Anti-TLR2 (CD282) Monoclonal Antibody

Human toll-like receptor (TLR) family includes ten members that activate the innate immune response via an ability to recognize molecular structures found in a variety of microbial pathogens. All TLR family members are type I transmembrane proteins with a large number of extracellular leucine-rich repeats (LRRs) and a cytoplasmic Toll/IL-1 receptor (TIR) domain. Human TLR2 is synthesized as a 784 amino acid (aa) precursor that contains a signal sequence (aa 1-18), an extracellular domain (aa 19-588) with approximately 20 LRRs, a transmembrane segment (aa 589-609), and a cytoplasmic TIR domain (aa 610-784). The receptor is expressed on a number of cell types including monocytes, dendritic cells, neutrophils, B cells endothelial cells, and hepatocytes. TLR2 functions as part of a heterodimeric complex with either TLR1 or TLR6, and possibly other co-receptors. These complexes recognize lipoproteins and glycolipids from gram-positive and gram-negative bacteria as well as mycoplasma and yeast. TLR2/TLR1 heterodimers bind triacylated lipopeptides, while the TLR2/TLR6 heterodimer preferentially recognizes diacylated lipopeptides. Upon ligand recognition, TLR2 delivers an activating signal via the associated adapter molecules, MyD88 and TIRAP. TLR2 signaling results in dendritic cell maturation characterized by increased surface expression of class II MHC and the T cell costimulators, CD80 and CD86. Activation via TLR2 also results in production of a number of pro-inflammatory cytokines including TNF-alpha, IL-2, IL-6, IL-12, and MIP-2. 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 (PubMed:17889651, PubMed:21078852). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also activate immune cells and promote apoptosis in response to the lipid moiety of lipoproteins (PubMed:10426995, PubMed:10426996). 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 TLR6 (PubMed:11441107). Stimulation of monocytes in vitro with M.tuberculosis PstS1 induces p38 MAPK and ERK1/2 activation primarily via this receptor, but also partially via TLR4 (PubMed:16622205). MAPK activation in response to bacterial peptidoglycan also occurs via this receptor (PubMed:16622205). Acts as a receptor for M.tuberculosis lipoproteins LprA, LprG, LpqH and PstS1, some lipoproteins are dependent on other coreceptors (TLR1, CD14 and/or CD36), the lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). M.tuberculosis HSP70 (dnaK) but not HSP65 (groEL-2) acts via this protein to stimulate NF-kappa-B expression (PubMed:15809303). Recognizes M.tuberculosis major T-antigen EsxA (ESAT-6) which inhibits downstream MYD88-dependent signaling (shown in mouse). 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 (PubMed:16880211). Required for normal uptake of M.tuberculosis, a process that is inhibited by M.tuberculosis LppM. [The UniProt Consortium]