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Graphical abstract. Graphical abstract illustrating the hypothetical mechanism by which JMJD6 promotes tumor progression and immune evasion in GC. JMJD6 is overexpressed in gastric cancer cells and promotes BRD4 expression, which upregulates <t>IRF1</t> and consequently increases PD-L1 expression. Elevated PD-L1 expression on tumor cells inhibits T cell–mediated antitumor immunity, thereby facilitating immune escape.

Anti Irf1 Rabbit Monoclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 312 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Overexpression of JMJD6 drives immune evasion via the BRD4–IRF1–PD-L1 axis and promotes malignancy in gastric cancer"

Article Title: Overexpression of JMJD6 drives immune evasion via the BRD4–IRF1–PD-L1 axis and promotes malignancy in gastric cancer

Journal: Scientific Reports

doi: 10.1038/s41598-025-30705-y

Figure Legend Snippet: Graphical abstract. Graphical abstract illustrating the hypothetical mechanism by which JMJD6 promotes tumor progression and immune evasion in GC. JMJD6 is overexpressed in gastric cancer cells and promotes BRD4 expression, which upregulates IRF1 and consequently increases PD-L1 expression. Elevated PD-L1 expression on tumor cells inhibits T cell–mediated antitumor immunity, thereby facilitating immune escape.

Techniques Used: Expressing

JMJD6 regulates BRD4, IRF1 and PD-L1 expression. ( a ) The knockdown of JMJD6 by transfection with siRNA-JMJD6 suppressed BRD4, IRF1 and PD-L1 in MKN74. In addition, the knockdown of BRD4 by transfection with siRNA-BRD4 suppressed IRF1 and PD-L1 in MKN74. In contrast, the knockdown of BRD4 did not suppress JMJD6 in MKN74. ( b ) Knockdown of JMJD6 suppressed PD-L1 and BRD4 expression in MKN74 gastric cancer (GC) cells. White dotted lines indicate nuclear boundaries. ( c ) Co-culture assay of GC cells and T cells. Under JMJD6 knockdown, T cells had more potent anti-tumor activity against GC cells compared with NC, and the proliferation ratio of GC cells was significantly decreased (mean ± SD, n = 3; error bars indicate SD, n = 3). ( d ) An impedance-based tumor-cell killing assay. The knockdown of JMJD6 increased the anti-tumor activity of T cells and inhibited the proliferation of GC cells. ( e ) JMJD6 overexpression using plasmid transfection promotes BRD4, IRF1 and PD-L1 expression. ( f ) A hypothetical model of the overexpression or activation of JMJD6 in GC cells.

Figure Legend Snippet: JMJD6 regulates BRD4, IRF1 and PD-L1 expression. ( a ) The knockdown of JMJD6 by transfection with siRNA-JMJD6 suppressed BRD4, IRF1 and PD-L1 in MKN74. In addition, the knockdown of BRD4 by transfection with siRNA-BRD4 suppressed IRF1 and PD-L1 in MKN74. In contrast, the knockdown of BRD4 did not suppress JMJD6 in MKN74. ( b ) Knockdown of JMJD6 suppressed PD-L1 and BRD4 expression in MKN74 gastric cancer (GC) cells. White dotted lines indicate nuclear boundaries. ( c ) Co-culture assay of GC cells and T cells. Under JMJD6 knockdown, T cells had more potent anti-tumor activity against GC cells compared with NC, and the proliferation ratio of GC cells was significantly decreased (mean ± SD, n = 3; error bars indicate SD, n = 3). ( d ) An impedance-based tumor-cell killing assay. The knockdown of JMJD6 increased the anti-tumor activity of T cells and inhibited the proliferation of GC cells. ( e ) JMJD6 overexpression using plasmid transfection promotes BRD4, IRF1 and PD-L1 expression. ( f ) A hypothetical model of the overexpression or activation of JMJD6 in GC cells.

