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Cell Signaling Technology Inc p stat2
P Stat2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 186 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/p+stat2+tyr690/Phospho-Stat2+(Tyr690)+Rabbit+mAb/pmc13039202-279-60-80
Average 96 stars, based on 186 article reviews

p stat2 - by Bioz Stars, 2026-08

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Identification of physalin F as an inhibitor of SeV-induced innate immune signaling. ( A ) Compounds of a natural small molecule library ( n = 903) were sub-pooled into 4 compounds/sub-pool. HEK293T cells (5 × 10 4 ) stably transduced with an ISRE luciferase reporter were treated with each of the sub-pools (5 μM for each compound) for 0.5 h, followed by infection with SeV for 8 h before luciferase assays (left dot plot, the dashed line indicates inhibition of SeV-induced ISRE activation by 50%). Forty-eight individual compounds from the 12 positive sub-pools (inhibition rate > 50%) were then tested for their effects on SeV-induced ISRE activation by reporter assays (middle dot plots, the dashed line indicates inhibition of SeV-induced ISRE activation by >98%). The arrows indicate the workflow. The candidate compound physalin F was further tested for its dose-dependent effects on SeV-induced ISRE activation by reporter assay. The IC 50 value was calculated from the dose–response curve. IC 50 = 1.0 μM, (95% CI: 0.8 to 1.1 μM). ( B ) Effects of physalin F on transcription of downstream genes induced by SeV in HEK293T and THP1 cells. HEK293T or THP 1 cells (1 × 10 6 ) were treated with physalin F (0, 2.5, 5 μM) for 0.5 h and then infected with SeV for the indicated times before RT-qPCR analysis of mRNA levels of the indicated effector genes. GAPDH mRNA level was used as the internal control. ( C ) Effects of physalin F treatment on SeV-induced phosphorylation of TBK1, IRF3, STAT1, and STAT2. HEK293T or THP1 cells (1 × 10 6 ) were treated with the indicated concentrations of physalin F for 0.5 h and then infected with SeV for the indicated times. Immunoblotting analysis was performed with the indicated antibodies. The relative band intensities, which are normalized to the corresponding β-actin bands, are quantitated by densitometry analysis using ImageJ (1.53c) software and shown under the blots. Original Western blot images can be found in . ( D ) Effects of physalin F on IFN-γ induced transcription of the IRF1 gene in HEK293T cells. HEK293T cells (1 × 10 6 ) were treated with physalin F (0, 5 μM) for 0.5 h and then with IFN-γ for 6 h before RT-qPCR analysis of mRNA levels of the indicated antiviral genes. GAPDH mRNA level was used as the internal control. ( E ) Effects of physalin F on IFN-γ induced phosphorylation of STAT1. HEK293T (1 × 10 6 ) were treated with physalin F (0, 2.5, 5 μM) for 0.5 h and then with IFN-γ for 6 h. Immunoblotting analysis was performed with the indicated antibodies. Original Western blot images can be found in . Data shown in ( A ) (dose experiment), ( B , D ) are mean ± SD; n = 3 technical replicates. ns, not significant, * p < 0.05; ** p < 0.01. Experiments in ( B – E ) were repeated at least two times with similar results.

Journal: Pathogens

Article Title: Physalin F Promotes AFG3L2-Mediated Degradation of VISA/MAVS to Suppress Innate Immune Response to RNA Virus

