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Bioss anti irf7 rabbit polyclonal antibody pab
List of primers used in RT-qPCR.

Anti Irf7 Rabbit Polyclonal Antibody Pab, supplied by Bioss, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 92 stars, based on 4 article reviews

anti irf7 rabbit polyclonal antibody pab - by Bioz Stars, 2026-03

92/100 stars

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1) Product Images from "Infectious bursal disease virus affecting interferon regulatory factor 7 signaling through VP3 protein to facilitate viral replication"

Article Title: Infectious bursal disease virus affecting interferon regulatory factor 7 signaling through VP3 protein to facilitate viral replication

Journal: Frontiers in Cellular and Infection Microbiology

doi: 10.3389/fcimb.2024.1529159

Figure Legend Snippet: List of primers used in RT-qPCR.

Techniques Used: Sequencing

IBDV infection can suppress the expression of IRF7. IBDV viral load, relative expression levels of the IRF7 and IFN-β gene (detected by RT-qPCR) in DF-1 cells infected with 1 MOI vvIBDV NN1172 (A) or attenuated IBDV B87 (B) at different time points. (C) IBDV viral load, relative expression levels of the IRF7 and IFN-β gene in DF-1 cells infected with 0.5, 1, or 1.5 MOI vvIBDV at different time points. (D-F) The IRF7 and VP2 protein levels in DF-1 cells (detected by western blot) infected with 0.5, 1, 1.5 MOI vvIBDV at different time point. (G) The protein levels of IFN-β at different time points after varying titers of IBDV infection. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p < 0.05; **p < 0.01.

Figure Legend Snippet: IBDV infection can suppress the expression of IRF7. IBDV viral load, relative expression levels of the IRF7 and IFN-β gene (detected by RT-qPCR) in DF-1 cells infected with 1 MOI vvIBDV NN1172 (A) or attenuated IBDV B87 (B) at different time points. (C) IBDV viral load, relative expression levels of the IRF7 and IFN-β gene in DF-1 cells infected with 0.5, 1, or 1.5 MOI vvIBDV at different time points. (D-F) The IRF7 and VP2 protein levels in DF-1 cells (detected by western blot) infected with 0.5, 1, 1.5 MOI vvIBDV at different time point. (G) The protein levels of IFN-β at different time points after varying titers of IBDV infection. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p < 0.05; **p < 0.01.

Techniques Used: Infection, Expressing, Quantitative RT-PCR, Western Blot, Standard Deviation

Overexpression of IRF7 inhibits IBDV replication. (A) After transfecting DF-1 cells with the pcDNA3.1-His-IRF7 plasmid for 6 hours, cells were infected with 1 MOI vvIBDV. Samples were collected at various time points, and western blot was used to measure the expression levels of IRF7 and IBDV VP2 proteins. Alternatively, relative intensities of VP2 were normalized to β-actin. (B) RT-qPCR was employed to measure the IBDV viral load at various time points. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p < 0.05; **p < 0.01.

Figure Legend Snippet: Overexpression of IRF7 inhibits IBDV replication. (A) After transfecting DF-1 cells with the pcDNA3.1-His-IRF7 plasmid for 6 hours, cells were infected with 1 MOI vvIBDV. Samples were collected at various time points, and western blot was used to measure the expression levels of IRF7 and IBDV VP2 proteins. Alternatively, relative intensities of VP2 were normalized to β-actin. (B) RT-qPCR was employed to measure the IBDV viral load at various time points. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p < 0.05; **p < 0.01.

Techniques Used: Over Expression, Plasmid Preparation, Infection, Western Blot, Expressing, Quantitative RT-PCR, Standard Deviation

Knocking down IRF7 promotes IBDV replication. (A) DF-1 cells were transfected with siRNA targeting IRF7 for 6 hours, followed by infection with 1 MOI vvIBDV. Samples were collected at various time points, and western blot was used to measure the expression levels of IRF7 and IBDV VP2 proteins. Alternatively, relative intensities of IRF7 and VP2 were normalized to β-actin, respectively. (B) RT-qPCR was employed to measure the IBDV viral load at various time points. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p < 0.05; **p < 0.01.

Figure Legend Snippet: Knocking down IRF7 promotes IBDV replication. (A) DF-1 cells were transfected with siRNA targeting IRF7 for 6 hours, followed by infection with 1 MOI vvIBDV. Samples were collected at various time points, and western blot was used to measure the expression levels of IRF7 and IBDV VP2 proteins. Alternatively, relative intensities of IRF7 and VP2 were normalized to β-actin, respectively. (B) RT-qPCR was employed to measure the IBDV viral load at various time points. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p < 0.05; **p < 0.01.

