Anti-Human/ Mouse TLR2 (Clone: T2.5)

The monoclonal antibody 10-3506 recognizes human Toll-like receptor 2 (TLR2). Toll-like receptors (TLR) are highly conserved throughout evolution and have been implicated in the innate defense to many pathogens. At present, ligands for several of the TLR's, such as TLR2-6,9, have been identified, confirming their role in first line defense against invading microorganism. In mammals, TLRs are identified as type I transmembrane signaling receptors with an extracellular portion containing leucine-rich repeats with pattern recognition capabilities. Pathogen recognition by TLRs provokes rapid activation of innate immunity by inducing proliferation of proinflammatory cytokines and upregulation of costimulatory molecules and eventually toinitiation of adaptive immunity. TLR2 has been identified as a receptor that is central to the innate immune response to lipoproteins of Gram-negative bacteria, several whole Gram-positive bacteria, as well as a receptor for peptidoglycan and lipoteichoic acid and other bacterial cell membrane products. It is suggested that TLR2 is able to recognize such a wide variety of PAMPs (pathogen-specific molecular patterns) by forming heterodimers with other TLRs like e.g. TLR6. TLR2 is essential for recognizing lipopeptides and lipoproteins from several microorganisms and also peptidoglycans derived from gram-positive bacteria. Bacterial species as diverse as mycobacteria, spirochetes, mycoplasma, Staphylococcus aureus, and Streptococcus pneumoniae have all been shown to mediate cellular activation via TLR2. Protein function: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:15690042). May also promote apoptosis in response to lipoproteins. Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides. Recognizes M.tuberculosis major T-antigen EsxA (ESAT- 6) which inhibits downstream MYD88-dependent signaling (PubMed:17486091). Acts as the major receptor for M.tuberculosis lipoproteins LprA, LprG, LpqH and PhoS1 (pstS1), in conjunction with TLR1 and for some but not all lipoproteins CD14 and/or CD36. The lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). Recombinant MPT83 from M.tuberculosis stimulates secretion of cytokines (TNF-alpha, IL-6 and IL-12p40) by mouse macrophage cell lines in a TLR2-dependent fashion, which leads to increased host innate immunity responses against the bacterium (PubMed:22174456). Lung macrophages which express low levels of TLR2 respond poorly to stimulation by M.tuberculosis LpqH (PubMed:19362712). Required for normal uptake of M.tuberculosis, a process that is inhibited by M.tuberculosis LppM (PubMed:27220037). [The UniProt Consortium]