TLR4 Protein, Human (sf9, His, Solution)

TLR4, a transmembrane receptor, operates as a pattern recognition receptor, detecting pathogen- and damage-associated molecular patterns (PAMPs and DAMPs) to initiate innate immune responses. At the plasma membrane, it collaborates with LY96 to recognize bacterial lipopolysaccharide (LPS), triggering an immune response. Moreover, TLR4 is involved in LPS-independent inflammatory responses induced by free fatty acids and Ni(2+). The receptor acts through signaling pathways involving MYD88, TIRAP, and TRAF6, leading to NF-kappa-B activation and cytokine secretion. Additionally, CD14-mediated TLR4 internalization via endocytosis initiates a MYD88-independent signaling pathway through the TICAM1-TBK1-IRF3 axis, resulting in type I interferon production. TLR4 activation also leads to the activation of the NLRP3 inflammasome and a positive feedback loop between autophagy and the NF-kappa-B signaling cascade. In complex with TLR6, TLR4 promotes inflammation in monocytes/macrophages, and ligand binding triggers internalization and an inflammatory response. TLR4's diverse interactions, including those with LY96, MYD88, TIRAP, TICAM2, NOX4, CNPY3, HSP90B1, CD36, WDFY1, SMPDL3B, CEACAM1, RFTN1, SCIMP, TRAF3IP3, and TREM1, further highlight its pivotal role in orchestrating immune responses and cellular signaling.