Hepatic stellaque cells (HSCS) play an important role in the appearance of liver fibrosis, which can be treated by the inhibition and inversion of HSC activation. The silencer Gene TLR4 mediated by RNA could be a potential therapeutic approach for hepatic fibrosis. The crucial challenge of this method is the absence of an effective distribution system for the introduction of RNAI into the target cells. HSCS have an increased capacity of vitamin A because they contain retinoic acid receptors (rars).
In the current study, we have developed modified cationic liposomes with vitamin A to improve the specificity of delivery vehicles for HSCS. The result of this study revealed that cationic coupled VITA liposomes delivered the TLR4 lampshade to AHSCS more efficiently, compared to uncontrolled cationic liposomes, both in the conditions in vitro and in vivo. In addition, as evident from the result of this study, the TLR4 gene has inhibited HSCS activation and attenuates liver fibrosis via the inactivation of the transcription of the NF-KB, the secretion of the pro-inflammatory cytokines and The reactive synthesis of oxygen species (ROS).
Thus, VITA coupled liposomes encapsulated with the TLR4-SHRNA can be an effective therapeutic agent for liver fibrosis. The toll type 4 (TLR4) receiver, a key model recognition receiver, initiates the innate immune response and leads to chronic and acute inflammation. In recent decades, the accumulation of evidence involved an inflammatory intervention mediated by the TLR4 in the regulation of the hypertrophic renovation of myocardium, indicating that the regulation of the TLR4 signaling path can be an effective strategy for the management of the physiopathology of Cardiac hypertrophy. Given the meaning of TLR4, it is imperative to examine the molecular mechanisms and roles underlying TLR4 signaling in cardiac hypertrophy. We examine here exhaustively the current knowledge of the TLR4 inflammatory response and its interaction ligands and co-receptors, as well as the activation of various intracellular signals.
Previous research revealed that the GUT microbioma has a marked impact on the insufficiency of the acute liver (ALF). Here we evaluated the impact of betaine on the intestinal microbiota composition in an ALF animal model. The potential protective effect of betaine also regulating the toll receptor responses (TLR4) has also been explored. The experiments of mouse and cells included normal, models and betaine groups. The small line of IEC-18 rat intestinal cells was used for in vitro experiments.
Betaine has improved small intestinal tissue and damage to IEC-18 model of the model group by reducing the high expression of TLR4 and MYD88. In addition, the intestinal permeability of the model group has been improved by improving the expression of tight junction proteins (ZO) -1 and occlusin. There were 509 operational taxonomic units (otus) that have been identified in faecal samples of the mouse, including 156 main microbiomas taxa.
Betaine significantly improved microbial communities, impoverishes the microbiota constituents of Gut Coriobacteriaceae, Lachnospirsae, Enterorhabdus and Coriobacterial and significantly enriched the taxa bacteroids, bacteria, parabaches and prevotella in the model group. Between effectively improved intestinal lesions in the ALF by inhibiting the TLR4 / MyD88 signaling path, improving the intestinal mucosa barrier and maintaining the intestinal microbiota composition.
Acinar cell necrosis is one of the most important physiopathological changes in acute pancreatitis (AP). Asiaticoside (AS) is a Triterpene compound with confirmed activities of apoptosis and necrosis. However, the specific effects of as on AP have not been determined. In this study, we aimed at studying the protective effect of as on AP using two mouse models. In the cake-induced acute pancreatitis (map) model, we found that the administration reduces serum amylase levels and relieved the histopathological manifestations of pancreatic tissue in a dose-dependent manner. And toll receptor levels 4 (TLR4) and necrotic related proteins (RIP3 and P-MLKL) of pancreatic tissue have been reduced after administration. In addition, the TLR4 deficiency has eliminated the protective effect of as on AP induced by cotes in mice.
Correspondingly, we have elucidated the effect of as in vitro and found that, as protected against pancreatic acinar cells, necrosis and TAK-242 have neutralized this protective effect. Meanwhile, we found that, as improved the severity of the severity of pancreatic tissue and a pulmonary injury associated with pancreatitis in a pattern of acute pancreatitis severely induced by L-arginine. In addition, the molecular mooring results revealed an interaction between as and TLR4. Taken together, our data for the first time confirmed the protective effects of as on AP in mice via the TLR4 channel. The toll receiver 4 (TLR4) is an inflammatory receptor ubiquitously expressed in immune cells as well as skeletal muscles and other metabolic tissues.