Techniques Used: Expressing, Knockdown, Transfection, Co-culture Assay, Activity Assay, Over Expression, Plasmid Preparation, Activation Assay

Western Blot:

Article Title: IRF1 amplifies HSV-1-triggered antiviral innate immunity in a feed-forward manner
Article Snippet: .. The following antibodies and reagents were used for immunoblotting and immunoprecipitation: Mouse anti-FLAG monoclonal antibody (1:10,000, Dia-An Biotechnology, catalog no. 2064); Mouse anti-HA monoclonal antibody (1:5000, Dia-An Biotechnology, catalog no. 2063); Mouse anti-β-actin monoclonal antibody (1:5000, Dia-An Biotechnology, catalog no. 2060); Mouse anti-GAPDH monoclonal antibody (1:1000, Santa Cruz, sc-47724); Histone H3 antibody (1:1000, Santa Cruz, sc-517576); Rabbit anti-MITA/STING polyclonal antibody (1:5000, Proteintech, catalog no. 19851-1-AP); Rabbit anti-IRF3 polyclonal antibody (1:1000, Proteintech, catalog no. 11312-1-AP); Rabbit anti-TBK1 monoclonal antibody (1:1000, Cell Signaling Technology, catalog no. 3504); Rabbit anti-phospho-IRF3 (S386) monoclonal antibody (1:1000, Abcam, AB76493); Rabbit anti-phospho-TBK1 (S172) monoclonal antibody (1:1000, Cell Signaling Technology, catalog no. 5483); Rabbit anti-IRF1 monoclonal antibody (1:1000, Cell Signaling Technology, catalog no. 8478); Rabbit IgG (Proteintech, catalog no. 20010049); Mouse anti-ICP0 monoclonal antibody (1:1000, Santa Cruz, sc-53070); Mouse anti-ICP8 monoclonal antibody (1:1000, Santa Cruz, sc-53329); Mouse anti-ICP27 monoclonal antibody (1:1000, Santa Cruz, sc-69806); Mouse anti-ICP5 monoclonal antibody (1:1000, Santa Cruz, sc-56989); IRDye 800CW Goat anti-Rabbit and Goat anti-Mouse secondary antibodies (1:10,000, LI-COR); Anti-FLAG beads (Dia-An Biotechnology); Protein A/G agarose (GE healthcare). .. The chemical reagents used in this study include puromycin (InvivoGen), diABZI (Selleck), H-151 (MedChemExpress), MSA-2 (MedChemExpress) and SR-717 (MedChemExpress).

Immunoprecipitation:

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Journal: Scientific Reports

Article Title: Overexpression of JMJD6 drives immune evasion via the BRD4–IRF1–PD-L1 axis and promotes malignancy in gastric cancer

doi: 10.1038/s41598-025-30705-y

Figure Lengend Snippet: Graphical abstract. Graphical abstract illustrating the hypothetical mechanism by which JMJD6 promotes tumor progression and immune evasion in GC. JMJD6 is overexpressed in gastric cancer cells and promotes BRD4 expression, which upregulates IRF1 and consequently increases PD-L1 expression. Elevated PD-L1 expression on tumor cells inhibits T cell–mediated antitumor immunity, thereby facilitating immune escape.

Article Snippet: Anti-JMJD6 mouse monoclonal antibody (sc-28348; Santa Cruz Biotechnology, TX, USA), anti-PD-L1 rabbit monoclonal antibody (13684; Cell Signaling Technology, MA, USA), anti-ACTB rabbit monoclonal antibody (3700; Cell Signaling Technology), anti-BRD4 rabbit polyclonal antibody (A301-985A50; Bethyl Laboratories, TX, USA), and anti-IRF1 rabbit monoclonal antibody (8478; Cell Signaling Technology) were used.

