anti human mouse phospho irf 3 ser396 d6o1m antibody cell signaling technology rrid ab 2773013 anti human cgas  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti human mouse phospho irf 3 ser396 d6o1m antibody cell signaling technology rrid ab 2773013 anti human cgas
    Anti Human Mouse Phospho Irf 3 Ser396 D6o1m Antibody Cell Signaling Technology Rrid Ab 2773013 Anti Human Cgas, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho irf 3 ser396 d6o1m  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho irf 3 ser396 d6o1m
    Phospho Irf 3 Ser396 D6o1m, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho irf 3 ser396 d6o1m rabbit mab  (Cell Signaling Technology Inc)


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    phospho irf 3 ser396 d6o1m abbit mab  (Cell Signaling Technology Inc)


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    phospho irf 3 ser396 d6o1m rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho irf 3 ser396 d6o1m rabbit mab

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    1) Product Images from "STING-IRG1 inhibits liver metastasis of colorectal cancer by regulating the polarization of tumor-associated macrophages"

    Article Title: STING-IRG1 inhibits liver metastasis of colorectal cancer by regulating the polarization of tumor-associated macrophages

    Journal: iScience

    doi: 10.1016/j.isci.2023.107376


    Figure Legend Snippet:

    Techniques Used: Concentration Assay, Recombinant, Software

    phospho irf 3 ser396 d6o1m rabbit mab  (Cell Signaling Technology Inc)


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    d6o1m  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc d6o1m
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    phospho irf 3 ser396 d6o1m rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho irf 3 ser396 d6o1m rabbit mab
    The cytosolic DNA sensor cGAS is activated after cerebral ischemia/reperfusion. ( A ) The mRNA level of cGAS in primary microglia isolated from brain tissue 3 h post-tMCAO (9 mice per group). ( B ) The protein level of cGAS in primary microglia isolated from brain tissue at 1, 2, 3 and 6 h post-tMCAO, respectively. The gray values were analyzed by using ImageJ and were normalized to Iba1. ( C ) BV2 cells were transfected with siRNA against cGAS and harvested 48 h post-transfection to quantify the mRNA level of cGAS. ( D ) cGAS-silenced and control BV2 cells were transfected with poly(dA:dT) and harvested 3 h post-poly(dA:dT) treatment to analyze the protein levels of pIRF3, cGAS, and GAPDH. ( E ) cGAS-silenced, STING-silenced, and control BV2 cells were transfected with poly(dA:dT) and harvested 6 h post-poly(dA:dT) treatment to analyze the mRNA level of IFN-β. ( F ) BV2 cells were transfected with siRNA against STING and harvested 48 h post-transfection to quantify the mRNA level of STING. ( G ) cGAS-silenced, STING-silenced, and control BV2 cells were transfected with mtDNA and harvested 6 h post-transfection to analyze the mRNA level of IFN-β. ( H ) The cGAS-mtDNA complex was isolated from brain tissue extracted from mice subjected to tMCAO using an anti-cGAS antibody and quantified by real-time PCR. ( I ) The cGAS-mtDNA complex was isolated from OGD/R-treated primary microglia using an anti-cGAS antibody and quantified by real-time PCR with primer pairs against mtDNA. ( J and K ) The mRNA levels of IFN-β (J) and IL-6 (K) in control and cGAS-silenced BV2 cells after OGD/R treatment. (* indicates p < 0.05, ** indicates p < 0.01 by ANOVA or Student's t -test). Abbreviations: cGAS, cyclic GMP-AMP synthase; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; IFN-β, interferon-beta; IL-6, interleukin-6; mtDNA, mitochondrial DNA; OGD/R, oxygen-glucose deprivation/reperfusion; pIRF3, phosphorylated interferon regulatory factor 3; siRNA, small interfering RNA; STING, stimulator of interferon genes; tMCAO, transient middle cerebral artery occlusion.
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    1) Product Images from "HDAC3 inhibition ameliorates ischemia/reperfusion-induced brain injury by regulating the microglial cGAS-STING pathway"

    Article Title: HDAC3 inhibition ameliorates ischemia/reperfusion-induced brain injury by regulating the microglial cGAS-STING pathway

