Anti-Human TLR1 Antibody Pair

Product Description: Toll like receptor 1 (TLR1) is a type I transmembrane glycoprotein characterized by an extracellular domain containing leucine-rich repeat (LRR) motifs, which are essential for recognizing pathogen-associated molecular patterns (PAMPs), and an intracellular toll/interleukin-1 receptor (TIR) domain that initiates downstream signaling cascades. TLR1 typically forms heterodimers with TLR2, enabling the recognition of triacylated lipopeptides from bacteria, and this interaction is crucial for the activation of innate immune responses, including the production of proinflammatory cytokines and the bridging of innate and adaptive immunity. Structurally, the LRR domains in TLR1's extracellular region are divided into N-terminal, central, and C-terminal subdomains, with the central region displaying notable variability and unique structural features such as extra alpha helices, which influence ligand binding. Dysfunction or genetic variation in TLR1 has been associated with altered susceptibility to infectious and inflammatory diseases, as impaired TLR1 signaling can compromise immune responses to specific bacterial components. Protein Function: Participates in the innate immune response to microbial agents. Specifically recognizes diacylated and triacylated lipopeptides. Cooperates with TLR2 to mediate the innate immune response to bacterial lipoproteins or lipopeptides (PubMed:21078852). Forms the activation cluster TLR2:TLR1:CD14 in response to triacylated lipopeptides, 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 [The Uniprot Consortium]