Techniques: Expressing

Journal: Scientific Reports

Article Title: Overexpression of JMJD6 drives immune evasion via the BRD4–IRF1–PD-L1 axis and promotes malignancy in gastric cancer

doi: 10.1038/s41598-025-30705-y

Figure Lengend Snippet: JMJD6 regulates BRD4, IRF1 and PD-L1 expression. ( a ) The knockdown of JMJD6 by transfection with siRNA-JMJD6 suppressed BRD4, IRF1 and PD-L1 in MKN74. In addition, the knockdown of BRD4 by transfection with siRNA-BRD4 suppressed IRF1 and PD-L1 in MKN74. In contrast, the knockdown of BRD4 did not suppress JMJD6 in MKN74. ( b ) Knockdown of JMJD6 suppressed PD-L1 and BRD4 expression in MKN74 gastric cancer (GC) cells. White dotted lines indicate nuclear boundaries. ( c ) Co-culture assay of GC cells and T cells. Under JMJD6 knockdown, T cells had more potent anti-tumor activity against GC cells compared with NC, and the proliferation ratio of GC cells was significantly decreased (mean ± SD, n = 3; error bars indicate SD, n = 3). ( d ) An impedance-based tumor-cell killing assay. The knockdown of JMJD6 increased the anti-tumor activity of T cells and inhibited the proliferation of GC cells. ( e ) JMJD6 overexpression using plasmid transfection promotes BRD4, IRF1 and PD-L1 expression. ( f ) A hypothetical model of the overexpression or activation of JMJD6 in GC cells.

Techniques: Expressing, Knockdown, Transfection, Co-culture Assay, Activity Assay, Over Expression, Plasmid Preparation, Activation Assay

HSV-1 infection induces IRF1 and MITA/STING contributes to IRF1 induction. (A–B) HT1080 cells were either mock-infected or infected with HSV-1 (MOI = 5) for 8 h. The expression of IRF1 was quantified by RT-qPCR (A), and whole cell lysates (WCLs) were collected and analyzed by immunoblotting (B). (C–E) HT1080 cells transduced with control sgRNA (Ctrl) or sgRNA targeting MITA/STING were mock-infected or infected with HSV-1 (MOI = 5), and the expression of IRF1 (C) , IFNB1 (D), and CXCL10 (E) was quantified at 8 h post-infection. (F) HT1080 cells were mock-infected or infected with HSV-1 (MOI = 5), and WCLs were analyzed by immunoblotting at 8 h post-infection. (G–I) HT1080 cells were treated with H-151 (5 μM), and mock-infected or infected with HSV-1 (MOI = 5) for 8 h. The expression of IRF1 (G) , IFNB1 (H), and CXCL10 (I) was quantified by RT-qPCR. (J) HT1080 cells were treated with H-151 (5 μM), and mock-infected or infected with HSV-1 (MOI = 5) for 8 h. WCLs were analyzed by immunoblotting. (K–L) HT1080 cells transduced with control sgRNA (Ctrl) or sgRNA targeting MITA/STING. The expression of IRF1 was quantified by RT-qPCR (K), and WCLs were analyzed by immunoblotting (L).

Journal: Cell Insight

Article Title: IRF1 amplifies HSV-1-triggered antiviral innate immunity in a feed-forward manner

doi: 10.1016/j.cellin.2025.100255

Figure Lengend Snippet: HSV-1 infection induces IRF1 and MITA/STING contributes to IRF1 induction. (A–B) HT1080 cells were either mock-infected or infected with HSV-1 (MOI = 5) for 8 h. The expression of IRF1 was quantified by RT-qPCR (A), and whole cell lysates (WCLs) were collected and analyzed by immunoblotting (B). (C–E) HT1080 cells transduced with control sgRNA (Ctrl) or sgRNA targeting MITA/STING were mock-infected or infected with HSV-1 (MOI = 5), and the expression of IRF1 (C) , IFNB1 (D), and CXCL10 (E) was quantified at 8 h post-infection. (F) HT1080 cells were mock-infected or infected with HSV-1 (MOI = 5), and WCLs were analyzed by immunoblotting at 8 h post-infection. (G–I) HT1080 cells were treated with H-151 (5 μM), and mock-infected or infected with HSV-1 (MOI = 5) for 8 h. The expression of IRF1 (G) , IFNB1 (H), and CXCL10 (I) was quantified by RT-qPCR. (J) HT1080 cells were treated with H-151 (5 μM), and mock-infected or infected with HSV-1 (MOI = 5) for 8 h. WCLs were analyzed by immunoblotting. (K–L) HT1080 cells transduced with control sgRNA (Ctrl) or sgRNA targeting MITA/STING. The expression of IRF1 was quantified by RT-qPCR (K), and WCLs were analyzed by immunoblotting (L).