    Journal: Theranostics

    doi: 10.7150/thno.47651

    The cytosolic DNA sensor cGAS is activated after cerebral ischemia/reperfusion. ( A ) The mRNA level of cGAS in primary microglia isolated from brain tissue 3 h post-tMCAO (9 mice per group). ( B ) The protein level of cGAS in primary microglia isolated from brain tissue at 1, 2, 3 and 6 h post-tMCAO, respectively. The gray values were analyzed by using ImageJ and were normalized to Iba1. ( C ) BV2 cells were transfected with siRNA against cGAS and harvested 48 h post-transfection to quantify the mRNA level of cGAS. ( D ) cGAS-silenced and control BV2 cells were transfected with poly(dA:dT) and harvested 3 h post-poly(dA:dT) treatment to analyze the protein levels of pIRF3, cGAS, and GAPDH. ( E ) cGAS-silenced, STING-silenced, and control BV2 cells were transfected with poly(dA:dT) and harvested 6 h post-poly(dA:dT) treatment to analyze the mRNA level of IFN-β. ( F ) BV2 cells were transfected with siRNA against STING and harvested 48 h post-transfection to quantify the mRNA level of STING. ( G ) cGAS-silenced, STING-silenced, and control BV2 cells were transfected with mtDNA and harvested 6 h post-transfection to analyze the mRNA level of IFN-β. ( H ) The cGAS-mtDNA complex was isolated from brain tissue extracted from mice subjected to tMCAO using an anti-cGAS antibody and quantified by real-time PCR. ( I ) The cGAS-mtDNA complex was isolated from OGD/R-treated primary microglia using an anti-cGAS antibody and quantified by real-time PCR with primer pairs against mtDNA. ( J and K ) The mRNA levels of IFN-β (J) and IL-6 (K) in control and cGAS-silenced BV2 cells after OGD/R treatment. (* indicates p < 0.05, ** indicates p < 0.01 by ANOVA or Student's t -test). Abbreviations: cGAS, cyclic GMP-AMP synthase; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; IFN-β, interferon-beta; IL-6, interleukin-6; mtDNA, mitochondrial DNA; OGD/R, oxygen-glucose deprivation/reperfusion; pIRF3, phosphorylated interferon regulatory factor 3; siRNA, small interfering RNA; STING, stimulator of interferon genes; tMCAO, transient middle cerebral artery occlusion.
    Figure Legend Snippet: The cytosolic DNA sensor cGAS is activated after cerebral ischemia/reperfusion. ( A ) The mRNA level of cGAS in primary microglia isolated from brain tissue 3 h post-tMCAO (9 mice per group). ( B ) The protein level of cGAS in primary microglia isolated from brain tissue at 1, 2, 3 and 6 h post-tMCAO, respectively. The gray values were analyzed by using ImageJ and were normalized to Iba1. ( C ) BV2 cells were transfected with siRNA against cGAS and harvested 48 h post-transfection to quantify the mRNA level of cGAS. ( D ) cGAS-silenced and control BV2 cells were transfected with poly(dA:dT) and harvested 3 h post-poly(dA:dT) treatment to analyze the protein levels of pIRF3, cGAS, and GAPDH. ( E ) cGAS-silenced, STING-silenced, and control BV2 cells were transfected with poly(dA:dT) and harvested 6 h post-poly(dA:dT) treatment to analyze the mRNA level of IFN-β. ( F ) BV2 cells were transfected with siRNA against STING and harvested 48 h post-transfection to quantify the mRNA level of STING. ( G ) cGAS-silenced, STING-silenced, and control BV2 cells were transfected with mtDNA and harvested 6 h post-transfection to analyze the mRNA level of IFN-β. ( H ) The cGAS-mtDNA complex was isolated from brain tissue extracted from mice subjected to tMCAO using an anti-cGAS antibody and quantified by real-time PCR. ( I ) The cGAS-mtDNA complex was isolated from OGD/R-treated primary microglia using an anti-cGAS antibody and quantified by real-time PCR with primer pairs against mtDNA. ( J and K ) The mRNA levels of IFN-β (J) and IL-6 (K) in control and cGAS-silenced BV2 cells after OGD/R treatment. (* indicates p < 0.05, ** indicates p < 0.01 by ANOVA or Student's t -test). Abbreviations: cGAS, cyclic GMP-AMP synthase; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; IFN-β, interferon-beta; IL-6, interleukin-6; mtDNA, mitochondrial DNA; OGD/R, oxygen-glucose deprivation/reperfusion; pIRF3, phosphorylated interferon regulatory factor 3; siRNA, small interfering RNA; STING, stimulator of interferon genes; tMCAO, transient middle cerebral artery occlusion.

