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α py stat1 (Cell Signaling Technology Inc)

Name: α py stat1
Brand: Cell Signaling Technology Inc
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Cell Signaling Technology Inc α py stat1

( A ) Publicly available chromatin immunoprecipitation sequencing (ChIP-Seq) data for <t>STAT1</t> (GSM994528), STAT4 (GSM550303), and T-bet (GSM836124) were examined at Cxcr3 . Sequencing tracks were viewed using the Integrative Genomics Viewer (IGV). Regulatory regions of interest with transcription factor enrichment are indicated by the blue boxes. ( B ) Published RNA-Seq data (GSE203065) from in vitro–generated WT and Ikzf3 –/– Th1 cells were analyzed for DEGs. A heatmap of DEGs associated with IFN-γ/STAT1 and IL-12/STAT4 signaling in Th1 cells is shown, as well as additional genes involved in both pathways and Th cell differentiation. Gene names color-coded in blue are downregulated in Ikzf3 –/– Th1 cells. Note: Cxcr3 transcript data presented here are the same as in . ( C ) Schematic of proposed model in which Aiolos may regulate CXCR3 via impacts on components of the IFN-γ/STAT1 and IL-12/STAT4 cytokine signaling pathways. The downward arrows in blue indicate genes that are downregulated in the absence of Aiolos.

α Py Stat1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1536 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 98 stars, based on 1536 article reviews

α py stat1 - by Bioz Stars, 2026-02

98/100 stars

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1) Product Images from "Aiolos promotes CXCR3 expression on Th1 cells via positive regulation of IFN- γ /STAT1 signaling"

Article Title: Aiolos promotes CXCR3 expression on Th1 cells via positive regulation of IFN- γ /STAT1 signaling

Journal: JCI Insight

doi: 10.1172/jci.insight.180287

( A ) Publicly available chromatin immunoprecipitation sequencing (ChIP-Seq) data for STAT1 (GSM994528), STAT4 (GSM550303), and T-bet (GSM836124) were examined at Cxcr3 . Sequencing tracks were viewed using the Integrative Genomics Viewer (IGV). Regulatory regions of interest with transcription factor enrichment are indicated by the blue boxes. ( B ) Published RNA-Seq data (GSE203065) from in vitro–generated WT and Ikzf3 –/– Th1 cells were analyzed for DEGs. A heatmap of DEGs associated with IFN-γ/STAT1 and IL-12/STAT4 signaling in Th1 cells is shown, as well as additional genes involved in both pathways and Th cell differentiation. Gene names color-coded in blue are downregulated in Ikzf3 –/– Th1 cells. Note: Cxcr3 transcript data presented here are the same as in . ( C ) Schematic of proposed model in which Aiolos may regulate CXCR3 via impacts on components of the IFN-γ/STAT1 and IL-12/STAT4 cytokine signaling pathways. The downward arrows in blue indicate genes that are downregulated in the absence of Aiolos.

Figure Legend Snippet: ( A ) Publicly available chromatin immunoprecipitation sequencing (ChIP-Seq) data for STAT1 (GSM994528), STAT4 (GSM550303), and T-bet (GSM836124) were examined at Cxcr3 . Sequencing tracks were viewed using the Integrative Genomics Viewer (IGV). Regulatory regions of interest with transcription factor enrichment are indicated by the blue boxes. ( B ) Published RNA-Seq data (GSE203065) from in vitro–generated WT and Ikzf3 –/– Th1 cells were analyzed for DEGs. A heatmap of DEGs associated with IFN-γ/STAT1 and IL-12/STAT4 signaling in Th1 cells is shown, as well as additional genes involved in both pathways and Th cell differentiation. Gene names color-coded in blue are downregulated in Ikzf3 –/– Th1 cells. Note: Cxcr3 transcript data presented here are the same as in . ( C ) Schematic of proposed model in which Aiolos may regulate CXCR3 via impacts on components of the IFN-γ/STAT1 and IL-12/STAT4 cytokine signaling pathways. The downward arrows in blue indicate genes that are downregulated in the absence of Aiolos.

Techniques Used: ChIP-sequencing, Sequencing, RNA Sequencing, In Vitro, Generated, Cell Differentiation, Protein-Protein interactions