Article Snippet: The following antibodies and reagents were used for immunoblotting and immunoprecipitation: Mouse anti-FLAG monoclonal antibody (1:10,000, Dia-An Biotechnology, catalog no. 2064); Mouse anti-HA monoclonal antibody (1:5000, Dia-An Biotechnology, catalog no. 2063); Mouse anti-β-actin monoclonal antibody (1:5000, Dia-An Biotechnology, catalog no. 2060); Mouse anti-GAPDH monoclonal antibody (1:1000, Santa Cruz, sc-47724); Histone H3 antibody (1:1000, Santa Cruz, sc-517576); Rabbit anti-MITA/STING polyclonal antibody (1:5000, Proteintech, catalog no. 19851-1-AP); Rabbit anti-IRF3 polyclonal antibody (1:1000, Proteintech, catalog no. 11312-1-AP); Rabbit anti-TBK1 monoclonal antibody (1:1000, Cell Signaling Technology, catalog no. 3504); Rabbit anti-phospho-IRF3 (S386) monoclonal antibody (1:1000, Abcam, AB76493); Rabbit anti-phospho-TBK1 (S172) monoclonal antibody (1:1000, Cell Signaling Technology, catalog no. 5483); Rabbit anti-IRF1 monoclonal antibody (1:1000, Cell Signaling Technology, catalog no. 8478); Rabbit IgG (Proteintech, catalog no. 20010049); Mouse anti-ICP0 monoclonal antibody (1:1000, Santa Cruz, sc-53070); Mouse anti-ICP8 monoclonal antibody (1:1000, Santa Cruz, sc-53329); Mouse anti-ICP27 monoclonal antibody (1:1000, Santa Cruz, sc-69806); Mouse anti-ICP5 monoclonal antibody (1:1000, Santa Cruz, sc-56989); IRDye 800CW Goat anti-Rabbit and Goat anti-Mouse secondary antibodies (1:10,000, LI-COR); Anti-FLAG beads (Dia-An Biotechnology); Protein A/G agarose (GE healthcare).

Techniques: Infection, Expressing, Quantitative RT-PCR, Western Blot, Transduction, Control

MITA activation is sufficient to induce IRF1 . (A) HT1080 cells were stimulated with diABZI (2.5 μM), and the expression of IRF1 , IFNB1 , ISG56, and CXCL10 was quantified by RT-qPCR at 6 h post-stimulation. (B) HT1080 cells were stimulated with diABZI (2.5 μM), and WCLs were analyzed by immunoblotting at 6 h post-stimulation. (C) THP-1 cells were stimulated with diABZI (2.5 μM), and the expression of IRF1 , IFNB1 , ISG56, and CXCL10 was quantified by RT-qPCR at 6 h post-stimulation. (D) THP-1 cells were stimulated with diABZI (2.5 μM), and WCLs were analyzed by immunoblotting at the indicated time points post-stimulation. (E) HT1080 cells were stimulated with MSA-2 (20 μM) or SR-717 (10 μM), and the expression of IRF1 , IFNB1 , ISG56, and CXCL10 was quantified by RT-qPCR at 8 h post-stimulation. (F) HT1080 cells were stimulated with MSA-2 (20 μM) or SR-717 (10 μM), and WCLs were analyzed by immunoblotting at 8 h post-stimulation.

