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rabbit polyclonal anti irf3 antibody (Proteintech)

Proteintech rabbit polyclonal anti irf3 antibody
Rabbit Polyclonal Anti Irf3 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit polyclonal anti irf3 antibody/product/Proteintech
Average 96 stars, based on 1 article reviews

rabbit polyclonal anti irf3 antibody - by Bioz Stars, 2026-03

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rabbit anti p irf3 ser396 polyclonal antibody (Proteintech)

Proteintech rabbit anti p irf3 ser396 polyclonal antibody
Rabbit Anti P Irf3 Ser396 Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit anti p irf3 ser396 polyclonal antibody/product/Proteintech
Average 96 stars, based on 1 article reviews

rabbit anti p irf3 ser396 polyclonal antibody - by Bioz Stars, 2026-03

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rabbit anti irf3 polyclonal antibody (Proteintech)

Proteintech rabbit anti irf3 polyclonal antibody
$IRF1 interacts with <t>IRF3</t> 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 <t>an</t> <t>anti-IRF3</t> <t>polyclonal</t> 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.$
Rabbit Anti Irf3 Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit anti irf3 polyclonal antibody/product/Proteintech
Average 96 stars, based on 1 article reviews

rabbit anti irf3 polyclonal antibody - by Bioz Stars, 2026-03

96/100 stars

Buy from Supplier

rabbit ani irf3 polyclonal antibody (Proteintech)

Proteintech rabbit ani irf3 polyclonal antibody
$IRF1 interacts with <t>IRF3</t> 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 <t>an</t> <t>anti-IRF3</t> <t>polyclonal</t> 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.$
Rabbit Ani Irf3 Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit ani irf3 polyclonal antibody/product/Proteintech
Average 96 stars, based on 1 article reviews

rabbit ani irf3 polyclonal antibody - by Bioz Stars, 2026-03

96/100 stars

Buy from Supplier

irf3 rabbit polyclonal antibody (Proteintech)

Proteintech irf3 rabbit polyclonal antibody

Figure 3. Selectively packaging of phosphorylated STING into COPII vesicles and spatial activation of TBK1 and <t>IRF3</t> signaling using a cell-free COPII vesicle reconstitution approach. A) Schematic representation of the cell-free reconstitution strategy for COPII vesicle formation. B) Diagram illustrating the recognition of pSGME and pFS motifs by Sec24, leading to the packaging of both phosphorylated and unphosphorylated STING into COPII vesicles. C) Western blot analysis of STING packaging into COPII vesicles. i⃝Denotes 1% input. Phosphorylated STING is indicated by a red triangle. Sec22

Irf3 Rabbit Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/irf3 rabbit polyclonal antibody/product/Proteintech
Average 96 stars, based on 1 article reviews

irf3 rabbit polyclonal antibody - by Bioz Stars, 2026-03

96/100 stars

Buy from Supplier

rabbit polyclonal anti-irf3 (#sc-9082) (Santa Cruz Biotechnology)

Santa Cruz Biotechnology rabbit polyclonal anti-irf3 (#sc-9082)

Rabbit Polyclonal Anti Irf3 (#Sc 9082), supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit polyclonal anti-irf3 (#sc-9082)/product/Santa Cruz Biotechnology
Average 90 stars, based on 1 article reviews

rabbit polyclonal anti-irf3 (#sc-9082) - by Bioz Stars, 2026-03

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$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.

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: 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

Figure 3. Selectively packaging of phosphorylated STING into COPII vesicles and spatial activation of TBK1 and IRF3 signaling using a cell-free COPII vesicle reconstitution approach. A) Schematic representation of the cell-free reconstitution strategy for COPII vesicle formation. B) Diagram illustrating the recognition of pSGME and pFS motifs by Sec24, leading to the packaging of both phosphorylated and unphosphorylated STING into COPII vesicles. C) Western blot analysis of STING packaging into COPII vesicles. i⃝Denotes 1% input. Phosphorylated STING is indicated by a red triangle. Sec22

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: STING COPII ER Export Trafficking and Signaling Primed by Phosphorylation Switches.

doi: 10.1002/advs.202503660

Figure Lengend Snippet: Figure 3. Selectively packaging of phosphorylated STING into COPII vesicles and spatial activation of TBK1 and IRF3 signaling using a cell-free COPII vesicle reconstitution approach. A) Schematic representation of the cell-free reconstitution strategy for COPII vesicle formation. B) Diagram illustrating the recognition of pSGME and pFS motifs by Sec24, leading to the packaging of both phosphorylated and unphosphorylated STING into COPII vesicles. C) Western blot analysis of STING packaging into COPII vesicles. i⃝Denotes 1% input. Phosphorylated STING is indicated by a red triangle. Sec22

