Anti-Human TLR6 (Clone: TLR6.127)

The monoclonal antibody 10-3518 reacts with the human Toll-like receptor 6 (TLR6). Toll-like receptors (TLRs) are highly conserved throughout evolution. They play an essential role in initiating the innate immune response against infectious pathogens. In Drosophila, toll is required for anti-fungal response, while the related 18-wheeler is involved in antibacterial defence. In humans, ten members of the TLR family protein (TLR1 to TLR10) have been identified. TLRs recognize a wide variety of pathogen-associated molecular patterns from bacteria, viruses, and fungi and elicit a wide array of antimicrobial responses. Among TLRs, TLR6 is expressed on the cell surface of monocytes, monocyte-derived immature dendritic cells (iDCs), and neutrophils, but not on B, T or natural killer (NK) cells. Human TLR6 is a 796-aa type l transmembrane protein that is 74% identical with mouse. It contains an N-terminal signal peptide, 19 tandemly repeated extracellular leucine-rich motifs, and a cytoplasmic domain called Toll/IL-1R homology domain, as seen in other TLRs. TLR6 function has been studied mainly in mouse cells. Constitutive expression of TLR6 activates both the nuclear factor kappa-B (NFK-B) and Jun N-terminal kinase (JNK) pathways. Studies in human cells revealed that TLR6 and TLR2 colocalize at the plasma membrane of monocytes. Human TLR6 recognizes diacylated lipoprotein and peptidoglycan at the cell surface cooperatively with human TLR2. Thus, coexpression of TLR2 and TLR6 at the cell surface is crucial for recognition of diacylated lipopeptide and peptideoglycan and subsequent cellular activation in human cells. Protein function: Participates in the innate immune response to Gram- positive bacteria and fungi. Specifically recognizes diacylated and, to a lesser extent, triacylated lipopeptides (PubMed:20037584). In response to diacylated lipopeptides, forms the activation cluster TLR2:TLR6:CD14:CD36, this cluster triggers signaling from the cell surface and subsequently is targeted to the Golgi in a lipid-raft dependent pathway (PubMed:16880211). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR2 (PubMed:11441107). In complex with TLR4, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid- beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B- dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion (PubMed:11441107, PubMed:20037584). [The UniProt Consortium]