Journal: Cell Insight

Article Title: IRF1 amplifies HSV-1-triggered antiviral innate immunity in a feed-forward manner

doi: 10.1016/j.cellin.2025.100255

Figure Lengend Snippet: MITA activation is sufficient to induce IRF1 . (A) HT1080 cells were stimulated with diABZI (2.5 μM), and the expression of IRF1 , IFNB1 , ISG56, and CXCL10 was quantified by RT-qPCR at 6 h post-stimulation. (B) HT1080 cells were stimulated with diABZI (2.5 μM), and WCLs were analyzed by immunoblotting at 6 h post-stimulation. (C) THP-1 cells were stimulated with diABZI (2.5 μM), and the expression of IRF1 , IFNB1 , ISG56, and CXCL10 was quantified by RT-qPCR at 6 h post-stimulation. (D) THP-1 cells were stimulated with diABZI (2.5 μM), and WCLs were analyzed by immunoblotting at the indicated time points post-stimulation. (E) HT1080 cells were stimulated with MSA-2 (20 μM) or SR-717 (10 μM), and the expression of IRF1 , IFNB1 , ISG56, and CXCL10 was quantified by RT-qPCR at 8 h post-stimulation. (F) HT1080 cells were stimulated with MSA-2 (20 μM) or SR-717 (10 μM), and WCLs were analyzed by immunoblotting at 8 h post-stimulation.

Techniques: Activation Assay, Expressing, Quantitative RT-PCR, Western Blot

IRF1 restricts HSV-1 replication . (A) HT1080 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were infected with HSV-1 (MOI = 0.01). Viral titers in the supernatants were quantified at 48 h post-infection. (B–E) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 1). The expression of ICP0, ICP8, and UL19 was quantified by RT-qPCR (B–D). The mock-infected samples were labeled as N.D. (not detected), and the signals from wild-type (WT) cells infected with HSV-1 were normalized to 1. WCLs were analyzed by immunoblotting at 8 h post-infection (E). (F) HEK293T cells were transfected with an IFN-β promoter reporter plasmid mixture with increasing amounts of IRF1 expression plasmids (0, 0.1, 0.2, or 0.5 μg). Luciferase activities were measured at 24 h post-transfection. (G–H) HT1080 cells stably expressing vector control, IRF1-WT, or IRF1-R82A were infected with HSV-1-GFP (MOI = 0.05), and GFP expression was imaged at 24 h post-infection (G). Scale bars,100 μm. Viral titers in the supernatants were quantified at 24 h post-infection (H).

Journal: Cell Insight

Article Title: IRF1 amplifies HSV-1-triggered antiviral innate immunity in a feed-forward manner

doi: 10.1016/j.cellin.2025.100255

Figure Lengend Snippet: IRF1 restricts HSV-1 replication . (A) HT1080 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were infected with HSV-1 (MOI = 0.01). Viral titers in the supernatants were quantified at 48 h post-infection. (B–E) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 1). The expression of ICP0, ICP8, and UL19 was quantified by RT-qPCR (B–D). The mock-infected samples were labeled as N.D. (not detected), and the signals from wild-type (WT) cells infected with HSV-1 were normalized to 1. WCLs were analyzed by immunoblotting at 8 h post-infection (E). (F) HEK293T cells were transfected with an IFN-β promoter reporter plasmid mixture with increasing amounts of IRF1 expression plasmids (0, 0.1, 0.2, or 0.5 μg). Luciferase activities were measured at 24 h post-transfection. (G–H) HT1080 cells stably expressing vector control, IRF1-WT, or IRF1-R82A were infected with HSV-1-GFP (MOI = 0.05), and GFP expression was imaged at 24 h post-infection (G). Scale bars,100 μm. Viral titers in the supernatants were quantified at 24 h post-infection (H).

Techniques: Transduction, Control, Infection, Expressing, Quantitative RT-PCR, Labeling, Western Blot, Transfection, Plasmid Preparation, Luciferase, Stable Transfection

IRF1 amplifies HSV-1-triggered antiviral innate immunity. (A–B) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 5) for 6 h. RNA-seq was performed, and a Venn diagram displayed significantly upregulated ISG genes after HSV-1 infection (A). The human ISG gene set was obtained from previous studies ( ; ). Paired line plots showed the expression levels of these upregulated ISGs in control and IRF1 knockout cells (B). (C–I) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 5) for 6 h. The expression levels of the indicated genes were quantified by RT-qPCR.

