Recombinant human TLR4 protein (Active) is a Human Fragment protein, in the 24 to 632 aa range, expressed in HEK 293, with >=95% purity and suitable for SDS-PAGE, FuncS, HPLC.
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| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
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Transmembrane receptor that functions as a pattern recognition receptor recognizing pathogen- and damage-associated molecular patterns (PAMPs and DAMPs) to induce innate immune responses via downstream signaling pathways (PubMed:10835634, PubMed:15809303, PubMed:16622205, PubMed:17292937, PubMed:17478729, PubMed:20037584, PubMed:20711192, PubMed:23880187, PubMed:27022195, PubMed:29038465). At the plasma membrane, cooperates with LY96 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:27022195). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate, and Ni(2+) (PubMed:20711192). Mechanistically, acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:10835634, PubMed:21393102, PubMed:27022195, PubMed:36945827, PubMed:9237759). Alternatively, CD14-mediated TLR4 internalization via endocytosis is associated with the initiation of a MYD88-independent signaling via the TICAM1-TBK1-IRF3 axis leading to type I interferon production (PubMed:14517278). In addition to the secretion of proinflammatory cytokines, initiates the activation of NLRP3 inflammasome and formation of a positive feedback loop between autophagy and NF-kappa-B signaling cascade (PubMed:32894580). In complex with TLR6, promotes inflammation in monocytes/macrophages by associating with TLR6 and the receptor CD86 (PubMed:23880187). Upon ligand binding, such as oxLDL or amyloid-beta 42, the TLR4:TLR6 complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway (PubMed:23880187). In myeloid dendritic cells, vesicular stomatitis virus glycoprotein G but not LPS promotes the activation of IRF7, leading to type I IFN production in a CD14-dependent manner (PubMed:15265881, PubMed:23880187). Required for the migration-promoting effects of ZG16B/PAUF on pancreatic cancer cells.
CD284, Toll-like receptor 4, hToll, TLR4
Recombinant human TLR4 protein (Active) is a Human Fragment protein, in the 24 to 632 aa range, expressed in HEK 293, with >=95% purity and suitable for SDS-PAGE, FuncS, HPLC.
>= 95% by HPLC analysis.
Transmembrane receptor that functions as a pattern recognition receptor recognizing pathogen- and damage-associated molecular patterns (PAMPs and DAMPs) to induce innate immune responses via downstream signaling pathways (PubMed:10835634, PubMed:15809303, PubMed:16622205, PubMed:17292937, PubMed:17478729, PubMed:20037584, PubMed:20711192, PubMed:23880187, PubMed:27022195, PubMed:29038465). At the plasma membrane, cooperates with LY96 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:27022195). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate, and Ni(2+) (PubMed:20711192). Mechanistically, acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:10835634, PubMed:21393102, PubMed:27022195, PubMed:36945827, PubMed:9237759). Alternatively, CD14-mediated TLR4 internalization via endocytosis is associated with the initiation of a MYD88-independent signaling via the TICAM1-TBK1-IRF3 axis leading to type I interferon production (PubMed:14517278). In addition to the secretion of proinflammatory cytokines, initiates the activation of NLRP3 inflammasome and formation of a positive feedback loop between autophagy and NF-kappa-B signaling cascade (PubMed:32894580). In complex with TLR6, promotes inflammation in monocytes/macrophages by associating with TLR6 and the receptor CD86 (PubMed:23880187). Upon ligand binding, such as oxLDL or amyloid-beta 42, the TLR4:TLR6 complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway (PubMed:23880187). In myeloid dendritic cells, vesicular stomatitis virus glycoprotein G but not LPS promotes the activation of IRF7, leading to type I IFN production in a CD14-dependent manner (PubMed:15265881, PubMed:23880187). Required for the migration-promoting effects of ZG16B/PAUF on pancreatic cancer cells.
Belongs to the Toll-like receptor family.
N-glycosylated. Glycosylation of Asn-526 and Asn-575 seems to be necessary for the expression of TLR4 on the cell surface and the LPS-response. Likewise, mutants lacking two or more of the other N-glycosylation sites were deficient in interaction with LPS.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Migrates with an apparent molecular mass of approximately 90-100 kDa by SDS-PAGE gel, under reducing and non-reducing conditions.
Toll-like receptor 4 (TLR4) is a membrane protein involved in the innate immune response. It serves as a receptor that recognizes pathogen-associated molecular patterns such as lipopolysaccharides from bacterial cell walls. Often referred to by its alternate names TLR-2 and CD284 this protein has a molecular weight of approximately 95 kDa. TLR4 is mainly expressed on the surface of immune cells like macrophages and dendritic cells enabling these cells to detect and respond to microbial invaders effectively.
TLR4 plays an important role in activating the immune system. It forms a complex with myeloid differentiation factor 2 (MD-2) to facilitate binding to its ligands. Upon activation TLR4 triggers a signaling cascade that leads to the release of pro-inflammatory cytokines and interferons which are important for initiating the immune response. This early detection mechanism alerts the immune system to the presence of pathogens allowing the body to mount a defense.
TLR4 participates in the nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) and mitogen-activated protein kinase (MAPK) signaling pathways. These pathways are central to the inflammatory response with TLR4 acting as a sensor that activates downstream components like the MyD88 and TRIF proteins. These interactions result in the expression of genes that produce cytokines and enzymes involved in inflammation and immunity.
TLR4 has been implicated in the development of sepsis and atherosclerosis. In sepsis TLR4 recognizes lipopolysaccharides from bacterial infections which can cause excessive inflammation if uncontrolled. In atherosclerosis TLR4 receptors on vascular cells respond to endogenous ligands such as oxidized low-density lipoproteins contributing to plaque formation. The TLR4 interaction with proteins like CD14 and MD-2 is significant as it influences the inflammatory pathways that exacerbate these conditions.
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