doi: 10.3390/pathogens15010074

Figure Lengend Snippet: Identification of physalin F as an inhibitor of SeV-induced innate immune signaling. ( A ) Compounds of a natural small molecule library ( n = 903) were sub-pooled into 4 compounds/sub-pool. HEK293T cells (5 × 10 4 ) stably transduced with an ISRE luciferase reporter were treated with each of the sub-pools (5 μM for each compound) for 0.5 h, followed by infection with SeV for 8 h before luciferase assays (left dot plot, the dashed line indicates inhibition of SeV-induced ISRE activation by 50%). Forty-eight individual compounds from the 12 positive sub-pools (inhibition rate > 50%) were then tested for their effects on SeV-induced ISRE activation by reporter assays (middle dot plots, the dashed line indicates inhibition of SeV-induced ISRE activation by >98%). The arrows indicate the workflow. The candidate compound physalin F was further tested for its dose-dependent effects on SeV-induced ISRE activation by reporter assay. The IC 50 value was calculated from the dose–response curve. IC 50 = 1.0 μM, (95% CI: 0.8 to 1.1 μM). ( B ) Effects of physalin F on transcription of downstream genes induced by SeV in HEK293T and THP1 cells. HEK293T or THP 1 cells (1 × 10 6 ) were treated with physalin F (0, 2.5, 5 μM) for 0.5 h and then infected with SeV for the indicated times before RT-qPCR analysis of mRNA levels of the indicated effector genes. GAPDH mRNA level was used as the internal control. ( C ) Effects of physalin F treatment on SeV-induced phosphorylation of TBK1, IRF3, STAT1, and STAT2. HEK293T or THP1 cells (1 × 10 6 ) were treated with the indicated concentrations of physalin F for 0.5 h and then infected with SeV for the indicated times. Immunoblotting analysis was performed with the indicated antibodies. The relative band intensities, which are normalized to the corresponding β-actin bands, are quantitated by densitometry analysis using ImageJ (1.53c) software and shown under the blots. Original Western blot images can be found in . ( D ) Effects of physalin F on IFN-γ induced transcription of the IRF1 gene in HEK293T cells. HEK293T cells (1 × 10 6 ) were treated with physalin F (0, 5 μM) for 0.5 h and then with IFN-γ for 6 h before RT-qPCR analysis of mRNA levels of the indicated antiviral genes. GAPDH mRNA level was used as the internal control. ( E ) Effects of physalin F on IFN-γ induced phosphorylation of STAT1. HEK293T (1 × 10 6 ) were treated with physalin F (0, 2.5, 5 μM) for 0.5 h and then with IFN-γ for 6 h. Immunoblotting analysis was performed with the indicated antibodies. Original Western blot images can be found in . Data shown in ( A ) (dose experiment), ( B , D ) are mean ± SD; n = 3 technical replicates. ns, not significant, * p < 0.05; ** p < 0.01. Experiments in ( B – E ) were repeated at least two times with similar results.

Article Snippet: Physalin F (TargetMol, Wellesley Hills, MA, USA, T8716); Dual-Specific Luciferase Assay Kit (Promega, Madison, WI, USA, E2490); puromycin (Thermo Fisher Scientific, Waltham, MA, USA); M-MLV reverse transcriptase (Invitrogen, Carlsbad, CA, USA, 28025-013); SYBR (Bio-Rad laboratories, Hercules, CA, USA); RiboLock RNase inhibitor, pyrophosphatase (Thermo Fisher Scientific, Waltham, MA, USA); protease inhibitor cocktail (Roche, Basel, Switzerland); polybrene (Millipore, Burlington, MA, USA); ClarityTM Western ECL Substrate (Bio-Rad, Hercules, CA, USA); ELISA kits for murine IFN-β (PBL Assay Science, Piscataway, NJ, USA, 42400), murine IL-6 (BioLegend, San Diego, CA, USA, 431304); mouse antibodies against HA (OriGene, Rockville, MD, USA, TA180128) and FLAG (Sigma-Aldrich, Burlington, MA, USA, F3165); mouse antibodies against β-Tubulin (ABclonal, Woburn, MA, USA, A12289); rabbit antibodies against FLAG (14793), Rig-I (3743), β-actin (5125), p-IRF3 S396 (4947), STAT1 (14994), p-STAT1 Y701 (9167) STAT2 (72604), and p-STAT2 Y690 (88410) (Cell Signaling Technology, Danvers, MA, USA); rabbit antibodies against TBK1 (ab40676), p-TBK1 S172 (ab109272), and p-IRF3 S386 (ab76493) (Abcam, Cambridge, UK); rabbit antibodies against AFG3L2 (14631-1-AP), TOM40 (18409-1-AP), TOM70 (14528-1-AP) (Proteintech, Rosemont, IL, USA), VISA (Bethyl Laboratories, Montgomery, TX, USA, A300-782A), and GFP (GeneTex, Irvine, CA, USA, GTX113617); and HRP-conjugated anti-FLAG monoclonal antibody (Sigma-Aldrich, A8592) were purchased from the indicated companies.

