A recombinant protein corresponding to human TLR-2 extracellular domain was used as an immunogen.
Buffer
Store at -20C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.
Toll-like receptor 2 (TLR2) is a signalling receptor that is activated by LPS in a response that depends on LPS-binding protein and is enhanced by CD14. A region in the intracellular domain of TLR2 with homology to a portion of the interleukin (IL)-1 receptor that is implicated in the activation of the IL-1-receptor-associated kinase is required for this response. Results indicate that TLR2 is a direct mediator of signalling by LPS (1). All bacterial pathogens produce lipoproteins (BLPs), which trigger the innate immune response. BLPs were found to induce apoptosis in THP-1 monocytic cells through human TLR2. BLPs also initiated apoptosis in an epithelial cell line transfected with TLR2. BLPs stimulated nuclear factor-kappaB, a transcriptional activator of multiple host defense genes, and activated the respiratory burst through TLR2. Thus, TLR2 is a molecular link between microbial products, apoptosis, and host defense mechanisms (2). It has been found that in TLR2 extracellular domain (C-term) all four predicted glycosylation sites are substituted, although one site is inefficiently core-glycosylated and its removal drastically affects secretion. The remaining TLR2 glycosylation sites also contribute to efficient protein secretion, albeit to a lesser degree (3).
Related Pathway
Toll-like receptor signaling pathway
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