( A ) Schematic of culturing system. Naive CD4 + T cells were stimulated with α-CD3/CD28 and cultured under Th1-polarizing conditions (IL-12, α–IL-4). On day 3, cells were removed from stimulation and given IFN-γ, α–IL-4, and IL-2 for an additional 2 days. ( B ) At day 5, transcript analysis was performed via qRT-PCR. Transcript was normalized to Rps18 and presented as fold-change compared with WT control ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; ** P < 0.01, *** P < 0.001, **** P < 0.0001, 2-tailed unpaired Student’s t test). ( C ) Representative flow cytometric analysis for CXCR3 on IFN-γ–treated Th1 cells at day 5. Data are displayed as MFI fold-change compared with WT controls ( n = 3 biological replicates from 3 independent experiments, mean ± SEM; ** P < 0.01, 2-tailed unpaired Student’s t test). ( D ) An immunoblot was performed to assess the relative abundance of the indicated proteins. β-Actin serves as a loading control ( n = 4 independent experiments, mean ± SEM; * P < 0.05, *** P < 0.001, 2-tailed unpaired Student’s t test). ( E ) ChIP assays were performed to assess STAT1 association with Cxcr3 in WT and Ikzf3 –/– Th1 cells. Publicly available ChIP-Seq data for STAT1 (GSM994528) were examined to identify potential regions of STAT1 enrichment. Sequencing tracks were viewed using IGV, and regulatory regions of interest are indicated by blue boxes. Approximate ChIP primer locations at the Cxcr3 promoter (prom.) and 3′ enhancer (enhc.) are indicated with gray arrows. ( F ) The indicated regions were analyzed for STAT1 enrichment. Data were normalized to total input. Percentage enrichment relative to input was divided by IgG, and data are presented as fold-change relative to IgG. ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; ** P < 0.01, *** P < 0.001, 1-way ANOVA with Tukey’s multiple comparisons test.)

Figure Legend Snippet: ( A ) Schematic of culturing system. Naive CD4 + T cells were stimulated with α-CD3/CD28 and cultured under Th1-polarizing conditions (IL-12, α–IL-4). On day 3, cells were removed from stimulation and given IFN-γ, α–IL-4, and IL-2 for an additional 2 days. ( B ) At day 5, transcript analysis was performed via qRT-PCR. Transcript was normalized to Rps18 and presented as fold-change compared with WT control ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; ** P < 0.01, *** P < 0.001, **** P < 0.0001, 2-tailed unpaired Student’s t test). ( C ) Representative flow cytometric analysis for CXCR3 on IFN-γ–treated Th1 cells at day 5. Data are displayed as MFI fold-change compared with WT controls ( n = 3 biological replicates from 3 independent experiments, mean ± SEM; ** P < 0.01, 2-tailed unpaired Student’s t test). ( D ) An immunoblot was performed to assess the relative abundance of the indicated proteins. β-Actin serves as a loading control ( n = 4 independent experiments, mean ± SEM; * P < 0.05, *** P < 0.001, 2-tailed unpaired Student’s t test). ( E ) ChIP assays were performed to assess STAT1 association with Cxcr3 in WT and Ikzf3 –/– Th1 cells. Publicly available ChIP-Seq data for STAT1 (GSM994528) were examined to identify potential regions of STAT1 enrichment. Sequencing tracks were viewed using IGV, and regulatory regions of interest are indicated by blue boxes. Approximate ChIP primer locations at the Cxcr3 promoter (prom.) and 3′ enhancer (enhc.) are indicated with gray arrows. ( F ) The indicated regions were analyzed for STAT1 enrichment. Data were normalized to total input. Percentage enrichment relative to input was divided by IgG, and data are presented as fold-change relative to IgG. ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; ** P < 0.01, *** P < 0.001, 1-way ANOVA with Tukey’s multiple comparisons test.)

Techniques Used: Cell Culture, Quantitative RT-PCR, Control, Western Blot, ChIP-sequencing, Sequencing

( A ) Schematic of culturing system. WT naive CD4 + T cells were stimulated with α-CD3/CD28 under Th1-polarizing conditions (IL-12, α–IL-4). Some cells were also treated with α–IFN-γ to inhibit IFN-γ/STAT1 signaling. ( B ) At day 3, transcript analysis was performed via qRT-PCR. Transcript was normalized to Rps18 and presented as fold-change compared with WT control ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; ** P < 0.01, **** P < 0.0001, 2-tailed unpaired Student’s t test). ( C ) Representative flow cytometric analysis at day 3 for CXCR3 expression on WT Th1 cells treated with or without α–IFN-γ. Data are displayed as percentage positive for CXCR3 ( n = 3 biological replicates from 3 independent experiments, mean ± SEM; * P < 0.05, 2-tailed unpaired Student’s t test). ( D ) An immunoblot was performed to assess the relative abundance of the indicated proteins. β-Actin serves as a loading control ( n = 4 independent experiments, mean ± SEM; * P < 0.05, ** P < 0.01, **** P < 0.0001, 2-tailed unpaired Student’s t test). ( E ) At day 3, transcript and flow cytometric analyses were performed for Ikzf3 and Aiolos protein expression, respectively. Flow cytometric data are displayed as MFI fold-change compared with WT controls ( n = 3 biological replicates from 3 independent experiments, mean ± SEM; ** P < 0.01, 2-tailed unpaired Student’s t test).