    Techniques Used: Isolation, Transfection, Real-time Polymerase Chain Reaction, Small Interfering RNA

    HDAC3 promotes cGAS transcription by deacetylating p65. ( A ) BV2 cells transfected with siRNA against p65 or scrambled siRNA were treated with poly(dA:dT)-Lipofectamine 2000 complex for 3 h and the expression of pIRF3, cGAS, p65, and GAPDH was analyzed. ( B ) The mRNA level of cGAS in p65-silenced and control cells was quantified by real-time PCR. ( C ) BV2 cells transfected with siRNA against p65 or scramble were treated with poly(dA:dT)-Lipofectamine 2000 complex for 6 h and the transcription levels of IFN-β and β-actin were analyzed by real-time PCR. ( D ) p65-silenced and control cells that underwent OGD/R were collected and the expression of IL-6 was analyzed by real-time PCR. ( E ) pFlag-HDAC3 and pMyc-p65 plasmids were co-transfected into HEK293T cells, and the cells were harvested for Co-IP with anti-Flag tag magnetic beads. ( F ) Co-IP was performed with a rabbit anti-p65 antibody or control rabbit IgG with BV2 cells. ( G ) The binding sites of p65 in the promoter region were analyzed by chromatin immunoprecipitation and real-time PCR with an antibody against p65. ( H and I ) The binding activity of p65 in the promoter region of cGAS in HDAC3-inhibited (H) and HDAC3-silenced (I) BV2 cells. ( J ) Cells were co-transfected with pMyc-p65, cGAS reporter plasmid and TK-Renilla plasmids, treated with RGFP966 or vehicle, and harvested 24 h post-transfection for the dual-luciferase assay. ( K ) Plasmids encoding WT p65, mutant p65 K122Q , mutant p65 K122/123Q , mutant p65 K122R , or mutant p65 K122/123R were transfected into HEK293T cells with the cGAS reporter and TK-Renilla reference plasmids, and the cells were harvested for the dual-luciferase assay 24 h post-transfection. ( L ) Plasmids encoding Myc-p65 and HA-p300 and empty vectors were co-transfected into HEK293T cells with plasmids encoding Flag-HDAC1, Flag-HDAC2, and Flag-HDAC3 and empty vectors, and the acetylation level of p65 was analyzed with anti-acetylated lysine (pan-Ac) after p65 was purified with anti-Myc tag magnetic beads. ( M ) The cytoplasm and nucleus of HDAC1-silenced, HDAC2-silenced, HDAC3-silenced, and control BV2 cells were separated and the expression of p65 was analyzed by western blot. ( N and O ) BV2 cell lines stably expressing Flag-tagged WT p65 or mutant p65 K122R or control cell lines were pretreated with RGFP966 for 12 h, transfected with poly(dA:dT), and harvested to analyze the protein levels of pIRF3, cGAS, p65, and GAPDH (N) and the mRNA level of IFN-β (O). ( P ) Schematic showing how HDAC3 regulates the transcription of cGAS by deacetylating p65. (* indicates p < 0.05, ** indicates p < 0.01 by ANOVA or Student's t -test). Abbreviations: cGAS, cyclic GMP-AMP synthase; Co-IP, co-immunoprecipitation; GADPH, glyceraldehyde 3-phsophate dehydrogenase; HDAC3, histone deacetylase 3; IFN-β, interferon-beta; OGD/R, oxygen-glucose deprivation/reperfusion; pIRF3, phosphorylated interferon regulatory factor 3; siRNA, small interfering RNA; WT, wild-type.
    Figure Legend Snippet: HDAC3 promotes cGAS transcription by deacetylating p65. ( A ) BV2 cells transfected with siRNA against p65 or scrambled siRNA were treated with poly(dA:dT)-Lipofectamine 2000 complex for 3 h and the expression of pIRF3, cGAS, p65, and GAPDH was analyzed. ( B ) The mRNA level of cGAS in p65-silenced and control cells was quantified by real-time PCR. ( C ) BV2 cells transfected with siRNA against p65 or scramble were treated with poly(dA:dT)-Lipofectamine 2000 complex for 6 h and the transcription levels of IFN-β and β-actin were analyzed by real-time PCR. ( D ) p65-silenced and control cells that underwent OGD/R were collected and the expression of IL-6 was analyzed by real-time PCR. ( E ) pFlag-HDAC3 and pMyc-p65 plasmids were co-transfected into HEK293T cells, and the cells were harvested for Co-IP with anti-Flag tag magnetic beads. ( F ) Co-IP was performed with a rabbit anti-p65 antibody or control rabbit IgG with BV2 cells. ( G ) The binding sites of p65 in the promoter region were analyzed by chromatin immunoprecipitation and real-time PCR with an antibody against p65. ( H and I ) The binding activity of p65 in the promoter region of cGAS in HDAC3-inhibited (H) and HDAC3-silenced (I) BV2 cells. ( J ) Cells were co-transfected with pMyc-p65, cGAS reporter plasmid and TK-Renilla plasmids, treated with RGFP966 or vehicle, and harvested 24 h post-transfection for the dual-luciferase assay. ( K ) Plasmids encoding WT p65, mutant p65 K122Q , mutant p65 K122/123Q , mutant p65 K122R , or mutant p65 K122/123R were transfected into HEK293T cells with the cGAS reporter and TK-Renilla reference plasmids, and the cells were harvested for the dual-luciferase assay 24 h post-transfection. ( L ) Plasmids encoding Myc-p65 and HA-p300 and empty vectors were co-transfected into HEK293T cells with plasmids encoding Flag-HDAC1, Flag-HDAC2, and Flag-HDAC3 and empty vectors, and the acetylation level of p65 was analyzed with anti-acetylated lysine (pan-Ac) after p65 was purified with anti-Myc tag magnetic beads. ( M ) The cytoplasm and nucleus of HDAC1-silenced, HDAC2-silenced, HDAC3-silenced, and control BV2 cells were separated and the expression of p65 was analyzed by western blot. ( N and O ) BV2 cell lines stably expressing Flag-tagged WT p65 or mutant p65 K122R or control cell lines were pretreated with RGFP966 for 12 h, transfected with poly(dA:dT), and harvested to analyze the protein levels of pIRF3, cGAS, p65, and GAPDH (N) and the mRNA level of IFN-β (O). ( P ) Schematic showing how HDAC3 regulates the transcription of cGAS by deacetylating p65. (* indicates p < 0.05, ** indicates p < 0.01 by ANOVA or Student's t -test). Abbreviations: cGAS, cyclic GMP-AMP synthase; Co-IP, co-immunoprecipitation; GADPH, glyceraldehyde 3-phsophate dehydrogenase; HDAC3, histone deacetylase 3; IFN-β, interferon-beta; OGD/R, oxygen-glucose deprivation/reperfusion; pIRF3, phosphorylated interferon regulatory factor 3; siRNA, small interfering RNA; WT, wild-type.