Description: Interleukin 23 receptor is a type I cytokine receptor. IL23R is its human gene. The protein encoded by this gene is a subunit of the receptor for IL23A/IL23. This protein pairs with the receptor molecule IL12RB1/IL12Rbeta1, and both are required for IL23A signaling. This protein associates constitutively with Janus kinase 2 (JAK2), and also binds to transcription activator STAT3 in a ligand-dependent manner.
Description: Interleukin 23 receptor is a type I cytokine receptor. IL23R is its human gene. The protein encoded by this gene is a subunit of the receptor for IL23A/IL23. This protein pairs with the receptor molecule IL12RB1/IL12Rbeta1, and both are required for IL23A signaling. This protein associates constitutively with Janus kinase 2 (JAK2), and also binds to transcription activator STAT3 in a ligand-dependent manner.
Recombinant Mouse IL-23R/IL-23 Receptor Protein, Fc His Tag
Description: Recombinant Mouse Interleukin-23 Receptor is produced by our Mammalian expression system and the target gene encoding Gly24-Asp372 is expressed with a Fc tag at the C-terminus.
Description: The multifunctional factor interleukin 6 (IL-6) exerts its activities through binding to a high-affinity receptor complex consisting of two membrane glycoproteins: an 80 kDa component receptor that binds IL-6 with low affinity (IL-6 R) and a signal-transducing component of 130 kDa (gp 130) that does not bind IL-6 by itself, but is required for high-affinity binding of IL-6 by the complex. A soluble form of the IL-6 R alpha has been found in the urine of healthy adult humans. This soluble receptor apparently arises from proteolytic cleavage of membrane-bound IL-6 R alpha. No naturally-occurring mRNA encoding a truncated form of the IL-6 R alpha has been reported. Soluble forms of human and murine IL-6 R alphas have been constructed, however, by insertion of termination codons into the regions of the IL-6 R alpha cDNAs encoding the external portions of the receptors and prior to the transmembrane domains. These soluble receptors have been expressed in COS-7 and CHO cells and have been shown to bind to IL-6 in solution and to augment the activity of IL-6 as a result of the binding of the IL-6/IL-6 R alpha complex to membrane-bound gp130.
Description: The specific high affinity functional IL-9 receptor complex contains the common gamma chain as well as the IL-9 receptor (IL-9 R). The mouse and human transmembrane proteins share 53% amino acid sequence identity. As a result of alternate splicing, cDNA clones encoding isoforms of IL-9 R, including a putative soluble form, have also been identified. Cells known to express IL-9 R include T cells, neutrophils, mast cells and macrophages.
Description: IL-17 binds to IL-17 receptors (IL-17 R), which share no homology with any known family of receptors. While the expression of IL-17 is restricted to activated T cells, IL-17 R mRNA exhibits a broad tissue distribution, and has been detected in virtually all cells and tissues tested. The amino acid sequence of human IL-17 R is 69% identical to mouse IL-17 R.
Description: Human IL-18 R cDNA encodes a 541 amino acid (aa) precursor type I membrane protein with a hydrophobic signal, an extracellular domain comprised of three immunoglobulin-like domains, a transmembrane domain and a cytoplasmic region of approximately 200 aa residues. Human and mouse IL-18 R share 65% amino acid sequence homology. IL-18 R is widely expressed in numerous tissues including spleen, thymus, leukocyte, liver, lung, heart, small and large intestine, prostate and placenta.
Description: IL-21 R, also called NILR (novel interleukin receptor) is a type I cytokine receptor with four conserved cysteine residues and an extracellular WSXWS motif. It is most closely related to IL-2 R beta and IL-9 R alpha. Mouse and human IL-21 R share 62% amino acid identity. IL-21 R is expressed on lymphoid tissues, peripheral B cells, and cell lines of T, B and natural killer cell lineage. IL-21 mediated signaling requires the common gamma chain in addition to IL-21 R.
Description: IL-17B receptor (IL-17B R), also known as IL-17Rh1, IL-17ER and EVI27, is a 502 amino acid (aa) type I membrane protein with a 17 aa signal peptide, a 275 aa extracellular domain, a 21 aa transmembrane domain and a 189 aa cytoplasmic tail. By alternative splicing, a secreted variant of IL-17B R has also been identified.