Figure Legend Snippet: ( A ) Schematic of culturing system. WT naive CD4 + T cells were stimulated with α-CD3/CD28 under Th1-polarizing conditions (IL-12, α–IL-4). Some cells were also treated with α–IFN-γ to inhibit IFN-γ/STAT1 signaling. ( B ) At day 3, transcript analysis was performed via qRT-PCR. Transcript was normalized to Rps18 and presented as fold-change compared with WT control ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; ** P < 0.01, **** P < 0.0001, 2-tailed unpaired Student’s t test). ( C ) Representative flow cytometric analysis at day 3 for CXCR3 expression on WT Th1 cells treated with or without α–IFN-γ. Data are displayed as percentage positive for CXCR3 ( n = 3 biological replicates from 3 independent experiments, mean ± SEM; * P < 0.05, 2-tailed unpaired Student’s t test). ( D ) An immunoblot was performed to assess the relative abundance of the indicated proteins. β-Actin serves as a loading control ( n = 4 independent experiments, mean ± SEM; * P < 0.05, ** P < 0.01, **** P < 0.0001, 2-tailed unpaired Student’s t test). ( E ) At day 3, transcript and flow cytometric analyses were performed for Ikzf3 and Aiolos protein expression, respectively. Flow cytometric data are displayed as MFI fold-change compared with WT controls ( n = 3 biological replicates from 3 independent experiments, mean ± SEM; ** P < 0.01, 2-tailed unpaired Student’s t test).

Techniques Used: Quantitative RT-PCR, Control, Expressing, Western Blot

( A ) Publicly available ATAC-Seq data (GSE203064) from WT and Ikzf3 –/– Th1 cells were assessed for alterations in chromatin accessibility at the Stat1 promoter. Publicly available ChIP-Seq data for Aiolos (GSM5106065) were examined at Stat1 . Sequencing tracks were viewed using IGV. The Stat1 promoter region of significant differential accessibility is indicated by a blue box ( P adj = 0.0302). A ~500 bp region encompassing the indicated Aiolos DNA binding motifs within the Stat1 promoter was subcloned into a reporter plasmid. ( B ) Schematic depicting the zinc finger (ZF) domains of WT Aiolos and a DNA-binding mutant (Aiolos DBM ). ( C ) EL4 T cells were transfected with a Stat1 promoter-reporter and WT Aiolos, Aiolos DBM , or empty vector control. Cells were also transfected with SV40- Renilla as a control for transduction efficiency. Luciferase promoter-reporter values were normalized to Renilla control and presented relative to the empty vector control. Aiolos was assessed via immunoblot with an antibody for the V5 epitope tag. β-Actin serves as a loading control. Data are representative of 3 independent experiments ( n = 3, mean ± SEM; * P < 0.05, 1-way ANOVA with Tukey’s multiple comparisons test). ( D ) Publicly available ATAC-Seq data (GSE203064) from Th1 cells and ChIP-Seq data for STAT1 (GSM994528) were viewed using IGV to identify regions of STAT1 enrichment (blue box) at Ikzf3 . Approximate ChIP primer locations are indicated with a gray arrow. ( E ) The Ikzf3 promoter (prom.) and a negative control region (neg. ctrl.) were analyzed for STAT1 enrichment via ChIP. Data were normalized to total input. Percentage enrichment relative to input was divided by IgG, and data are presented as fold-change relative to IgG. ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; * P < 0.05, ** P < 0.01, 1-way ANOVA with Tukey’s multiple comparisons test.)

Figure Legend Snippet: ( A ) Publicly available ATAC-Seq data (GSE203064) from WT and Ikzf3 –/– Th1 cells were assessed for alterations in chromatin accessibility at the Stat1 promoter. Publicly available ChIP-Seq data for Aiolos (GSM5106065) were examined at Stat1 . Sequencing tracks were viewed using IGV. The Stat1 promoter region of significant differential accessibility is indicated by a blue box ( P adj = 0.0302). A ~500 bp region encompassing the indicated Aiolos DNA binding motifs within the Stat1 promoter was subcloned into a reporter plasmid. ( B ) Schematic depicting the zinc finger (ZF) domains of WT Aiolos and a DNA-binding mutant (Aiolos DBM ). ( C ) EL4 T cells were transfected with a Stat1 promoter-reporter and WT Aiolos, Aiolos DBM , or empty vector control. Cells were also transfected with SV40- Renilla as a control for transduction efficiency. Luciferase promoter-reporter values were normalized to Renilla control and presented relative to the empty vector control. Aiolos was assessed via immunoblot with an antibody for the V5 epitope tag. β-Actin serves as a loading control. Data are representative of 3 independent experiments ( n = 3, mean ± SEM; * P < 0.05, 1-way ANOVA with Tukey’s multiple comparisons test). ( D ) Publicly available ATAC-Seq data (GSE203064) from Th1 cells and ChIP-Seq data for STAT1 (GSM994528) were viewed using IGV to identify regions of STAT1 enrichment (blue box) at Ikzf3 . Approximate ChIP primer locations are indicated with a gray arrow. ( E ) The Ikzf3 promoter (prom.) and a negative control region (neg. ctrl.) were analyzed for STAT1 enrichment via ChIP. Data were normalized to total input. Percentage enrichment relative to input was divided by IgG, and data are presented as fold-change relative to IgG. ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; * P < 0.05, ** P < 0.01, 1-way ANOVA with Tukey’s multiple comparisons test.)