    Techniques Used: Transfection, Expressing, Real-time Polymerase Chain Reaction, Co-Immunoprecipitation Assay, FLAG-tag, Magnetic Beads, Binding Assay, Chromatin Immunoprecipitation, Activity Assay, Plasmid Preparation, Luciferase, Mutagenesis, Purification, Western Blot, Stable Transfection, Immunoprecipitation, Histone Deacetylase Assay, Small Interfering RNA

    Proposed mechanism: HDAC3 regulates the transcription of cGAS by deacetylating p65 at K122, which plays a role in ischemic/reperfusion-induced neuroinflammation and brain injury. Briefly, mtDNA released from dead cells in the ischemic core is engulfed by microglia in the penumbra. Toxic mtDNA then activates the microglial cGAS-STING-IRF3 pathway and potentiates neuroinflammation, which in turn aggravates ischemia-induced neuronal cell death. Within microglia, HDAC deacetylates p65, which promotes its nuclear translocation and induces cGAS expression and cGAS-STING pathway activation. Abbreviations: cGAS, cyclic GMP-AMP synthase; HDAC, histone deacetylase; IRF3, interferon regulatory factor 3; mtDNA, mitochondrial DNA; STING, simulator of interferon genes.
    Figure Legend Snippet: Proposed mechanism: HDAC3 regulates the transcription of cGAS by deacetylating p65 at K122, which plays a role in ischemic/reperfusion-induced neuroinflammation and brain injury. Briefly, mtDNA released from dead cells in the ischemic core is engulfed by microglia in the penumbra. Toxic mtDNA then activates the microglial cGAS-STING-IRF3 pathway and potentiates neuroinflammation, which in turn aggravates ischemia-induced neuronal cell death. Within microglia, HDAC deacetylates p65, which promotes its nuclear translocation and induces cGAS expression and cGAS-STING pathway activation. Abbreviations: cGAS, cyclic GMP-AMP synthase; HDAC, histone deacetylase; IRF3, interferon regulatory factor 3; mtDNA, mitochondrial DNA; STING, simulator of interferon genes.