Description: IL-2 R beta is a 551 amino acid (aa) precursor type I membrane protein with a 26 aa signal peptide, a 214 aa extracellular region, a 25 aa transmembrane region and a 286 aa cytoplasmic domain. IL-2 R beta binds IL-2 as a part of the IL-2 R alpha/IL-2 R beta/common gamma chain complex.
Description: The high-affinity receptors for Interleukin-3 (IL-3), IL-5, and Granulocyte-Macrophage Colony-stimulating Factor (GM-CSF) consist of a cytokine-specific a chain, and a shared common beta chain subunit (CD131) that is essential for receptor signaling. CD131 also associates with the receptor for Erythropoietin, forming a tissue-protective heteroreceptor complex. Phosphorylation of CD131 following receptor activation imparts growth and survival signals to the responding hematopoietic cells.
Description: Interleukin 3 (IL-3) is a pleiotropic cytokine that can stimulate proliferation and differentiation of pluripotent hematopoietic stem cells as well as various lineage committed progenitors. IL-3 exerts its activity through binding to a specific cell surface receptor known as IL-3 R. IL-3 R is a heterodimeric structure composed of a 70 kDa IL-3 R alpha subunit (CD123 or beta common) and a 120-140 kDa IL-3 R beta subunit (CD131). CD131 also associates with the receptor for Erythropoietin, forming a tissue-protective hetero-receptor complex.
Description: Two types of IL-4 receptor complexes have been described. The typeI IL-4 receptor complex is composed of a high-affinity IL-4-binding subunit (referred to as IL-4 R or IL-4 R alpha) and the common gamma chain that does not bind IL-4 by itself. The type II IL-4 receptor complex is composed of IL-4 R and IL-13 R alpha 1. Besides IL-4 signals, the type II IL-4 receptor complex can also transduce IL-13 signals. In the type II complex, IL-4 R subunit binds only IL-4 and not IL-13. Similarly, the IL-13 R alpha 1 subunit binds only IL-13 and not IL-4.
Description: The biological effects of IL-7 are mediated by the binding of IL-7 to the specific cell surface receptor complex. The functional high-affinity IL-7 receptor (IL-7 R) comprises the IL-7 R alpha chain in association with the common gamma chain (gamma c). Both IL-7 R alpha and gamma c are members of the hematopoietin receptor superfamily. Human and mouse IL-7 R alpha show 64% amino acid sequence identity. IL-7 R alpha transcripts were observed in murine spleen, thymus, fetal liver, developing T cells, B cells, mature T cells and bone marrow-derived macrophages.
Description: Human and mouse IL-10 receptors are structurally related to the IFN-gamma receptor. These receptors are members of the class II subgroup of the cytokine receptor superfamily. The deduced amino acid sequence of human IL-10 R is approximately 60% identical to mouse IL-10 R. Although human IL-10 has cross-species activities and is active on mouse cells, mouse IL-10 is species-specific in its actions and does not bind to the human IL-10 receptor. The human IL-10 R gene has been mapped to chromosome 11q23.3. Recombinant IL-10 soluble receptor, consisting of the extracellular domain of IL-10 R, binds IL-10 with high affinity in solution and is a potent IL-10 antagonist.
Description: Interleukin 15 receptor alpha (IL-15 R alpha) is a high affinity receptor that specifically binds IL-15 and associates as a heterotrimer with the IL-2 receptor beta and gamma subunits (Common gamma chain, or gamma c) to initiate signal transduction. IL-15 R alpha is expressed on a wide variety of Tand B cells as well as non-lymphoid cells. Human IL-15 R alpha shares 45% amino acid sequence homology with the mouse form of the receptor. Eight isoforms of IL-15 R alpha mRNA have been identified, resulting from alternative splicing events involving different exons.
Description: IL-20 R alpha is widely expressed and is detected at high levels in multiple tissues including skin, testis, heart, placenta, salivary gland and prostate gland. The expression of IL-20 R alpha, together with that of IL-20 R beta, is upregulated in psoriatic skin lesions on keratinocytes, immune cells, and endothelial cells. IL-20 R alpha heterodimerizes with IL-20 R beta to form the functional receptor that mediates IL-19, IL-20 and IL-24 signals. IL-20 R alpha also heterodimerizes with IL-10 R beta to form the functional receptor complex for IL-26. Binding of these IL-10 family class II cytokines to their functional receptors induces activation of the JAK-STAT signal transduction pathway. At low ligand concentrations, STAT3 has been shown to be the predominant STAT proteins activated through either complexes.
