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Mouse TLR6 Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q9EPW9 |
| Other Accession | NP_035734 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 91116 Da |
| Antigen Region | 1-30 aa |
| Gene ID | 21899 |
|---|---|
| Other Names | Toll-like receptor 6, CD286, Tlr6 |
| Target/Specificity | This Mouse TLR6 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of mouse TLR6. |
| Dilution | WB~~1:1000 IHC-P~~1:50~100 |
| 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 | Mouse TLR6 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | Tlr6 |
|---|---|
| Function | Participates in the innate immune response to Gram-positive bacteria and fungi. Specifically recognizes diacylated and, to a lesser extent, triacylated lipopeptides (PubMed:19931471). 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. 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. 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:20037584, PubMed:23812099). |
| Cellular Location | Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, phagosome membrane; Single-pass type I membrane protein. Membrane raft {ECO:0000250|UniProtKB:Q9Y2C9}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y2C9}. 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. {ECO:0000250|UniProtKB:Q9Y2C9} |
| Tissue Location | Detected in thymus, spleen, ovary and lung. Expressed in macrohpages. |
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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
Ozinsky, A., et al., Proc. Natl. Acad. Sci. U.S.A. 97(25):13766-13771 (2000).
Takeuchi, O., et al., Gene 231 (1-2), 59-65 (1999).
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