Article Snippet: Antibodies and Chemicals: All the antibodies used in this study were purchased as follows: STING Rabbit mAb (CST, Cat: 13647), PhosphoSTING (Ser366) (E9A9K) rabbit mAb (CST, Cat: 50907), TBK1/NAK rabbit polyclonal antibody (CST, Cat:3013), Phospho-TBK1/NAK (Ser172) (D52C2) rabbit mAb (CST, Cat: 5483), IRF3 rabbit polyclonal antibody (Proteintech, Cat: 11312-1-AP), Phospho-IRF-3 (Ser396) (4D4G) rabbit mAb(CST, Cat: 4947), TMP21 rabbit polyclonal antibody (Proteintech, Cat: 15199-1-AP), Sec22Brabbit mAb (CST, Cat:ab181076), Ribophorin I rabbit mAb (CST, Cat:ab197888), rabbit polyclonal anti-GM130 (Proteintech, Cat: 11308-1-AP), rabbit polyclonal anti-Sec61β (Proteintech, Cat: 15087-1-AP), rabbit polyclonal anti-ERGIC53 (Proteintech, Cat: 13364-1-AP), mouse monoclonal anti-GAPDH (Proteintech, Cat: 60004-1-Ig), goat anti-rabbit IgG (H+L) secondary antibody, HRP (Invitrogen, Cat: 31460), goat antimouse IgG (H+L) secondary antibody, HRP (Invitrogen, Cat: 31430), goat anti-rabbit IgG H&L (Alexa Fluor 594) antibody (Abcam, Cat: ab150080).

Techniques: Activation Assay, Western Blot

Figure 4. 4-PBA attenuates STING-mediated IRF3 activation by competing with STING for Sec24 B sites. A) 4-PBA inhibits the IFN-𝛽luciferase reporter response in a concentration-dependent manner. Data is presented as mean ± SEM after analysis of two-way ANOVA, n = 3. ****P < 0.0001, compared to the 0 mM 4-PBA + cGAMP group. B) 4-PBA reduces the expression of IFIT1-3, as measured by RT-qPCR. Data is presented as mean ± SEM after analysis of one-way ANOVA, n = 4. ****P < 0.0001, compared to the cGAMP group. C,D) 4-PBA treatment does not aﬀect TBK1 activation but signiﬁcantly inhibits IRF3 phosphorylation. E,F) 4-PBA delays STING export from the ER, with rates calculated based on the colocalization of STING with ERGIC. Data is presented as mean ± SEM after analysis of one-way ANOVA, n = 60. ****P < 0.0001, ns indicates no signiﬁcant diﬀerence. G) Adding 4- PBA reduced the packaging of phosphorylated STING in COPII vesicles. H,I) 4-PBA attenuates hyperactivation of SAVI-associated STING mutants, as demonstrated by IFN-𝛽luciferase reporter assays (G) and Western blot analysis (H). Data is presented as mean ± SEM after one-way ANOVA analysis, n = 3. ****P < 0.0001, compared to 0 mM 4-PBA.

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: STING COPII ER Export Trafficking and Signaling Primed by Phosphorylation Switches.

doi: 10.1002/advs.202503660

Figure Lengend Snippet: Figure 4. 4-PBA attenuates STING-mediated IRF3 activation by competing with STING for Sec24 B sites. A) 4-PBA inhibits the IFN-𝛽luciferase reporter response in a concentration-dependent manner. Data is presented as mean ± SEM after analysis of two-way ANOVA, n = 3. ****P < 0.0001, compared to the 0 mM 4-PBA + cGAMP group. B) 4-PBA reduces the expression of IFIT1-3, as measured by RT-qPCR. Data is presented as mean ± SEM after analysis of one-way ANOVA, n = 4. ****P < 0.0001, compared to the cGAMP group. C,D) 4-PBA treatment does not aﬀect TBK1 activation but signiﬁcantly inhibits IRF3 phosphorylation. E,F) 4-PBA delays STING export from the ER, with rates calculated based on the colocalization of STING with ERGIC. Data is presented as mean ± SEM after analysis of one-way ANOVA, n = 60. ****P < 0.0001, ns indicates no signiﬁcant diﬀerence. G) Adding 4- PBA reduced the packaging of phosphorylated STING in COPII vesicles. H,I) 4-PBA attenuates hyperactivation of SAVI-associated STING mutants, as demonstrated by IFN-𝛽luciferase reporter assays (G) and Western blot analysis (H). Data is presented as mean ± SEM after one-way ANOVA analysis, n = 3. ****P < 0.0001, compared to 0 mM 4-PBA.

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

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