TLR2 Protein, Human (sf9, His)

TLR2 protein collaborates with LY96 to orchestrate the innate immune response against bacterial lipoproteins and various microbial cell wall components. Additionally, TLR2 forms functional complexes with either TLR1 or TLR6 to recognize bacterial lipopeptides. Through the signaling pathways involving MYD88 and TRAF6, TLR2 activation leads to NF-kappa-B activation, cytokine secretion, and the initiation of inflammatory responses. The receptor plays a pivotal role in recognizing specific ligands, such as mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2) and B.burgdorferi outer surface protein A lipoprotein (OspA-L), often in cooperation with TLR6. TLR2 engages in complex interactions with other receptors, including CD14 and CD36, to form activation clusters that trigger signaling events at the cell surface before being directed to the Golgi in a lipid-raft dependent pathway. Furthermore, TLR2 is crucial for the normal uptake of M.tuberculosis, and its interactions extend to various regulatory proteins such as MYD88, TICAM1, and TIRAP.