Techniques Used: Transfection, Infection, Western Blot, Expressing, Quantitative RT-PCR, Standard Deviation

Overexpression of IRF7 couldn’t inhibit IRF7 degradation in vvIBDV-infected cells. (A) DF-1 cells were transfected with pcDNA3.1-His-IRF7 and infected with 1 MOI vvIBDV. Samples were collected at 6, 9, 12, 18, and 24 hpi, and the expression of IRF7 protein was detected using western blot. Alternatively, relative intensities of IRF7 were normalized to β-actin. (B) DF-1 cells were transfected with pcDNA3.1-His-IRF7 and infected with 1 MOI attenuated IBDV. Samples were collected at 12, 18, 24, and 36 hpi, and the expression of IRF7 protein was detected using western blot. Alternatively, relative intensities of IRF7 were normalized to β-actin. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. **p < 0.01.

Figure Legend Snippet: Overexpression of IRF7 couldn’t inhibit IRF7 degradation in vvIBDV-infected cells. (A) DF-1 cells were transfected with pcDNA3.1-His-IRF7 and infected with 1 MOI vvIBDV. Samples were collected at 6, 9, 12, 18, and 24 hpi, and the expression of IRF7 protein was detected using western blot. Alternatively, relative intensities of IRF7 were normalized to β-actin. (B) DF-1 cells were transfected with pcDNA3.1-His-IRF7 and infected with 1 MOI attenuated IBDV. Samples were collected at 12, 18, 24, and 36 hpi, and the expression of IRF7 protein was detected using western blot. Alternatively, relative intensities of IRF7 were normalized to β-actin. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. **p < 0.01.

Techniques Used: Over Expression, Infection, Transfection, Expressing, Western Blot, Standard Deviation

IBDV affects the expression of IRF7 through the proteasomal pathway. In the control group, cells were treated with DMSO, while in the experimental group, cells were treated with different inhibitors (PYR-41, Wortmannin, MG132) after being infected with vvIBDV. Samples were then collected for western blot analysis to measure the expression levels of IRF7 and VP2 proteins. Alternatively, relative intensities of IRF7 and VP2 were normalized to β-actin. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. **p < 0.01.

Figure Legend Snippet: IBDV affects the expression of IRF7 through the proteasomal pathway. In the control group, cells were treated with DMSO, while in the experimental group, cells were treated with different inhibitors (PYR-41, Wortmannin, MG132) after being infected with vvIBDV. Samples were then collected for western blot analysis to measure the expression levels of IRF7 and VP2 proteins. Alternatively, relative intensities of IRF7 and VP2 were normalized to β-actin. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. **p < 0.01.

Techniques Used: Expressing, Control, Infection, Western Blot, Standard Deviation

Interaction between IBDV VP3 and IRF7. (A) After co-transfecting DF-1 cells with Flag-VP3 and His-IRF7, we harvested samples 48 hours later. Cells were lysed and immunoprecipitation was performed using Flag-tag antibodies, followed by Western blot detection. (B) DF-1 cells transfected with p3×FLAG-CMV-14-VP3 and pcDNA3.1-His-IRF7 were subjected to immunofluorescence staining with anti-FLAG rabbit mAb and anti-His mouse mAb.

Figure Legend Snippet: Interaction between IBDV VP3 and IRF7. (A) After co-transfecting DF-1 cells with Flag-VP3 and His-IRF7, we harvested samples 48 hours later. Cells were lysed and immunoprecipitation was performed using Flag-tag antibodies, followed by Western blot detection. (B) DF-1 cells transfected with p3×FLAG-CMV-14-VP3 and pcDNA3.1-His-IRF7 were subjected to immunofluorescence staining with anti-FLAG rabbit mAb and anti-His mouse mAb.

Techniques Used: Immunoprecipitation, FLAG-tag, Western Blot, Transfection, Immunofluorescence, Staining

Overexpression of IBDV VP3 inhibits IRF7 expression. (A) DF-1 cells were transfected with the p3×FLAG-CMV14-VP3 plasmid for 6 hours and then stimulated with polyI:C. RT-qPCR was used to detect the gene expression levels of IRF7 and IFN-β at various time points post-infection. (B) DF-1 cells were transfected with the p3×FLAG-CMV14-VP3 plasmid for 6 hours and then stimulated with polyI:C for 24 h Western blot analysis was performed to detect the protein expression levels of IRF7 and Flag-VP3. Alternatively, relative intensities of IRF7 were normalized to β-actin. Three independent experiments were performed, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p<0.05; **p<0.01.

Figure Legend Snippet: Overexpression of IBDV VP3 inhibits IRF7 expression. (A) DF-1 cells were transfected with the p3×FLAG-CMV14-VP3 plasmid for 6 hours and then stimulated with polyI:C. RT-qPCR was used to detect the gene expression levels of IRF7 and IFN-β at various time points post-infection. (B) DF-1 cells were transfected with the p3×FLAG-CMV14-VP3 plasmid for 6 hours and then stimulated with polyI:C for 24 h Western blot analysis was performed to detect the protein expression levels of IRF7 and Flag-VP3. Alternatively, relative intensities of IRF7 were normalized to β-actin. Three independent experiments were performed, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p<0.05; **p<0.01.