Techniques Used: ChIP-sequencing, Sequencing, Binding Assay, Plasmid Preparation, Mutagenesis, Transfection, Control, Transduction, Luciferase, Western Blot, Negative Control

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Journal: JCI Insight

Article Title: Aiolos promotes CXCR3 expression on Th1 cells via positive regulation of IFN- γ /STAT1 signaling

doi: 10.1172/jci.insight.180287

Figure Lengend Snippet: ( A ) Publicly available chromatin immunoprecipitation sequencing (ChIP-Seq) data for STAT1 (GSM994528), STAT4 (GSM550303), and T-bet (GSM836124) were examined at Cxcr3 . Sequencing tracks were viewed using the Integrative Genomics Viewer (IGV). Regulatory regions of interest with transcription factor enrichment are indicated by the blue boxes. ( B ) Published RNA-Seq data (GSE203065) from in vitro–generated WT and Ikzf3 –/– Th1 cells were analyzed for DEGs. A heatmap of DEGs associated with IFN-γ/STAT1 and IL-12/STAT4 signaling in Th1 cells is shown, as well as additional genes involved in both pathways and Th cell differentiation. Gene names color-coded in blue are downregulated in Ikzf3 –/– Th1 cells. Note: Cxcr3 transcript data presented here are the same as in . ( C ) Schematic of proposed model in which Aiolos may regulate CXCR3 via impacts on components of the IFN-γ/STAT1 and IL-12/STAT4 cytokine signaling pathways. The downward arrows in blue indicate genes that are downregulated in the absence of Aiolos.

Article Snippet: The following antibodies were used to detect proteins: α-JAK2 (1:1,000; 3230, Cell Signaling Technology), α–pY-STAT4 (1:1,000; 5267, Cell Signaling Technology), α-STAT4 (1:1,000; 2653S, Cell Signaling Technology), α–pY-STAT1 (1:1,000; 9167S, Cell Signaling Technology), α-STAT1 (1:1,000; sc-417, Santa Cruz Biotechnology), α-Aiolos (1:20,000; 39293, Active Motif), α–β-actin–HRP (1:15,000; A00730, GenScript), goat α-mouse (1:5,000; 115-035-174, Jackson Immunoresearch), and mouse α-rabbit (1:5,000–1:10,000; sc-2357, Santa Cruz Biotechnology).

Techniques: ChIP-sequencing, Sequencing, RNA Sequencing, In Vitro, Generated, Cell Differentiation, Protein-Protein interactions

Journal: JCI Insight

Article Title: Aiolos promotes CXCR3 expression on Th1 cells via positive regulation of IFN- γ /STAT1 signaling

doi: 10.1172/jci.insight.180287

Figure Lengend Snippet: ( A ) Schematic of culturing system. Naive CD4 + T cells were stimulated with α-CD3/CD28 and cultured under Th1-polarizing conditions (IL-12, α–IL-4). On day 3, cells were removed from stimulation and given IFN-γ, α–IL-4, and IL-2 for an additional 2 days. ( B ) At day 5, transcript analysis was performed via qRT-PCR. Transcript was normalized to Rps18 and presented as fold-change compared with WT control ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; ** P < 0.01, *** P < 0.001, **** P < 0.0001, 2-tailed unpaired Student’s t test). ( C ) Representative flow cytometric analysis for CXCR3 on IFN-γ–treated Th1 cells at day 5. Data are displayed as MFI fold-change compared with WT controls ( n = 3 biological replicates from 3 independent experiments, mean ± SEM; ** P < 0.01, 2-tailed unpaired Student’s t test). ( D ) An immunoblot was performed to assess the relative abundance of the indicated proteins. β-Actin serves as a loading control ( n = 4 independent experiments, mean ± SEM; * P < 0.05, *** P < 0.001, 2-tailed unpaired Student’s t test). ( E ) ChIP assays were performed to assess STAT1 association with Cxcr3 in WT and Ikzf3 –/– Th1 cells. Publicly available ChIP-Seq data for STAT1 (GSM994528) were examined to identify potential regions of STAT1 enrichment. Sequencing tracks were viewed using IGV, and regulatory regions of interest are indicated by blue boxes. Approximate ChIP primer locations at the Cxcr3 promoter (prom.) and 3′ enhancer (enhc.) are indicated with gray arrows. ( F ) The indicated regions were analyzed for STAT1 enrichment. Data were normalized to total input. Percentage enrichment relative to input was divided by IgG, and data are presented as fold-change relative to IgG. ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; ** P < 0.01, *** P < 0.001, 1-way ANOVA with Tukey’s multiple comparisons test.)

