepsis and septic shock. in Blood 2004
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Human Monoclonal LY96 Primary Antibody for FACS, InhA - ABIN2192085
Daubeuf, Mathison, Spiller, Hugues, Herren, Ferlin, Kosco-Vilbois, Wagner, Kirschning, Ulevitch, Elson: TLR4/MD-2 monoclonal antibody therapy affords protection in experimental models of septic shock. in Journal of immunology (Baltimore, Md. : 1950) 2007
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Human Monoclonal LY96 Primary Antibody for FACS - ABIN2192086
Elson, Dunn-Siegrist, Daubeuf, Pugin: Contribution of Toll-like receptors to the innate immune response to Gram-negative and Gram-positive bacteria. in Blood 2007
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Human Monoclonal LY96 Primary Antibody for IHC (p), WB - ABIN534453
Takeda, Kaisho, Akira: Toll-like receptors. in Annual review of immunology 2003
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Human Monoclonal LY96 Primary Antibody for IHC (p), WB - ABIN534452
Janeway, Medzhitov: Innate immune recognition. in Annual review of immunology 2002
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These results show that isofraxidin binds to and inhibits MD-2, thus preventing TLR4/MD-2 complex formation without altering TLR2 signalling. We demonstrated that isofraxidin promoted cell proliferation and inhibited the lipopolysaccharide induced inflammatory response through suppressing the activation of the TLR4/MD-2 axis and NF-kappaB signalling in human osteoarthritis chondrocytes.
An increase of MD-2 expression levels was associated with an absolute mortality risk increase in dilated cardiomyopathy patients.
sTLR4/MD-2 complex inhibits colorectal cancer migration and invasiveness in vitro and in vivo by lncRNA H19 down-regulation.
MD-2 siRNA or plasmid further confirmed the efficacy of Iturin A by suppressing MD-2/TLR4 signaling pathway. The in silico docking study showed that the Iturin A interacted well with the MD-2 in MD-2/TLR4 receptor complex. Conclusively, inhibition of MD-2/TLR4 complex with Iturin A offered strategic advancement in cancer therapy.
data confirm that engineered human cells expressing TLR4, MD2 and CD14 can respond to CMP with NF-kappaB activation and the response can be influenced by variations in CMP-mannosylation
The observations suggest that MD-2 helps to regulate lipopolysaccharide-induced NLRP3 inflammasome activation and the inflammatory response in NR8383 cells, and likely does so by affecting MyD88/NF-kappaB signaling.
MD2 plays an important role in induction of allergic sensitization to cat dander and common pollens relevant to human allergic diseases.
we report that exogenous CnB is taken up by cells in a time- and concentration-dependent manner via clathrin-dependent receptor-mediated internalization. Our findings further confirm that uptake is mediated by the TLR4/MD2 complex together with the co-receptor CD14
In this study, a novel naturally occurring spliceosome of human MD2, termed as MD2-T3, has been identified.
Results show that cigarette smoke may alter innate immune responses reducing the expression of the MD2, a molecule with an important role in TLR4 signaling.
Predominantly hydrophobic interactions between MD-2 and TLR4 contribute to the stabilization of the TLR4/MD-2/metal ion complex in a conformation that enables activation.
The intensity of the intra-amniotic inflammatory response to bacteria or perhaps to other TLR4 ligands may be facilitated through synthesis and release of sMD2 by the amniochorion.
Three genes (LY96, IL8 DPR) were significantly downregulated over time. This finding was confirmed in a validation cohort of stroke patients (n=8).
The study revealed the impact of specific residues and regions of MD-2 on the binding of lipolysaccharides and TLR4.
Gene polymorphisms of MD2 and GM2A were associated with the occurrence or severity of neonatal necrotizing enterocolitis.
In patients undergoing CABG surgery, we found genetic polymorphisms in LY96 associated with decreased risk of postoperative AF.
Aminoarabinose residues in lipid A contribute to Burkholderia lipid A binding to the TLR4.Myeloid Differentiation Factor 2 complex.
