Recombinant human TLR4 protein (Active)
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(5 Publications)
Recombinant human TLR4 protein (Active) is a Human Fragment protein, in the 24 to 632 aa range, expressed in HEK 293 cells, with >95%, suitable for SDS-PAGE, FuncS, HPLC.
View Alternative Names
CD284, Toll-like receptor 4, hToll, TLR4
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Specifications
Form
Lyophilized
Additional notes
>= 95% by HPLC analysis.
General info
Function
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, PubMed : 17803912, PubMed : 15852007). 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.
Sequence similarities
Belongs to the Toll-like receptor family.
Post-translational modifications
N-Glycosylation of Asn-526 and Asn-575 by STT3A-containing OST-A complex is necessary for the expression of TLR4 on the cell surface and the LPS-response (PubMed:11706042, PubMed:38670073). Likewise, mutants lacking two or more of the other N-glycosylation sites were deficient in interaction with LPS (PubMed:11706042, PubMed:38670073).. Phosphorylated on tyrosine residues by LYN after binding lipopolysaccharide.. Ubiquitinated by RNF128 via 'Lys-28'-linked polyubiquitin chains, leading to proteasomal degradation.
Target data
Publications (5)
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Journal of biomedical science 32:19 PubMed39930418
2025
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Cell communication and signaling : CCS 23:64 PubMed39910535
2025
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The EMBO journal 43:4954-4983 PubMed39294473
2024
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Cell reports 41:111562 PubMed36288690
2022
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Frontiers in oncology 11:736882 PubMed34900687
2021
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Product promise
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