Techniques: Cell Culture, Quantitative RT-PCR, Control, Western Blot, ChIP-sequencing, Sequencing

Journal: JCI Insight

Article Title: Aiolos promotes CXCR3 expression on Th1 cells via positive regulation of IFN- γ /STAT1 signaling

doi: 10.1172/jci.insight.180287

Figure Lengend Snippet: ( A ) Schematic of culturing system. WT naive CD4 + T cells were stimulated with α-CD3/CD28 under Th1-polarizing conditions (IL-12, α–IL-4). Some cells were also treated with α–IFN-γ to inhibit IFN-γ/STAT1 signaling. ( B ) At day 3, transcript analysis was performed via qRT-PCR. Transcript was normalized to Rps18 and presented as fold-change compared with WT control ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; ** P < 0.01, **** P < 0.0001, 2-tailed unpaired Student’s t test). ( C ) Representative flow cytometric analysis at day 3 for CXCR3 expression on WT Th1 cells treated with or without α–IFN-γ. Data are displayed as percentage positive for CXCR3 ( n = 3 biological replicates from 3 independent experiments, mean ± SEM; * P < 0.05, 2-tailed unpaired Student’s t test). ( D ) An immunoblot was performed to assess the relative abundance of the indicated proteins. β-Actin serves as a loading control ( n = 4 independent experiments, mean ± SEM; * P < 0.05, ** P < 0.01, **** P < 0.0001, 2-tailed unpaired Student’s t test). ( E ) At day 3, transcript and flow cytometric analyses were performed for Ikzf3 and Aiolos protein expression, respectively. Flow cytometric data are displayed as MFI fold-change compared with WT controls ( n = 3 biological replicates from 3 independent experiments, mean ± SEM; ** P < 0.01, 2-tailed unpaired Student’s t test).

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

Journal: JCI Insight

Article Title: Aiolos promotes CXCR3 expression on Th1 cells via positive regulation of IFN- γ /STAT1 signaling

doi: 10.1172/jci.insight.180287

Figure Lengend Snippet: ( A ) Publicly available ATAC-Seq data (GSE203064) from WT and Ikzf3 –/– Th1 cells were assessed for alterations in chromatin accessibility at the Stat1 promoter. Publicly available ChIP-Seq data for Aiolos (GSM5106065) were examined at Stat1 . Sequencing tracks were viewed using IGV. The Stat1 promoter region of significant differential accessibility is indicated by a blue box ( P adj = 0.0302). A ~500 bp region encompassing the indicated Aiolos DNA binding motifs within the Stat1 promoter was subcloned into a reporter plasmid. ( B ) Schematic depicting the zinc finger (ZF) domains of WT Aiolos and a DNA-binding mutant (Aiolos DBM ). ( C ) EL4 T cells were transfected with a Stat1 promoter-reporter and WT Aiolos, Aiolos DBM , or empty vector control. Cells were also transfected with SV40- Renilla as a control for transduction efficiency. Luciferase promoter-reporter values were normalized to Renilla control and presented relative to the empty vector control. Aiolos was assessed via immunoblot with an antibody for the V5 epitope tag. β-Actin serves as a loading control. Data are representative of 3 independent experiments ( n = 3, mean ± SEM; * P < 0.05, 1-way ANOVA with Tukey’s multiple comparisons test). ( D ) Publicly available ATAC-Seq data (GSE203064) from Th1 cells and ChIP-Seq data for STAT1 (GSM994528) were viewed using IGV to identify regions of STAT1 enrichment (blue box) at Ikzf3 . Approximate ChIP primer locations are indicated with a gray arrow. ( E ) The Ikzf3 promoter (prom.) and a negative control region (neg. ctrl.) were analyzed for STAT1 enrichment via ChIP. Data were normalized to total input. Percentage enrichment relative to input was divided by IgG, and data are presented as fold-change relative to IgG. ( n = 4 biological replicates from 4 independent experiments, mean ± SEM; * P < 0.05, ** P < 0.01, 1-way ANOVA with Tukey’s multiple comparisons test.)