    Techniques Used: Translocation Assay, Expressing, Activation Assay, Histone Deacetylase Assay

    phospho irf 3 ser396 d6o1m rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho irf 3 ser396 d6o1m rabbit mab
    (A,D,G) Representative images of astrocytes (GFAP-positive cells, green) and stimulator of interferon genes (STING) (red), p-TANK-binding kinase 1 (p-TBK1; red), p-interferon regulatory factor 3 (p-IRF3; red) immunofluorescence double-labeling in white matter at 4 weeks after bilateral common carotid artery occlusion (2VO). (C,F) shows immunofluorescence of STING (red) and p-IRF3(red) expression were colocalized with neurons (NEUN-positive cells, green) in the hippocampus. (B,E) Representative immunofluorescent images of microglia (Iba-1-positive cells, green) and STING (red), p-IRF3(red) immunofluorescence double-labeling in white matter. (×400, Blue, DAPI, Scale bar, 20 μm, n = 3 per group) (H) Quantitative analysis of the number of GFAP + cells. (I–K) Quantitation of the number of STING + /GFAP + cells, p-TBK1 + /GFAP + cells, and p-IRF3 + /GFAP + cells in different groups. (L,M) Quantitation of the number of STING + /Iba-1 + cells, p-IRF3 + /Iba-1 + cells. * p < 0.05 vs. Sham; $ p < 0.05, 2VO + RES 4w group vs. 2VO 4w group. Data are presented as mean ± SD.
    Phospho Irf 3 Ser396 D6o1m Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Resveratrol reduces inflammatory response and detrimental effects in chronic cerebral hypoperfusion by down-regulating stimulator of interferon genes/TANK-binding kinase 1/interferon regulatory factor 3 signaling"

    Article Title: Resveratrol reduces inflammatory response and detrimental effects in chronic cerebral hypoperfusion by down-regulating stimulator of interferon genes/TANK-binding kinase 1/interferon regulatory factor 3 signaling

    Journal: Frontiers in Aging Neuroscience

    doi: 10.3389/fnagi.2022.868484

    (A,D,G) Representative images of astrocytes (GFAP-positive cells, green) and stimulator of interferon genes (STING) (red), p-TANK-binding kinase 1 (p-TBK1; red), p-interferon regulatory factor 3 (p-IRF3; red) immunofluorescence double-labeling in white matter at 4 weeks after bilateral common carotid artery occlusion (2VO). (C,F) shows immunofluorescence of STING (red) and p-IRF3(red) expression were colocalized with neurons (NEUN-positive cells, green) in the hippocampus. (B,E) Representative immunofluorescent images of microglia (Iba-1-positive cells, green) and STING (red), p-IRF3(red) immunofluorescence double-labeling in white matter. (×400, Blue, DAPI, Scale bar, 20 μm, n = 3 per group) (H) Quantitative analysis of the number of GFAP + cells. (I–K) Quantitation of the number of STING + /GFAP + cells, p-TBK1 + /GFAP + cells, and p-IRF3 + /GFAP + cells in different groups. (L,M) Quantitation of the number of STING + /Iba-1 + cells, p-IRF3 + /Iba-1 + cells. * p < 0.05 vs. Sham; $ p < 0.05, 2VO + RES 4w group vs. 2VO 4w group. Data are presented as mean ± SD.
    Figure Legend Snippet: (A,D,G) Representative images of astrocytes (GFAP-positive cells, green) and stimulator of interferon genes (STING) (red), p-TANK-binding kinase 1 (p-TBK1; red), p-interferon regulatory factor 3 (p-IRF3; red) immunofluorescence double-labeling in white matter at 4 weeks after bilateral common carotid artery occlusion (2VO). (C,F) shows immunofluorescence of STING (red) and p-IRF3(red) expression were colocalized with neurons (NEUN-positive cells, green) in the hippocampus. (B,E) Representative immunofluorescent images of microglia (Iba-1-positive cells, green) and STING (red), p-IRF3(red) immunofluorescence double-labeling in white matter. (×400, Blue, DAPI, Scale bar, 20 μm, n = 3 per group) (H) Quantitative analysis of the number of GFAP + cells. (I–K) Quantitation of the number of STING + /GFAP + cells, p-TBK1 + /GFAP + cells, and p-IRF3 + /GFAP + cells in different groups. (L,M) Quantitation of the number of STING + /Iba-1 + cells, p-IRF3 + /Iba-1 + cells. * p < 0.05 vs. Sham; $ p < 0.05, 2VO + RES 4w group vs. 2VO 4w group. Data are presented as mean ± SD.