Techniques: Stable Transfection, Transduction, Luciferase, Infection, Inhibition, Activation Assay, Reporter Assay, Quantitative RT-PCR, Control, Phospho-proteomics, Western Blot, Software

FMDV 3D protein interacts with STAT2. (A) HEK-293T cells were co-transfected with Flag-3D and various Myc-tagged innate immune molecule-expressing plasmids (JAK1, TYK2, STAT1, STAT2, or IRF9). At 36 hpt, the cell lysates were subjected to Co-IP assay analysis. Immunoprecipitated proteins and whole-cell lysates (WCL) were analyzed by western blotting using specified antibodies. ( B) HEK-293T cells were co-transfected with Myc-STAT2 and either an empty vector or Flag-3D expressing plasmids for 36 h. Cell lysates were immunoprecipitated with anti-Myc or control IgG antibodies and analyzed by western blotting. ( C) HEK-293T cells were co-transfected with Flag-3D along with Vec or Myc-STAT2. At 36 hpt, cell lysates were subjected to Co-IP assay. Immunoprecipitated proteins and WCL were analyzed by western blotting. (D) PK-15 cells were transfected with Flag-3D or empty vector plasmids. At 36 hpt, cell lysates were immunoprecipitated with anti-Flag antibodies and analyzed by western blotting. (E) PK-15 cells were mock-infected or infected with FMDV for 12 h, cell lysates were immunoprecipitated with anti-3D antibodies and analyzed by western blotting with the indicated antibodies. (F) PK-15 cells were transfected with porcine HA-STAT2 expressing plasmids for 24 h, then mock-infected or infected with FMDV (MOI = 0.1) for 10 h. Colocalization of HA-STAT2 (red) and FMDV 3D (green) was assessed by immunofluorescence assay (IFA). Nuclei were counterstained with DAPI (blue).

Journal: Virus Research

Article Title: Foot-and-mouth disease virus 3D polymerase antagonizes the interferon signaling pathway by blocking STAT2 nuclear translocation

doi: 10.1016/j.virusres.2025.199671

Figure Lengend Snippet: FMDV 3D protein interacts with STAT2. (A) HEK-293T cells were co-transfected with Flag-3D and various Myc-tagged innate immune molecule-expressing plasmids (JAK1, TYK2, STAT1, STAT2, or IRF9). At 36 hpt, the cell lysates were subjected to Co-IP assay analysis. Immunoprecipitated proteins and whole-cell lysates (WCL) were analyzed by western blotting using specified antibodies. ( B) HEK-293T cells were co-transfected with Myc-STAT2 and either an empty vector or Flag-3D expressing plasmids for 36 h. Cell lysates were immunoprecipitated with anti-Myc or control IgG antibodies and analyzed by western blotting. ( C) HEK-293T cells were co-transfected with Flag-3D along with Vec or Myc-STAT2. At 36 hpt, cell lysates were subjected to Co-IP assay. Immunoprecipitated proteins and WCL were analyzed by western blotting. (D) PK-15 cells were transfected with Flag-3D or empty vector plasmids. At 36 hpt, cell lysates were immunoprecipitated with anti-Flag antibodies and analyzed by western blotting. (E) PK-15 cells were mock-infected or infected with FMDV for 12 h, cell lysates were immunoprecipitated with anti-3D antibodies and analyzed by western blotting with the indicated antibodies. (F) PK-15 cells were transfected with porcine HA-STAT2 expressing plasmids for 24 h, then mock-infected or infected with FMDV (MOI = 0.1) for 10 h. Colocalization of HA-STAT2 (red) and FMDV 3D (green) was assessed by immunofluorescence assay (IFA). Nuclei were counterstained with DAPI (blue).

Article Snippet: The commercial antibodies used in this study include: anti-Flag mouse Ab (Sigma, F1804), anti-Myc mouse Ab (Sigma, M5546), anti-HA mouse Ab (Sigma, H9658), and anti-GAPDH mouse Ab (Abclonal, AC002), anti-JAK1 rabbit Ab (Cell Signaling Technology, 3332), anti-TYK2 rabbit Ab (Cell Signaling Technology, 9312), anti-STAT1 rabbit Ab (Cell Signaling Technology, 9172), anti-STAT2 rabbit Ab (Cell Signaling Technology, 4594), anti-p-STAT2 rabbit Ab (Cell Signaling Technology, 4441), anti-IRF9 rabbit Ab (Cell Signaling Technology, 76,684).