TLR4 along with its accessory protein MD-2 builds a heterodimeric complex that specifically recognizes lipopolysaccharides, which are present on the cell wall of gram-negative bacteria, activating the immune response. (Review)
genetic polymorphism is associated with asthma exacerbations in children
In monocytes of sepsis, MD-2 expression was found to be regulated by STAT1.
These results provide further evidence for the critical role of MD2 in the development of non-alcoholic steatohepatitis.
Studied anti-inflammatory effects of ethyl acetate extracts of E. sagittatum (Ying-Yang-Huo) and found it to inhibit toll-like receptor 4(TLR4)/ lymphocyte antigen 96(MD-2) thru the NF-kappaB signal pathway.
We conclude that MD2 is a significant contributor in the Ang II-induced kidney inflammatory injury in chronic renal diseases.
Blockade of MD2 prevents obesity-induced inflammation and nephropathy.
MD2 is essential to obesity-related cardiac hypertrophy through activating JNK/ERK and NF-kappaB-dependent cardiac inflammatory pathways. Targeting MD2 would be a therapeutic approach to prevent obesity-induced cardiac injury and remodeling.
RTFs contribute to the regulation of LPS-induced inflammatory response in RAW264.7 cells through TLR4/MD-2 mediated NF-kappaB and JNK pathway. It
This study provides evidence that MD2 plays a key role in the pathogenesis of retinal I/R damage.
Data suggest that C4bp prevents interaction between Tlr4/MD-2 and its ligand; C4bp does not appear to interact with Tlr3; C4bp binds to macrophage surface Tlr4 and inhibits Tlr/Tlr ligand interaction, thereby inhibiting Tlr4 activation. (C4bp = complement component 4 binding protein; Tlr = toll-like receptor; MD-2 = myeloid differentiation protein-2)
Oxidative stress in retinal ischemia-reperfusion injury activates TLR4 signaling via MD2.
Neoseptin-3 and lipid A form dissimilar molecular contacts to achieve receptor activation; hence strong TLR4/MD-2 agonists need not mimic LPS
Here we demonstrate that cholesterol binds to myeloid differentiation-2 (MD-2), a TLR4 ancillary molecule.
MD-2 is a critical regulator of the establishment of allergic airway sensitization to HDM in mice. Serum MD-2 may represent a potential biomarker for the amplification of allergic sensitization and allergic inflammation.
Data show that myeloid differentiation factor 2 (MD-2) binds specifically to disulfide isoform of box protein 1, high mobility group (HMGB1) to facilitate toll-like receptor 4 (TLR4)-dependent signaling.
Carbon monoxide treatment reduces the expression of the TLR4/MD2 complex on the surface of myeloid cells, which renders them resistant to lipopolysaccharide priming in vitro, as well as in vivo in a model of endotoxic shock.
Mechanistically, engagement of MD-2 by PTX3-opsonized Aspergillus conidia activated the TLR4/Toll/IL-1R domain-containing adapter inducing IFN-beta-dependent signaling pathway converging on IL-10.
SAA3 directly binds MD-2 and activates the MyD88-dependent TLR4/MD-2 pathway.
Monophosphoryl lipid A is unable to efficiently form TLR4/MD-2 heterotetramers, but it still needs heterotetramer formation for the full extent of signaling it is able to achieve.
Data show that rifampin binds to myeloid differentiation protein 2 (MD-2), the key coreceptor for innate immune TLR4.
This gene encodes a protein which associates with toll-like receptor 4 on the cell surface and confers responsiveness to lipopolysaccyaride (LPS), thus providing a link between the receptor and LPS signaling. Studies of the mouse ortholog suggest that this gene may be involved in endotoxin neutralization. Alternative splicing results in multiple transcript variants encoding different isoforms.
myeloid differentiation protein-2
, protein MD-2
, myeloid differentiation factor-2
, LPS co-receptor MD-2
, lymphocyte antigen 96
, Protein MD-2