TLR6 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 1
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, WB, FC, E |
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Primary Accession | Q9Y2C9 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 91880 Da |
Antigen Region | 393-423 aa |
Gene ID | 10333 |
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Other Names | Toll-like receptor 6, CD286, TLR6 |
Target/Specificity | This TLR6 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 393-423 amino acids from the C-terminal region of human TLR6. |
Dilution | WB~~1:1000 IHC-P~~1:50~100 FC~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | TLR6 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | TLR6 |
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Function | Participates in the innate immune response to Gram-positive bacteria and fungi. Specifically recognizes diacylated and, to a lesser extent, triacylated lipopeptides (PubMed:20037584). In response to diacylated lipopeptides, forms the activation cluster TLR2:TLR6:CD14:CD36, 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. 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 TLR2 (PubMed:11441107). In complex with TLR4, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42- binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion (PubMed:11441107, PubMed:20037584). |
Cellular Location | Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9EPW9}; Single-pass type I membrane protein. Membrane raft. Golgi apparatus. Note=Upon complex formation with CD36 and TLR4, internalized through dynamin-dependent endocytosis. Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to diacylated lipoproteins, TLR2:TLR6 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus (PubMed:16880211). |
Tissue Location | Detected in monocytes, CD11c+ immature dendritic cells, plasmacytoid pre-dendritic cells and dermal microvessel endothelial cells |
Provided below are standard protocols that you may find useful for product applications.
Background
TLR6, a Type I membrane protein that belongs to the Toll-like rceptor family, participates in the innate immune response to Gram-positive bacteria and fungi. It acts via MyD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. The protein 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 TLR2. It binds to TLR2 via their respective extracellular domains, and to MyD88 via their respective TIR domains. TLR6 is detected in monocytes, CD11c+ immature dendritic cells, plasmacytoid pre-dendritic cells and dermal microvessel endothelial cells.
References
Bulut, Y., et al., J. Immunol. 167(2):987-994 (2001).
Takeuchi, O., et al., Gene 231 (1-2), 59-65 (1999).
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