Techniques: ChIP-sequencing, Sequencing, Binding Assay, Plasmid Preparation, Mutagenesis, Transfection, Control, Transduction, Luciferase, Western Blot, Negative Control

Figure 2. Increased IRF9 expression in sorafenib‑resistant liver cancer cells. (A) Procedure for establishing sorafenib‑resistant liver cancer cells. (B) liver cancer cells were treated with an increasing dose of sorafenib for 24 h. Cell viability was measured by MTT assay. (C) Protein levels of STAT1, STAT2 and IRF9 from immunoblotting. (D) mRNA levels of STAT1, STAT2 and IRF9 from reverse transcription‑quantitative PCR. *P<0.05 and **P<0.01 vs. liver cancer cell lines (Huh‑7 and HepG2). IRF9, interferon regulatory factor 9; wks, weeks; p‑, phosphorylated.

Journal: Oncology letters

Article Title: Machine learning model reveals roles of interferon‑stimulated genes in sorafenib‑resistant liver cancer.

doi: 10.3892/ol.2024.14571

Figure Lengend Snippet: Figure 2. Increased IRF9 expression in sorafenib‑resistant liver cancer cells. (A) Procedure for establishing sorafenib‑resistant liver cancer cells. (B) liver cancer cells were treated with an increasing dose of sorafenib for 24 h. Cell viability was measured by MTT assay. (C) Protein levels of STAT1, STAT2 and IRF9 from immunoblotting. (D) mRNA levels of STAT1, STAT2 and IRF9 from reverse transcription‑quantitative PCR. *P<0.05 and **P<0.01 vs. liver cancer cell lines (Huh‑7 and HepG2). IRF9, interferon regulatory factor 9; wks, weeks; p‑, phosphorylated.

Article Snippet: After blocking the membrane in TBS containing 5% skim milk for 1 h. The antibodies used for immunoblotting were as follows: rabbit monoclonal anti‐STAT1 (Cell signaling Technology, Cat#9176S), rabbit monoclonal anti‐PY STAT1 (Cell signaling Technology, Cat#9167S), rabbit polyclonal anti‐STAT2 (Cell signaling Technology, Cat#4594S), rabbit polyclonal anti‐PY STAT2 (Cell signaling Technology, Cat#4441S), rabbit monoclonal IRF9 (Cell signaling Technology, Cat#28492), and horseradish peroxidase‐conjugated secondary antibody (1:5,000). siRNA transfection.

Techniques: Expressing, MTT Assay, Western Blot

Figure 4. U‑ISGs unresponsiveness depends on STAT1, STAT2 and IRF9 in Huh‑7‑SR cells. (A) Huh‑7‑SR cells were transfected with si‑control, si‑STAT1, si‑STAT2, and si‑IRF9. Then, 48 h after transfection, cells were harvested and immunoblotting of STAT1, STAT2 and IRF9 was performed. (B) mRNA levels of U‑ISGs were measured by reverse transcription‑quantitative PCR. (C) After transfection, Huh‑7‑SR cells were treated with an increasing dose of sorafenib for 24 h. **P<0.01 vs. siControl. IRF, interferon regulatory factor; si, small interfering; OAS1; oligoadenylate synthetase 1; IFI27, Interferon Alpha Inducible Protein 27.

Journal: Oncology letters

Article Title: Machine learning model reveals roles of interferon‑stimulated genes in sorafenib‑resistant liver cancer.

doi: 10.3892/ol.2024.14571

Figure Lengend Snippet: Figure 4. U‑ISGs unresponsiveness depends on STAT1, STAT2 and IRF9 in Huh‑7‑SR cells. (A) Huh‑7‑SR cells were transfected with si‑control, si‑STAT1, si‑STAT2, and si‑IRF9. Then, 48 h after transfection, cells were harvested and immunoblotting of STAT1, STAT2 and IRF9 was performed. (B) mRNA levels of U‑ISGs were measured by reverse transcription‑quantitative PCR. (C) After transfection, Huh‑7‑SR cells were treated with an increasing dose of sorafenib for 24 h. **P<0.01 vs. siControl. IRF, interferon regulatory factor; si, small interfering; OAS1; oligoadenylate synthetase 1; IFI27, Interferon Alpha Inducible Protein 27.

Techniques: Transfection, Western Blot

Primers sequence used in SYBR-based reverse transcription-quantitative PCR.

Journal: Oncology Letters

Article Title: Machine learning model reveals roles of interferon‑stimulated genes in sorafenib‑resistant liver cancer

doi: 10.3892/ol.2024.14571

Figure Lengend Snippet: Primers sequence used in SYBR-based reverse transcription-quantitative PCR.

Article Snippet: After blocking the membrane in TBS containing 5% skim milk for 1 h. The antibodies used for immunoblotting were as follows: rabbit monoclonal anti-STAT1 (Cell signaling Technology, Cat#9176S), rabbit monoclonal anti-PY STAT1 (Cell signaling Technology, Cat#9167S), rabbit polyclonal anti-STAT2 (Cell signaling Technology, Cat#4594S), rabbit polyclonal anti-PY STAT2 (Cell signaling Technology, Cat#4441S), rabbit monoclonal IRF9 (Cell signaling Technology, Cat#28492), and horseradish peroxidase-conjugated secondary antibody (1:5,000).