Techniques Used: Over Expression, Expressing, Transfection, Plasmid Preparation, Quantitative RT-PCR, Infection, Western Blot, Standard Deviation

IBDV VP3 promote IRF7 degradation through the proteasome pathway. After transfecting DF-1 cells with the p3×FLAG-CMV14-VP3 plasmid for 6 hours, cells were treated with inhibitor: PYR-41, Wortmannin, or MG132, respectively. Samples were collected 24 h after polyI:C treatment and the IRF7 and VP2 protein levels were analyzed using Western blot. Alternatively, relative intensities of IRF7 were normalized to β-actin. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. **p < 0.01.

Figure Legend Snippet: IBDV VP3 promote IRF7 degradation through the proteasome pathway. After transfecting DF-1 cells with the p3×FLAG-CMV14-VP3 plasmid for 6 hours, cells were treated with inhibitor: PYR-41, Wortmannin, or MG132, respectively. Samples were collected 24 h after polyI:C treatment and the IRF7 and VP2 protein levels were analyzed using Western blot. Alternatively, relative intensities of IRF7 were normalized to β-actin. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. **p < 0.01.

Techniques Used: Plasmid Preparation, Western Blot, Standard Deviation

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Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Infectious bursal disease virus affecting interferon regulatory factor 7 signaling through VP3 protein to facilitate viral replication

doi: 10.3389/fcimb.2024.1529159

Figure Lengend Snippet: List of primers used in RT-qPCR.

Article Snippet: Other antibodies used in our study were anti-IRF7 rabbit polyclonal antibody (pAb) (bs-2994R, BIOSS, China), anti-FLAG mouse mAb (CW0287, CWBIO, China), anti-β-actin mouse mAb (CW0096M, CWBIO, China), anti-His mouse mAb (M20001M, Abmart, China), AbBox Fluor 594-labeled goat anti-rabbit IgG (BD9279, Biodragon, China), FITC-labeled goat anti-mouse IgG (BF05001, Biodragon, China), goat anti-rabbit IgG H&L antibody (CW0103S, CWBIO, China), goat anti-mouse IgG H&L antibody (CW0102S, CWBIO, China).

Techniques: Sequencing

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Infectious bursal disease virus affecting interferon regulatory factor 7 signaling through VP3 protein to facilitate viral replication

doi: 10.3389/fcimb.2024.1529159

Figure Lengend Snippet: IBDV infection can suppress the expression of IRF7. IBDV viral load, relative expression levels of the IRF7 and IFN-β gene (detected by RT-qPCR) in DF-1 cells infected with 1 MOI vvIBDV NN1172 (A) or attenuated IBDV B87 (B) at different time points. (C) IBDV viral load, relative expression levels of the IRF7 and IFN-β gene in DF-1 cells infected with 0.5, 1, or 1.5 MOI vvIBDV at different time points. (D-F) The IRF7 and VP2 protein levels in DF-1 cells (detected by western blot) infected with 0.5, 1, 1.5 MOI vvIBDV at different time point. (G) The protein levels of IFN-β at different time points after varying titers of IBDV infection. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p < 0.05; **p < 0.01.

Techniques: Infection, Expressing, Quantitative RT-PCR, Western Blot, Standard Deviation

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Infectious bursal disease virus affecting interferon regulatory factor 7 signaling through VP3 protein to facilitate viral replication

doi: 10.3389/fcimb.2024.1529159

Figure Lengend Snippet: Overexpression of IRF7 inhibits IBDV replication. (A) After transfecting DF-1 cells with the pcDNA3.1-His-IRF7 plasmid for 6 hours, cells were infected with 1 MOI vvIBDV. Samples were collected at various time points, and western blot was used to measure the expression levels of IRF7 and IBDV VP2 proteins. Alternatively, relative intensities of VP2 were normalized to β-actin. (B) RT-qPCR was employed to measure the IBDV viral load at various time points. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p < 0.05; **p < 0.01.

Techniques: Over Expression, Plasmid Preparation, Infection, Western Blot, Expressing, Quantitative RT-PCR, Standard Deviation

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Infectious bursal disease virus affecting interferon regulatory factor 7 signaling through VP3 protein to facilitate viral replication

doi: 10.3389/fcimb.2024.1529159

Figure Lengend Snippet: Knocking down IRF7 promotes IBDV replication. (A) DF-1 cells were transfected with siRNA targeting IRF7 for 6 hours, followed by infection with 1 MOI vvIBDV. Samples were collected at various time points, and western blot was used to measure the expression levels of IRF7 and IBDV VP2 proteins. Alternatively, relative intensities of IRF7 and VP2 were normalized to β-actin, respectively. (B) RT-qPCR was employed to measure the IBDV viral load at various time points. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p < 0.05; **p < 0.01.

