|Calculated MW||89838 Da|
|Other Names||Toll-like receptor 2, Toll/interleukin-1 receptor-like protein 4, CD282, TLR2, TIL4|
|Target/Specificity||A synthetic peptide corresponding to residues surrounding human TLR2 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||TLR-2 Antibody (extracellular) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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. May also promote apoptosis in response to lipoproteins. 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.|
|Cellular Location||Membrane; Single-pass type I membrane protein|
|Tissue Location||Highly expressed in peripheral blood leukocytes, in particular in monocytes, in bone marrow, lymph node and in spleen. Also detected in lung and in fetal liver. Levels are low in other tissues|
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Provided below are standard protocols that you may find useful for product applications.
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).
1. Yang RB, et al. Nature 395(6699):284-8, 1998
2. Aloprantis AO, et al. Science 285(5428):736-9, 1999
3. Weber AN, et al. J Biol Chem 279(33):34589-94, 2004.
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