Techniques: Sequencing

Increased IRF9 expression in sorafenib-resistant liver cancer cells. (A) Procedure for establishing sorafenib-resistant liver cancer cells. (B) liver cancer cells were treated with an increasing dose of sorafenib for 24 h. Cell viability was measured by MTT assay. (C) Protein levels of STAT1, STAT2 and IRF9 from immunoblotting. (D) mRNA levels of STAT1, STAT2 and IRF9 from reverse transcription-quantitative PCR. *P<0.05 and **P<0.01 vs. liver cancer cell lines (Huh-7 and HepG2). IRF9, interferon regulatory factor 9; wks, weeks; p-, phosphorylated.

Journal: Oncology Letters

Article Title: Machine learning model reveals roles of interferon‑stimulated genes in sorafenib‑resistant liver cancer

doi: 10.3892/ol.2024.14571

Figure Lengend Snippet: Increased IRF9 expression in sorafenib-resistant liver cancer cells. (A) Procedure for establishing sorafenib-resistant liver cancer cells. (B) liver cancer cells were treated with an increasing dose of sorafenib for 24 h. Cell viability was measured by MTT assay. (C) Protein levels of STAT1, STAT2 and IRF9 from immunoblotting. (D) mRNA levels of STAT1, STAT2 and IRF9 from reverse transcription-quantitative PCR. *P<0.05 and **P<0.01 vs. liver cancer cell lines (Huh-7 and HepG2). IRF9, interferon regulatory factor 9; wks, weeks; p-, phosphorylated.

Techniques: Expressing, MTT Assay, Western Blot, Reverse Transcription, Real-time Polymerase Chain Reaction

U-ISGs unresponsiveness depends on STAT1, STAT2 and IRF9 in Huh-7-SR cells. (A) Huh-7-SR cells were transfected with si-control, si-STAT1, si-STAT2, and si-IRF9. Then, 48 h after transfection, cells were harvested and immunoblotting of STAT1, STAT2 and IRF9 was performed. (B) mRNA levels of U-ISGs were measured by reverse transcription-quantitative PCR. (C) After transfection, Huh-7-SR cells were treated with an increasing dose of sorafenib for 24 h. **P<0.01 vs. siControl. IRF, interferon regulatory factor; si, small interfering; OAS1; oligoadenylate synthetase 1; IFI27, Interferon Alpha Inducible Protein 27.

Journal: Oncology Letters

Article Title: Machine learning model reveals roles of interferon‑stimulated genes in sorafenib‑resistant liver cancer

doi: 10.3892/ol.2024.14571

Figure Lengend Snippet: U-ISGs unresponsiveness depends on STAT1, STAT2 and IRF9 in Huh-7-SR cells. (A) Huh-7-SR cells were transfected with si-control, si-STAT1, si-STAT2, and si-IRF9. Then, 48 h after transfection, cells were harvested and immunoblotting of STAT1, STAT2 and IRF9 was performed. (B) mRNA levels of U-ISGs were measured by reverse transcription-quantitative PCR. (C) After transfection, Huh-7-SR cells were treated with an increasing dose of sorafenib for 24 h. **P<0.01 vs. siControl. IRF, interferon regulatory factor; si, small interfering; OAS1; oligoadenylate synthetase 1; IFI27, Interferon Alpha Inducible Protein 27.

Techniques: Transfection, Control, Western Blot, Reverse Transcription, Real-time Polymerase Chain Reaction

Mechanisms of U-ISGF3 complex in sorafenib resistance. U-ISGF complex, unphosphorylated interferon-stimulated gene factor-3; U-STAT1, unphosphorylated signal transducer and activator of transcription 1; U-STAT2, unphosphorylated signal transducer and activator of transcription 2; IRF9, interferon regulatory factor 9; U-ISGs, Unphosphorylated interferon-stimulated genes.

Journal: Oncology Letters

Article Title: Machine learning model reveals roles of interferon‑stimulated genes in sorafenib‑resistant liver cancer

doi: 10.3892/ol.2024.14571

Figure Lengend Snippet: Mechanisms of U-ISGF3 complex in sorafenib resistance. U-ISGF complex, unphosphorylated interferon-stimulated gene factor-3; U-STAT1, unphosphorylated signal transducer and activator of transcription 1; U-STAT2, unphosphorylated signal transducer and activator of transcription 2; IRF9, interferon regulatory factor 9; U-ISGs, Unphosphorylated interferon-stimulated genes.

