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Anti-TLR7, clone A94B10, Cat. No. MABF2273, is a mouse monoclonal antibody that detects Toll-like receptor 7 (TLR7) and is tested for use in Flow Cytometry, Immunocytochemistry, and Immunoprecipitation.
More>>Anti-TLR7, clone A94B10, Cat. No. MABF2273, is a mouse monoclonal antibody that detects Toll-like receptor 7 (TLR7) and is tested for use in Flow Cytometry, Immunocytochemistry, and Immunoprecipitation. Less<<
Toll-like receptor 7 (UniProt: P58681; also known as TLR7) is encoded by the Tlr7 gene (Gene ID: 170743) in murine species. Toll-like Receptors (TLRs) are transmembrane proteins that are expressed on various immune cells. They contain an N-terminal extracellular and a C-terminal cytoplasmic domain. The N-terminal region contains leucine-rich repeats (LRR) that recognize specific pathogen components. Although the ligand recognition mechanisms of the TLRs vary significantly, all TLR dimers exhibit similar overall arrangement. At least 13 different members of TLR family have been identified that detect different pathogen associated molecular patterns (PAMPs). TLR7 is a single-pass type I membrane glycoprotein that is activated by single-stranded RNA. It is processed in the endoplasmic reticulum (ER) membrane and is then directed to the endosome by a complex shuttling process mediated by several chaperone proteins. It localizes to endosome and lysosome upon stimulation with agonist. TLR7 is initially produced as an inactive protein in the ER and is correctly folded prior to exiting the ER with the help of two ER-resident chaperone proteins, gp96 and protein-associated with TLR4 (PRAT4A). In the absence of gp96, macrophages and B cells fail to respond to TLR7 ligation. PRAT4A-deficient macrophages also display impaired TLR7 responsiveness. To avoid autoimmune responses, TLR7 is silenced until the N-terminal half of the TLR7 ectodomain (TLR7N) is cleaved off. TLR7 is synthesized with a signal peptide (aa 1-26), which is subsequently cleaved off to generate the mature form that contains an extracellular domain (aa 27-8370, a transmembrane domain (aa 838-858), and a cytoplasmic domain (aa 859-1050). (Ref.: Petes, C., et al. (2018). Front. Immunol. 9; 256; Kanno, A., et al. (2013). Int. Immunol. 25(7); 413-422).
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Anti-TLR7, clone A94B10, Cat. No. MABF2273, is a mouse monoclonal antibody that detects Toll-like receptor 7 (TLR7) and is tested for use in Flow Cytometry, Immunocytochemistry, and Immunoprecipitation.
Key Applications
Flow Cytometry
Immunocytochemistry
Immunoprecipitation
Application Notes
Flow Cytometry Analysis: A representative lot detected TLR7 in Flow Cytometry applications (Fukui, R., et. al. (2016). J Immunol. 196(1):416-27; Kanno, A., et. al. (2013). Int Immunol. 25(7):413-22).
Immunocytochemistry Analysis: A representative lot detected TLR7 in Immunocytochemistry applications (Kanno, A., et. al. (2013). Int Immunol. 25(7):413-22).
Immunoprecipitation Analysis: A representative lot immunoprecipitated TLR7 in Immunoprecipitation applications (Kanno, A., et. al. (2013). Int Immunol. 25(7):413-22).
Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user
Biological Information
Immunogen
Ba/F3 cells expressing mouse TLR7.
Epitope
Unknown
Clone
A94B10
Concentration
1.0 mg/mL. Please refer to guidance on suggested starting dilutions and/or titers per application and sample type.
Host
Mouse
Specificity
Clone A94B10 is a mouse monoclonal antibody that detects Toll-like receptor 7 (TLR7).
Evaluated by Immunocytochemistry in RAW264.7 cells.
Immunocytochemistry Analysis: A 1:500 dilution of this antibody detected TLR7 in RAW264.7 cells.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Type I IFN Contributes to the Phenotype of Unc93b1D34A/D34A Mice by Regulating TLR7 Expression in B Cells and Dendritic Cells. Fukui R, Kanno A, Miyake K. J Immunol
196(1)
416-27
2015
TLR7 recognizes pathogen-derived and self-derived RNA, and thus a regulatory system for control of the TLR7 response is required to avoid excessive activation. Unc93 homolog B1 (Unc93B1) is a regulator of TLR7 that controls the TLR7 response by transporting TLR7 from the endoplasmic reticulum to endolysosomes. We have previously shown that a D34A mutation in Unc93B1 induces hyperactivation of TLR7, and that Unc93b1(D34A/D34A) mice (D34A mice) have systemic inflammation spontaneously. In this study, we examined the roles of inflammatory cytokines such as IFN-γ, IL-17A, and type I IFNs to understand the mechanism underlying the phenotype in D34A mice. mRNAs for IFN-γ and IL-I7A in CD4(+) T cells increased, but inflammatory phenotype manifesting as thrombocytopenia and splenomegaly was still observed in Ifng(-/-) or Il17a(-/-) D34A mice. In contrast to T cell-derived cytokines, Ifnar1(-/-) D34A mice showed an ameliorated phenotype with lower expression of TLR7 in B cells and conventional dendritic cells (cDCs). The amount of TLR7 decreased in B cells from Ifnar1(-/-) D34A mice, but the percentage of TLR7(+) cells decreased among CD8α(-) cDCs. In conclusion, type I IFNs maintain expression of TLR7 in B cells and cDCs in different ways; total amount of TLR7 is kept in B cells and TLR7(+) population is retained among cDCs. Our results suggested that these TLR7-expressing cells are activated initially and influence TLR7-dependent systemic inflammation.
Essential role for Toll-like receptor 7 (TLR7)-unique cysteines in an intramolecular disulfide bond, proteolytic cleavage and RNA sensing. Kanno A, Yamamoto C, Onji M, Fukui R, Saitoh S, Motoi Y, Shibata T, Matsumoto F, Muta T, Miyake K. Int Immunol
25(7)
413-22
2013
Toll-like receptor 7 (TLR7) an innate immune sensor for microbial RNA, erroneously responds to self-derived RNA. To avoid autoimmune responses, TLR7 is suggested to be silenced until the N-terminal half of the TLR7 ectodomain (TLR7N) is cleaved off. Resultant truncated TLR7 (TLR7C) is thought to signal microbial RNA. We here show that TLR7N remains associated with TLR7C through a disulfide bond. By N-terminal amino acid sequencing, TLR7C was found to start at 461E or 462A. The newly established monoclonal anti-TLR7N showed that endogenous TLR7 in bone marrow-derived dendritic cells was almost all cleaved and cleaved TLR7N remained in endolysosomes. TLR7N in endolysosomes was linked with TLR7C by a disulfide bond. In contrast, TLR9 did not have a disulfide bond between TLR9N and TLR9C fragments. Among the cysteines unique to the ectodomain of TLR7 but not TLR9 (Cys98, Cys445, Cys475 and Cys722), Cys98 in TLR7N and Cys475 in TLR7C were required for an intramolecular disulfide bond. These cysteines were also needed for proteolytic cleavage of and RNA sensing by TLR7, but not for TLR7 trafficking from endoplasmic reticulum to endosomes. No response was seen in TLR7 mutants lacking the proteolytic cleavage site or TLR7C alone. These results demonstrate requirement for proteolytic cleavage and TLR7N in TLR7 responses and indicate RNA sensing by TLR7N + TLR7C.