Description: Interleukin 15 receptor alpha (IL-15 R alpha) is a high affinity receptor that specifically binds IL-15 and associates as a heterotrimer with the IL-2 receptor beta and gamma subunits (Common gamma chain, or gamma c) to initiate signal transduction. IL-15 R alpha is expressed on a wide variety of Tand B cells as well as non-lymphoid cells. Human IL-15 R alpha shares 45% amino acid sequence homology with the mouse form of the receptor. Eight isoforms of IL-15 R alpha mRNA have been identified, resulting from alternative splicing events involving different exons.
Description: Quantitativesandwich ELISA kit for measuring Mouse Interleukin-23 receptor (IL23R) in samples from serum, plasma, tissue homogenates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.
Description: Quantitativesandwich ELISA kit for measuring Mouse Interleukin-23 receptor(IL23R) in samples from serum, plasma, tissue homogenates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits.
Description: IL-1 receptor antagonist (IL-1ra) was originally isolated from the urine of patients with monocytic leukemia and has also been purified from adherent monocytes. The protein shows 26% amino acid homology to IL-1 beta and 19% homology to IL-1 alpha. It will compete with either factor for receptor binding, but does not interact with either one. Human IL-1ra will bind to both types of IL-1 receptor (I and II) on human cells. In mouse, IL-1RII does not bind IL-1ra.
Description: Quantitativesandwich ELISA kit for measuring Human Interleukin-23 receptor (IL-23R) in samples from serum, plasma, tissue homogenates, urine. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.
Description: Quantitativesandwich ELISA kit for measuring Human Interleukin-23 receptor (IL-23R) in samples from serum, plasma, tissue homogenates, urine. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits.
Description: The specific high affinity functional IL-9 receptor complex contains the common gamma chain as well as the IL-9 receptor (IL-9 R). The mouse and human transmembrane proteins share 53% amino acid sequence identity. As a result of alternate splicing, cDNA clones encoding isoforms of IL-9 R, including a putative soluble form, have also been identified. Cells known to express IL-9 R include T cells, neutrophils, mast cells and macrophages.
Description: Interleukin-2 receptor alpha chain (also called CD25) is a protein that in humans is encoded by the IL2RA gene.The interleukin 2 (IL2) receptor alpha (IL2RA) and beta (IL2RB) chains, together with the common gamma chain (IL2RG), constitute the high-affinity IL2 receptor. Homodimeric alpha chains (IL2RA) result in low-affinity receptor, while homodimeric beta (IL2RB) chains produce a medium-affinity receptor. Normally an integral-membrane protein, soluble IL2RA has been isolated and determined to result from extracellular proteolysis. Alternately-spliced IL2RA mRNAs have been isolated, but the significance of each is currently unknown.
Description: IL-17 binds to IL-17 receptors (IL-17 R), which share no homology with any known family of receptors. While the expression of IL-17 is restricted to activated T cells, IL-17 R mRNA exhibits a broad tissue distribution, and has been detected in virtually all cells and tissues tested. The amino acid sequence of human IL-17 R is 69% identical to mouse IL-17 R.
Description: IL-21 R, also called NILR (novel interleukin receptor) is a type I cytokine receptor with four conserved cysteine residues and an extracellular WSXWS motif. It is most closely related to IL-2 R beta and IL-9 R alpha. Mouse and human IL-21 R share 62% amino acid identity. IL-21 R is expressed on lymphoid tissues, peripheral B cells, and cell lines of T, B and natural killer cell lineage. IL-21 mediated signaling requires the common gamma chain in addition to IL-21 R.
Description: IL-17B receptor (IL-17B R), also known as IL-17Rh1, IL-17ER and EVI27, is a 502 amino acid (aa) type I membrane protein with a 17 aa signal peptide, a 275 aa extracellular domain, a 21 aa transmembrane domain and a 189 aa cytoplasmic tail. By alternative splicing, a secreted variant of IL-17B R has also been identified.
Description: Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
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The skeletal muscle develops metabolic adaptations mediated by a favorable inflammation of training for the exercise. Several inflammatory myokines, downstream of TLR4, are offered links to the metabolic benefits of the exercise. In addition, the activation of the TLR4 modifies the preference of the skeletal muscle substrate. The role of the skeletal muscle TLR4 (MTLR4) in the metabolism of the exercise has not been examined before. In this document, we aimed to specifically test the importance of MTLR4 for metabolic adaptations induced by the exercise.