Journal: Cell Insight

Article Title: IRF1 amplifies HSV-1-triggered antiviral innate immunity in a feed-forward manner

doi: 10.1016/j.cellin.2025.100255

Figure Lengend Snippet: IRF1 amplifies HSV-1-triggered antiviral innate immunity. (A–B) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 5) for 6 h. RNA-seq was performed, and a Venn diagram displayed significantly upregulated ISG genes after HSV-1 infection (A). The human ISG gene set was obtained from previous studies ( ; ). Paired line plots showed the expression levels of these upregulated ISGs in control and IRF1 knockout cells (B). (C–I) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 5) for 6 h. The expression levels of the indicated genes were quantified by RT-qPCR.

Techniques: Transduction, Control, Infection, RNA Sequencing, Expressing, Knock-Out, Quantitative RT-PCR

$IRF1 interacts with IRF3 and promotes IRF3 recruitment to ISG promoters . (A) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 5), and WCLs were analyzed by immunoblotting at 8 h post-infection. (B) THP-1 cells were mock-infected or infected with HSV-1 (MOI = 5), and nuclear and cytoplasmic fractions were isolated at the indicated time points and analyzed by immunoblotting. (C) HEK293T cells were transfected with the indicated plasmids, and WCLs were collected for immunoprecipitation with anti-FLAG affinity agarose. The input and precipitated samples were analyzed by immunoblotting. (D) HT1080 cells were infected with HSV-1 (MOI = 10) for 8 h. Co-immunoprecipitation was performed with the indicated antibodies, followed by immunoblotting analysis. (E) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 10), and nuclear and cytoplasmic fractions were isolated at 8 h post-infection and analyzed by immunoblotting. (F) THP-1 cells were mock-infected or infected with HSV-1 (MOI = 10) for 5 or 10 h. Cell lysates were collected and pulldown assays were performed using a biotin-labeled ISG54 ISRE probe. The input and probe-bound proteins were analyzed with the indicated antibodies. (G) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 10) for 8 h. Cell lysates were collected and pulldown assays were performed using a biotin-labeled ISG54 ISRE probe. The input and probe-bound proteins were analyzed using an anti-IRF3 polyclonal antibody, and the input samples were also analyzed using an anti-IRF1 monoclonal antibody. (H) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were infected with HSV-1 (MOI = 10) for 10 h, followed by chromatin immunoprecipitation (ChIP) using an anti-IRF3 antibody or control IgG. IRF3 occupancy at the IFNB1 and IFNL1 promoter regions was assessed by qPCR.$

Journal: Cell Insight

Article Title: IRF1 amplifies HSV-1-triggered antiviral innate immunity in a feed-forward manner

doi: 10.1016/j.cellin.2025.100255

Figure Lengend Snippet: IRF1 interacts with IRF3 and promotes IRF3 recruitment to ISG promoters . (A) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 5), and WCLs were analyzed by immunoblotting at 8 h post-infection. (B) THP-1 cells were mock-infected or infected with HSV-1 (MOI = 5), and nuclear and cytoplasmic fractions were isolated at the indicated time points and analyzed by immunoblotting. (C) HEK293T cells were transfected with the indicated plasmids, and WCLs were collected for immunoprecipitation with anti-FLAG affinity agarose. The input and precipitated samples were analyzed by immunoblotting. (D) HT1080 cells were infected with HSV-1 (MOI = 10) for 8 h. Co-immunoprecipitation was performed with the indicated antibodies, followed by immunoblotting analysis. (E) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 10), and nuclear and cytoplasmic fractions were isolated at 8 h post-infection and analyzed by immunoblotting. (F) THP-1 cells were mock-infected or infected with HSV-1 (MOI = 10) for 5 or 10 h. Cell lysates were collected and pulldown assays were performed using a biotin-labeled ISG54 ISRE probe. The input and probe-bound proteins were analyzed with the indicated antibodies. (G) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were mock-infected or infected with HSV-1 (MOI = 10) for 8 h. Cell lysates were collected and pulldown assays were performed using a biotin-labeled ISG54 ISRE probe. The input and probe-bound proteins were analyzed using an anti-IRF3 polyclonal antibody, and the input samples were also analyzed using an anti-IRF1 monoclonal antibody. (H) THP-1 cells transduced with control sgRNA (Ctrl) or sgRNA targeting IRF1 were infected with HSV-1 (MOI = 10) for 10 h, followed by chromatin immunoprecipitation (ChIP) using an anti-IRF3 antibody or control IgG. IRF3 occupancy at the IFNB1 and IFNL1 promoter regions was assessed by qPCR.