Techniques: Transfection, Expressing, Co-Immunoprecipitation Assay, Immunoprecipitation, Western Blot, Plasmid Preparation, Control, Infection, Immunofluorescence

FMDV 3D protein does not alter the protein level of STAT2. (A) PK-15 cells were transfected with empty vector or Flag-3D expressing plasmids. At 24 hpt, cell lysates were analyzed by western blotting with specified antibodies. (B) PK-15 cells were transfected with 0, 0.25, 0.5 or 1 μg of Flag-3D expressing plasmids for 24 h. Endogenous STAT2 protein expression levels were detected by western blotting. (C) PK-15 cells were transfected with an increasing amount of Flag-3D expressing plasmids (0, 0.25, 0.5 or 1 μg) for 24 h. Total RNA was extracted, and STAT2 mRNA levels were quantified by qPCR. (D) PK-15 cells mock-infected or infected with FMDV (MOI=0.1) for 6 and 12 h, followed by IFN-β (1000 U/mL) or mock treatment for 30 min. The expression and phosphorylation levels of STAT2 were detected by western blotting.

Journal: Virus Research

Article Title: Foot-and-mouth disease virus 3D polymerase antagonizes the interferon signaling pathway by blocking STAT2 nuclear translocation

doi: 10.1016/j.virusres.2025.199671

Figure Lengend Snippet: FMDV 3D protein does not alter the protein level of STAT2. (A) PK-15 cells were transfected with empty vector or Flag-3D expressing plasmids. At 24 hpt, cell lysates were analyzed by western blotting with specified antibodies. (B) PK-15 cells were transfected with 0, 0.25, 0.5 or 1 μg of Flag-3D expressing plasmids for 24 h. Endogenous STAT2 protein expression levels were detected by western blotting. (C) PK-15 cells were transfected with an increasing amount of Flag-3D expressing plasmids (0, 0.25, 0.5 or 1 μg) for 24 h. Total RNA was extracted, and STAT2 mRNA levels were quantified by qPCR. (D) PK-15 cells mock-infected or infected with FMDV (MOI=0.1) for 6 and 12 h, followed by IFN-β (1000 U/mL) or mock treatment for 30 min. The expression and phosphorylation levels of STAT2 were detected by western blotting.

Techniques: Transfection, Plasmid Preparation, Expressing, Western Blot, Infection, Phospho-proteomics

FMDV 3D protein suppresses phosphorylation and nuclear translocation of STAT2. (A) PK-15 cells were transfected with either an empty vector or Flag-3D expressing plasmids. At 24 hpt, cells were treated with IFN-β (1000 U/mL) or solvent control for 30 min. Cell lysates were analyzed by western blotting with specified antibodies. (B) PK-15 cells were transfected with increasing amounts of Flag-3D expressing plasmids (0, 0.25, 0.5, or 1 μg). At 24 hpt, cells were treated with IFN-β (1000 U/mL) for 30 min. Cell lysates were analyzed by western blotting with indicated antibodies. (C) HEK-293T cells were co-transfected with Myc-STAT2 and HA-STAT1 or HA-vector, along with increasing amounts Flag-3D expressing plasmids. At 36 hpt, the cells were treated with IFN-β (1000 U/mL) for 30 min. The cell lysates were immunoprecipitated with anti-Myc antibodies. The immunoprecipitated proteins and WCL were analyzed by western blotting using the specified antibodies. (D) PK-15 cells mock-infected or infected with FMDV (MOI=0.1) for 10 h, followed by IFN-β (1000 U/mL) or mock treatment for 30 min. The subcellular localization of STAT2 and FMDV 3D was assessed by IFA. Nuclei were stained with DAPI (blue), and fluorescence was visualized for 3D (green) and STAT2 (red). (E) PK-15 cells were transfected with an increasing amounts Flag-3D expressing plasmids for 24 h, the cell lysates were analyzed by western blotting using the specified antibodies. (F) PK-15 cells were transfected with Flag-3D expressing plasmids for 24 h, then mock-infected or infected with FMDV (MOI=0.1) for 12 h. Cell lysates were analyzed by western blotting with indicated antibodies.