    Techniques Used: Binding Assay, Immunofluorescence, Labeling, Expressing, Quantitation Assay

    Increased expression of stimulators of type 1 interferon gene (STING), p-TANK-binding kinase 1 (p-TBK1), and p-interferon regulatory factor 3 (p-IRF3) in bilateral common carotid artery occlusion (2VO) Rats. The expression of STING, p-TBK1, and p-IRF3 was decreased in 2VO rats treated with resveratrol (RES). 2VO promotes the nuclear translocation of IRF3. RES treatment counteracted the nuclear translocation of IRF3. (A) Western blot and quantitative analysis of STING, TBK1, IRF3, p-TBK1, and p-IRF3 at weeks 4 and 8 in hippocampus and white matter extract after 2VO. β-actin was used as an internal control ( n = 3 per group). (B) Western blot analysis of nucleus and cytosolic IRF3 in white matter and hippocampus in different groups after 2VO. β-actin was used as an internal control ( n = 3 per group). (C) mRNA levels of STING, TBK1, and IRF3 in white matter were detected by qRT-PCR. GAPDH was used as an internal control ( n = 4 per group). * p < 0.05 vs. Sham; & p < 0.05, 2VO 8w group vs. 2VO 4w group; # p < 0.05, 2VO + RES 8w group vs. 2VO + RES 4w group; $ p < 0.05, 2VO + RES 4w group vs. 2VO 4w group; ^ p < 0.05, 2VO + RES 8w group vs. 2VO 8w group. Data are presented as mean ± SD.
    Figure Legend Snippet: Increased expression of stimulators of type 1 interferon gene (STING), p-TANK-binding kinase 1 (p-TBK1), and p-interferon regulatory factor 3 (p-IRF3) in bilateral common carotid artery occlusion (2VO) Rats. The expression of STING, p-TBK1, and p-IRF3 was decreased in 2VO rats treated with resveratrol (RES). 2VO promotes the nuclear translocation of IRF3. RES treatment counteracted the nuclear translocation of IRF3. (A) Western blot and quantitative analysis of STING, TBK1, IRF3, p-TBK1, and p-IRF3 at weeks 4 and 8 in hippocampus and white matter extract after 2VO. β-actin was used as an internal control ( n = 3 per group). (B) Western blot analysis of nucleus and cytosolic IRF3 in white matter and hippocampus in different groups after 2VO. β-actin was used as an internal control ( n = 3 per group). (C) mRNA levels of STING, TBK1, and IRF3 in white matter were detected by qRT-PCR. GAPDH was used as an internal control ( n = 4 per group). * p < 0.05 vs. Sham; & p < 0.05, 2VO 8w group vs. 2VO 4w group; # p < 0.05, 2VO + RES 8w group vs. 2VO + RES 4w group; $ p < 0.05, 2VO + RES 4w group vs. 2VO 4w group; ^ p < 0.05, 2VO + RES 8w group vs. 2VO 8w group. Data are presented as mean ± SD.

    Techniques Used: Expressing, Binding Assay, Translocation Assay, Western Blot, Quantitative RT-PCR

    phospho irf 3 ser396 d6o1m rabbit mab  (Cell Signaling Technology Inc)


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