Techniques: Transduction, Control, Infection, Western Blot, Isolation, Transfection, Immunoprecipitation, Labeling, Chromatin Immunoprecipitation

IRF1 promotes antiviral innate immunity through its DNA-binding activity . (A) HEK293T cells were transfected with the indicated plasmids, and WCLs were collected for immunoprecipitation with anti-FLAG affinity agarose. The input and immunoprecipitated samples were analyzed by immunoblotting. (B–E) THP-1 cells stably expressing vector control, IRF1-WT, or IRF1-R82A were mock-infected or infected with HSV-1 (MOI = 5). The indicated genes were quantified by RT-qPCR (B–D), and WCLs were analyzed by immunoblotting at 8 h post-infection (E). (F) THP-1 cells stably expressing vector control, IRF1-WT, or IRF1-R82A were mock-infected or infected with HSV-1 (MOI = 10) for 8 h. Cell lysates were collected and pulldown assays were performed using a biotin-labeled ISG54 ISRE probe. The input and probe-bound proteins were analyzed by immunoblotting using an anti-IRF3 polyclonal antibody, and the input samples were also analyzed using an anti-IRF1 monoclonal antibody. (G–K) HT1080 cells stably expressing vector control, IRF1-WT, or IRF1-R82A were mock-infected or infected with VSV (MOI = 5) for 8 h. The expression levels of the indicated genes were quantified by RT-qPCR.

Journal: Cell Insight

Article Title: IRF1 amplifies HSV-1-triggered antiviral innate immunity in a feed-forward manner

doi: 10.1016/j.cellin.2025.100255

Figure Lengend Snippet: IRF1 promotes antiviral innate immunity through its DNA-binding activity . (A) HEK293T cells were transfected with the indicated plasmids, and WCLs were collected for immunoprecipitation with anti-FLAG affinity agarose. The input and immunoprecipitated samples were analyzed by immunoblotting. (B–E) THP-1 cells stably expressing vector control, IRF1-WT, or IRF1-R82A were mock-infected or infected with HSV-1 (MOI = 5). The indicated genes were quantified by RT-qPCR (B–D), and WCLs were analyzed by immunoblotting at 8 h post-infection (E). (F) THP-1 cells stably expressing vector control, IRF1-WT, or IRF1-R82A were mock-infected or infected with HSV-1 (MOI = 10) for 8 h. Cell lysates were collected and pulldown assays were performed using a biotin-labeled ISG54 ISRE probe. The input and probe-bound proteins were analyzed by immunoblotting using an anti-IRF3 polyclonal antibody, and the input samples were also analyzed using an anti-IRF1 monoclonal antibody. (G–K) HT1080 cells stably expressing vector control, IRF1-WT, or IRF1-R82A were mock-infected or infected with VSV (MOI = 5) for 8 h. The expression levels of the indicated genes were quantified by RT-qPCR.

Techniques: Binding Assay, Activity Assay, Transfection, Immunoprecipitation, Western Blot, Stable Transfection, Expressing, Plasmid Preparation, Control, Infection, Quantitative RT-PCR, Labeling

Journal: Cell Reports Medicine

Article Title: Macrophages are activated toward phagocytic lymphoma cell clearance by pentose phosphate pathway inhibition

doi: 10.1016/j.xcrm.2024.101830

Figure Lengend Snippet:

Article Snippet: Rabbit monoclonal anti-IRF1 (D5E4) , Cell Signaling Technology , Cat#8478; RRID: AB_10949108.