Techniques: Transfection, Infection, Western Blot, Expressing, Quantitative RT-PCR, Standard Deviation

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Infectious bursal disease virus affecting interferon regulatory factor 7 signaling through VP3 protein to facilitate viral replication

doi: 10.3389/fcimb.2024.1529159

Figure Lengend Snippet: Overexpression of IRF7 couldn’t inhibit IRF7 degradation in vvIBDV-infected cells. (A) DF-1 cells were transfected with pcDNA3.1-His-IRF7 and infected with 1 MOI vvIBDV. Samples were collected at 6, 9, 12, 18, and 24 hpi, and the expression of IRF7 protein was detected using western blot. Alternatively, relative intensities of IRF7 were normalized to β-actin. (B) DF-1 cells were transfected with pcDNA3.1-His-IRF7 and infected with 1 MOI attenuated IBDV. Samples were collected at 12, 18, 24, and 36 hpi, and the expression of IRF7 protein was detected using western blot. Alternatively, relative intensities of IRF7 were normalized to β-actin. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. **p < 0.01.

Techniques: Over Expression, Infection, Transfection, Expressing, Western Blot, Standard Deviation

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Infectious bursal disease virus affecting interferon regulatory factor 7 signaling through VP3 protein to facilitate viral replication

doi: 10.3389/fcimb.2024.1529159

Figure Lengend Snippet: IBDV affects the expression of IRF7 through the proteasomal pathway. In the control group, cells were treated with DMSO, while in the experimental group, cells were treated with different inhibitors (PYR-41, Wortmannin, MG132) after being infected with vvIBDV. Samples were then collected for western blot analysis to measure the expression levels of IRF7 and VP2 proteins. Alternatively, relative intensities of IRF7 and VP2 were normalized to β-actin. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. **p < 0.01.

Techniques: Expressing, Control, Infection, Western Blot, Standard Deviation

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Infectious bursal disease virus affecting interferon regulatory factor 7 signaling through VP3 protein to facilitate viral replication

doi: 10.3389/fcimb.2024.1529159

Figure Lengend Snippet: Interaction between IBDV VP3 and IRF7. (A) After co-transfecting DF-1 cells with Flag-VP3 and His-IRF7, we harvested samples 48 hours later. Cells were lysed and immunoprecipitation was performed using Flag-tag antibodies, followed by Western blot detection. (B) DF-1 cells transfected with p3×FLAG-CMV-14-VP3 and pcDNA3.1-His-IRF7 were subjected to immunofluorescence staining with anti-FLAG rabbit mAb and anti-His mouse mAb.

Techniques: Immunoprecipitation, FLAG-tag, Western Blot, Transfection, Immunofluorescence, Staining

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Infectious bursal disease virus affecting interferon regulatory factor 7 signaling through VP3 protein to facilitate viral replication

doi: 10.3389/fcimb.2024.1529159

Figure Lengend Snippet: Overexpression of IBDV VP3 inhibits IRF7 expression. (A) DF-1 cells were transfected with the p3×FLAG-CMV14-VP3 plasmid for 6 hours and then stimulated with polyI:C. RT-qPCR was used to detect the gene expression levels of IRF7 and IFN-β at various time points post-infection. (B) DF-1 cells were transfected with the p3×FLAG-CMV14-VP3 plasmid for 6 hours and then stimulated with polyI:C for 24 h Western blot analysis was performed to detect the protein expression levels of IRF7 and Flag-VP3. Alternatively, relative intensities of IRF7 were normalized to β-actin. Three independent experiments were performed, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. *p<0.05; **p<0.01.

Techniques: Over Expression, Expressing, Transfection, Plasmid Preparation, Quantitative RT-PCR, Infection, Western Blot, Standard Deviation

Journal: Frontiers in Cellular and Infection Microbiology

Article Title: Infectious bursal disease virus affecting interferon regulatory factor 7 signaling through VP3 protein to facilitate viral replication

doi: 10.3389/fcimb.2024.1529159

Figure Lengend Snippet: IBDV VP3 promote IRF7 degradation through the proteasome pathway. After transfecting DF-1 cells with the p3×FLAG-CMV14-VP3 plasmid for 6 hours, cells were treated with inhibitor: PYR-41, Wortmannin, or MG132, respectively. Samples were collected 24 h after polyI:C treatment and the IRF7 and VP2 protein levels were analyzed using Western blot. Alternatively, relative intensities of IRF7 were normalized to β-actin. Three independent experiments were conducted, and the data are presented as the mean ± standard deviation of three replicates from a representative experiment. **p < 0.01.

Techniques: Plasmid Preparation, Western Blot, Standard Deviation

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