Techniques:

(A) Stereoscopic brightfield and GFP fluorescent images of pancreata from adult experimental mice that carry the Pdx1-Flp, Rosa26 CAG-FSF-CreERT , and CAG-LSL-GFP transgenes on the background of two Jak1 conditional knockout alleles ( Jak1 fl/fl ) before (—TAM) or 2 months after the administration of tamoxifen (+Tam); control, animal without Rosa26 CAG-FSF-CreERT ; bar, 0.5 cm. (B) Immunoblot analysis of the expression of JAK1 and JAK2, as well as total and tyrosine phosphorylated STAT3 and STAT1 in pancreata of experimental mice shown in (A). GAPDH served as loading control. (C) IF staining of GFP and pSTAT3 on a histologic section of a pancreas from a JAK1 conditional knockout. PI, pancreatic islet; asterisks (*) mark areas devoid of GFP. The inset shows the pancreas of a control mouse that lacked the Rosa26 CAG-FSF-CreERT ; bars, 100 μm. (D) Immunoblot analysis of JAKs and STATs in pancreata of JAK1 knockout (+Tam) experimental mice expressing mutant KRAS and untreated controls (—Tam). (E) H&E-stained histologic sections of pancreata from 6-month-old mice expressing mutant KRAS in the presence (left) or absence of JAK1 (right); bars 100 μm. Experimental mice were treated with Tam at 3 weeks of age. (F) IF staining of pSTAT3 and GFP on KRAS G12D -induced pancreatic precursor lesions of JAK1-deficient mice (+Tam) and age-matched controls expressing JAK1 (—TAM); bars 50 μm. (G) GFP and pSTAT3 expression in pancreatic tumors of mice that were treated early (3 weeks, left panel) or late in life (6 months, right panel) with Tam to delete JAK1; bars, 50 μm. Brightfield and GFP fluorescent images of the tumor with normal pancreatic tissues adjacent to the tumors (NAT) in a mouse treated with Tam later in life are also shown; bar, 0.5 cm. Blue arrows point to selected GFP-positive tumor cells that retained nuclear expression of STAT3.

Journal: Cell reports

Article Title: The Janus kinase 1 is critical for pancreatic cancer initiation and progression

doi: 10.1016/j.celrep.2024.114202

Figure Lengend Snippet: (A) Stereoscopic brightfield and GFP fluorescent images of pancreata from adult experimental mice that carry the Pdx1-Flp, Rosa26 CAG-FSF-CreERT , and CAG-LSL-GFP transgenes on the background of two Jak1 conditional knockout alleles ( Jak1 fl/fl ) before (—TAM) or 2 months after the administration of tamoxifen (+Tam); control, animal without Rosa26 CAG-FSF-CreERT ; bar, 0.5 cm. (B) Immunoblot analysis of the expression of JAK1 and JAK2, as well as total and tyrosine phosphorylated STAT3 and STAT1 in pancreata of experimental mice shown in (A). GAPDH served as loading control. (C) IF staining of GFP and pSTAT3 on a histologic section of a pancreas from a JAK1 conditional knockout. PI, pancreatic islet; asterisks (*) mark areas devoid of GFP. The inset shows the pancreas of a control mouse that lacked the Rosa26 CAG-FSF-CreERT ; bars, 100 μm. (D) Immunoblot analysis of JAKs and STATs in pancreata of JAK1 knockout (+Tam) experimental mice expressing mutant KRAS and untreated controls (—Tam). (E) H&E-stained histologic sections of pancreata from 6-month-old mice expressing mutant KRAS in the presence (left) or absence of JAK1 (right); bars 100 μm. Experimental mice were treated with Tam at 3 weeks of age. (F) IF staining of pSTAT3 and GFP on KRAS G12D -induced pancreatic precursor lesions of JAK1-deficient mice (+Tam) and age-matched controls expressing JAK1 (—TAM); bars 50 μm. (G) GFP and pSTAT3 expression in pancreatic tumors of mice that were treated early (3 weeks, left panel) or late in life (6 months, right panel) with Tam to delete JAK1; bars, 50 μm. Brightfield and GFP fluorescent images of the tumor with normal pancreatic tissues adjacent to the tumors (NAT) in a mouse treated with Tam later in life are also shown; bar, 0.5 cm. Blue arrows point to selected GFP-positive tumor cells that retained nuclear expression of STAT3.

Article Snippet: Rabbit polyclonal, pY-STAT1 , Origene , Cat#TA309955.

Techniques: Knock-Out, Control, Western Blot, Expressing, Staining, Mutagenesis

Journal: Cell reports

Article Title: The Janus kinase 1 is critical for pancreatic cancer initiation and progression

doi: 10.1016/j.celrep.2024.114202

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: Rabbit polyclonal, pY-STAT1 , Origene , Cat#TA309955.

Techniques: Recombinant, Transduction, Polymer, Virus, Western Blot, Software

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1) Product Images from "Aiolos promotes CXCR3 expression on Th1 cells via positive regulation of IFN- γ /STAT1 signaling"

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