Techniques: Staining, Virus, Recombinant, Bicinchoninic Acid Protein Assay, Cell Viability Assay, Enzyme-linked Immunosorbent Assay, Plasmid Preparation, Blocking Assay, Phospho-proteomics, Purification, Mass Spectrometry, Software, Modification

Journal: Cell reports

Article Title: Proteogenomic characterization of primary colorectal cancer and metastatic progression identifies proteome-based subtypes and signatures

doi: 10.1016/j.celrep.2024.113810

Figure Lengend Snippet: (A) A heatmap with immune signature and clinical attributes. The immune score significantly correlates with IHC immune infiltrate scores and immune-related pathways, except for CD4 and FOXP3 IHC scores. * denotes statistical significance. (B) A GSE plot with antigen processing and presenting pathways from KEGG and REACTOME terms. Both antigen processing pathways are strongly downregulated in the immune-cold group. (C) A correlation plot (Spearman correlation coefficient) of IHC scores that involve the antigen processing machinery. Protein expression of STAT is derived from mass spectrometry data. The IFNγ response score is derived from ssGSEA analysis with HALLMARK_INTERFERON_GAMMA_RESPONSE. *p < 0.05, **p < 0.01, ***p < 0.001. Clear correlations of CD4-MHC class II and CD8-MHC class II are shown with statistical significance. In addition, the IFNγ pathway and STAT1 positively correlate with their direct targets (IRF1 and CIITA) and with downstream targets (MHC class I and II). (D) A correlation plot (Spearman correlation coefficient) with IRF1 IHC score and antigen processing machinery protein expression. *p < 0.05, **p < 0.01. ***p < 0.001. IRF1 expression positively correlates with immunoproteasome subunits but negatively correlates with catalytic conventional proteasome subunits. (E) Boxplots of IHC analysis results for HLA-ABC, HLA-DP/DQ/DR, CD3, CD4, CD8, IFR1, and CIITA. 22 P1, 42 P2, 51 P3, 16 M1, 53 M2, and 30 M3 samples were assessed. M1 shows the lowest expression of HLA-ABC (MHC class I) among all proteome subtypes. Although the infiltrating lymphocyte profile (CD3, CD4, and CD8) shows no significant differences, M1 has the lowest CD3+ lymphocyte count and lower median counts of CD8+ lymphocytes than other subtypes. This is concordant with the lowest expression of HLA-ABC (MHC class I) in the M1 subtype. In addition, IRF1, a key transcription initiator of MHC class I, shows the lowest expression in M1. (F) Kaplan-Meier survival curve analysis stratified by CD4 expression level of pCRC. (G) Kaplan-Meier survival curve analysis stratified by CD8 expression level of pCRC. (H) Kaplan-Meier survival curve analysis stratified by CD4 expression level of mCRC. (I) Kaplan-Meier survival curve analysis stratified by CD8 expression level of mCRC.

Article Snippet: Rabbit monoclonal anti-IRF1 , Abcam , Cat. # ab243895; RRID: AB_2832955.

Techniques: Expressing, Derivative Assay, Mass Spectrometry

Journal: Cell reports

Article Title: Proteogenomic characterization of primary colorectal cancer and metastatic progression identifies proteome-based subtypes and signatures

doi: 10.1016/j.celrep.2024.113810

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: Rabbit monoclonal anti-IRF1 , Abcam , Cat. # ab243895; RRID: AB_2832955.

Techniques: Recombinant, Bicinchoninic Acid Protein Assay, Software

Review

anti irf1 rabbit monoclonal antibody (Cell Signaling Technology Inc)

Structured Review

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1) Product Images from "Overexpression of JMJD6 drives immune evasion via the BRD4–IRF1–PD-L1 axis and promotes malignancy in gastric cancer"

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