Journal: Virus Research

Article Title: Foot-and-mouth disease virus 3D polymerase antagonizes the interferon signaling pathway by blocking STAT2 nuclear translocation

doi: 10.1016/j.virusres.2025.199671

Figure Lengend Snippet: FMDV 3D protein suppresses phosphorylation and nuclear translocation of STAT2. (A) PK-15 cells were transfected with either an empty vector or Flag-3D expressing plasmids. At 24 hpt, cells were treated with IFN-β (1000 U/mL) or solvent control for 30 min. Cell lysates were analyzed by western blotting with specified antibodies. (B) PK-15 cells were transfected with increasing amounts of Flag-3D expressing plasmids (0, 0.25, 0.5, or 1 μg). At 24 hpt, cells were treated with IFN-β (1000 U/mL) for 30 min. Cell lysates were analyzed by western blotting with indicated antibodies. (C) HEK-293T cells were co-transfected with Myc-STAT2 and HA-STAT1 or HA-vector, along with increasing amounts Flag-3D expressing plasmids. At 36 hpt, the cells were treated with IFN-β (1000 U/mL) for 30 min. The cell lysates were immunoprecipitated with anti-Myc antibodies. The immunoprecipitated proteins and WCL were analyzed by western blotting using the specified antibodies. (D) PK-15 cells mock-infected or infected with FMDV (MOI=0.1) for 10 h, followed by IFN-β (1000 U/mL) or mock treatment for 30 min. The subcellular localization of STAT2 and FMDV 3D was assessed by IFA. Nuclei were stained with DAPI (blue), and fluorescence was visualized for 3D (green) and STAT2 (red). (E) PK-15 cells were transfected with an increasing amounts Flag-3D expressing plasmids for 24 h, the cell lysates were analyzed by western blotting using the specified antibodies. (F) PK-15 cells were transfected with Flag-3D expressing plasmids for 24 h, then mock-infected or infected with FMDV (MOI=0.1) for 12 h. Cell lysates were analyzed by western blotting with indicated antibodies.

Techniques: Phospho-proteomics, Translocation Assay, Transfection, Plasmid Preparation, Expressing, Solvent, Control, Western Blot, Immunoprecipitation, Infection, Staining, Fluorescence

Prediction the key interaction residues between STAT2 and FMDV-3D The interaction model between STAT2 and FMDV-3D was constructed using the ZDOCK online service. Predicted salt bridge interactions, Pi-Alkyl interaction of STAT2 phosphorylation residue Y690 with 3D P23, and key residues STAT2 R687, E686, N683, H693 and 3D E33, R174, R174, G28 were highlighted using PyMOL software.

Journal: Virus Research

Article Title: Foot-and-mouth disease virus 3D polymerase antagonizes the interferon signaling pathway by blocking STAT2 nuclear translocation

doi: 10.1016/j.virusres.2025.199671

Figure Lengend Snippet: Prediction the key interaction residues between STAT2 and FMDV-3D The interaction model between STAT2 and FMDV-3D was constructed using the ZDOCK online service. Predicted salt bridge interactions, Pi-Alkyl interaction of STAT2 phosphorylation residue Y690 with 3D P23, and key residues STAT2 R687, E686, N683, H693 and 3D E33, R174, R174, G28 were highlighted using PyMOL software.

Techniques: Construct, Phospho-proteomics, Residue, Software

Mechanisms by which FMDV 3D protein targets STAT2 to impede the activation of the JAK-STAT signaling pathway. Upon FMDV infection of host cells, the viral 3D protein interacts with STAT2, hinders the phosphorylation and inhibits the nuclear translocation of STAT2, thereby blocks the activation of the JAK-STAT signaling pathway and suppresses host antiviral response.

Journal: Virus Research

Article Title: Foot-and-mouth disease virus 3D polymerase antagonizes the interferon signaling pathway by blocking STAT2 nuclear translocation

doi: 10.1016/j.virusres.2025.199671

Figure Lengend Snippet: Mechanisms by which FMDV 3D protein targets STAT2 to impede the activation of the JAK-STAT signaling pathway. Upon FMDV infection of host cells, the viral 3D protein interacts with STAT2, hinders the phosphorylation and inhibits the nuclear translocation of STAT2, thereby blocks the activation of the JAK-STAT signaling pathway and suppresses host antiviral response.

Techniques: Activation Assay, Infection, Phospho-proteomics, Translocation Assay

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