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Biotechnology Information irf1 gene coding sequence cds
Expression of <t>IRF1</t> and Type I interferon pathway-related proteins in gastric cancer cells. A : Simulation of type I interferon response in gastric cancer cells by incubating with interferon, showing increased expression of interferon pathway protein IRF1. B : Protein expression in gastric cancer cells after transfection with pcDNA3.1(+) -IRF1-HA.1 C : Protein expression in gastric cancer cells after transfection with siRNA-IRF1. D : Changes in the expression of interferon pathway proteins after overexpression or inhibition of IRF1 in gastric cancer cells
Irf1 Gene Coding Sequence Cds, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/irf1+gene+coding+sequence+cds/cds+coding+gene+irf1+sequence/pmc12799679-114-1-13
Average 86 stars, based on 1 article reviews
irf1 gene coding sequence cds - by Bioz Stars, 2026-10
86/100 stars

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Article Title: IRF1 suppresses gastric tumorigenesis via dual PI3K/AKT-ERK pathway modulation and functional antagonism of oncogenic MX2

Journal: Cellular Oncology (Dordrecht, Netherlands)

doi: 10.1007/s13402-025-01134-w

Expression of IRF1 and Type I interferon pathway-related proteins in gastric cancer cells. A : Simulation of type I interferon response in gastric cancer cells by incubating with interferon, showing increased expression of interferon pathway protein IRF1. B : Protein expression in gastric cancer cells after transfection with pcDNA3.1(+) -IRF1-HA.1 C : Protein expression in gastric cancer cells after transfection with siRNA-IRF1. D : Changes in the expression of interferon pathway proteins after overexpression or inhibition of IRF1 in gastric cancer cells
Figure Legend Snippet: Expression of IRF1 and Type I interferon pathway-related proteins in gastric cancer cells. A : Simulation of type I interferon response in gastric cancer cells by incubating with interferon, showing increased expression of interferon pathway protein IRF1. B : Protein expression in gastric cancer cells after transfection with pcDNA3.1(+) -IRF1-HA.1 C : Protein expression in gastric cancer cells after transfection with siRNA-IRF1. D : Changes in the expression of interferon pathway proteins after overexpression or inhibition of IRF1 in gastric cancer cells

Techniques Used: Expressing, Transfection, Over Expression, Inhibition

Expression characteristics and clinical relevance of IRF1 in gastric cancer tissues. A : IRF1 expression is significantly higher in gastric cancer tissues compared to adjacent normal tissues ( P < 0.001). B : Paired analysis shows that IRF1 expression is significantly upregulated in gastric cancer tissues compared to matched adjacent tissues ( P = 0.002). C : Survival analysis indicates that high IRF1 expression is associated with a relatively better prognosis in gastric cancer patients (Log-rank P = 0.030). D : Representative immunohistochemistry (IHC) images showing high and low IRF1 expression in tumor tissues. E : Differential expression analysis confirms that IRF1 is significantly upregulated in tumor tissues ( P = 0.021). F : Paired analysis of tumor and adjacent normal tissues demonstrates significantly higher IRF1 expression in tumors ( P < 0.001). G : Survival analysis further supports that high IRF1 expression correlates with a better prognosis in gastric cancer patients (Log-rank P = 0.010). * P < 0.05, ** P < 0.01, *** P < 0.001, *** P < 0.0001
Figure Legend Snippet: Expression characteristics and clinical relevance of IRF1 in gastric cancer tissues. A : IRF1 expression is significantly higher in gastric cancer tissues compared to adjacent normal tissues ( P < 0.001). B : Paired analysis shows that IRF1 expression is significantly upregulated in gastric cancer tissues compared to matched adjacent tissues ( P = 0.002). C : Survival analysis indicates that high IRF1 expression is associated with a relatively better prognosis in gastric cancer patients (Log-rank P = 0.030). D : Representative immunohistochemistry (IHC) images showing high and low IRF1 expression in tumor tissues. E : Differential expression analysis confirms that IRF1 is significantly upregulated in tumor tissues ( P = 0.021). F : Paired analysis of tumor and adjacent normal tissues demonstrates significantly higher IRF1 expression in tumors ( P < 0.001). G : Survival analysis further supports that high IRF1 expression correlates with a better prognosis in gastric cancer patients (Log-rank P = 0.010). * P < 0.05, ** P < 0.01, *** P < 0.001, *** P < 0.0001

Techniques Used: Expressing, Immunohistochemistry, Quantitative Proteomics

Effects of IRF1 expression on gastric cancer cell function. A - B : CCK8 cytotoxicity assay showing inhibition of AGS and BGC-823 cell proliferation after transfection with IRF1-HA overexpression plasmid. C - D : Transwell migration and invasion assay showing suppression of AGS and BGC-823 cell migration and invasion 48 h after transfection with IRF1-HA overexpression plasmid. E - F : CCK8 cytotoxicity assay showing promotion of AGS and BGC-823 cell proliferation after transfection with siRNA-IRF1. G - H : Transwell migration and invasion assay showing enhanced migration and invasion of AGS and BGC-823 cells 48 h after transfection with siRNA-IRF1. I : Flow cytometry apoptosis assay showing increased apoptosis in gastric cancer cells 48 h after Dox-induced IRF1 overexpression in stable cell lines. J : Changes in apoptosis-related protein expression 48 h after Dox-induced IRF1 overexpression in gastric cancer cell stable lines. K : Immunofluorescence localization experiment confirming nuclear localization of IRF1 in gastric cancer cells. Scale bar: 10 μm. * P < 0.05, ** P < 0.01, ** P < 0.001
Figure Legend Snippet: Effects of IRF1 expression on gastric cancer cell function. A - B : CCK8 cytotoxicity assay showing inhibition of AGS and BGC-823 cell proliferation after transfection with IRF1-HA overexpression plasmid. C - D : Transwell migration and invasion assay showing suppression of AGS and BGC-823 cell migration and invasion 48 h after transfection with IRF1-HA overexpression plasmid. E - F : CCK8 cytotoxicity assay showing promotion of AGS and BGC-823 cell proliferation after transfection with siRNA-IRF1. G - H : Transwell migration and invasion assay showing enhanced migration and invasion of AGS and BGC-823 cells 48 h after transfection with siRNA-IRF1. I : Flow cytometry apoptosis assay showing increased apoptosis in gastric cancer cells 48 h after Dox-induced IRF1 overexpression in stable cell lines. J : Changes in apoptosis-related protein expression 48 h after Dox-induced IRF1 overexpression in gastric cancer cell stable lines. K : Immunofluorescence localization experiment confirming nuclear localization of IRF1 in gastric cancer cells. Scale bar: 10 μm. * P < 0.05, ** P < 0.01, ** P < 0.001

Techniques Used: Expressing, Cell Function Assay, Cytotoxicity Assay, Inhibition, Transfection, Over Expression, Plasmid Preparation, Migration, Invasion Assay, Flow Cytometry, Apoptosis Assay, Stable Transfection, Immunofluorescence

Establishment of an Inducible IRF1 expression nude mouse subcutaneous xenograft and lung metastasis model. A : In vivo experiments show that the tumor volume of the IRF1 overexpression group in nude mouse subcutaneous xenografts is significantly smaller than that of the control group (Mean ± SEM). B : Gross anatomy of subcutaneous xenograft tumors in nude mice. C : HE staining of subcutaneous xenograft tumors (tumor tissues from mouse #1 and #2). D : Immunohistochemistry (IHC) analysis of IRF1 expression in subcutaneous xenograft tumors, showing significant IRF1 overexpression in the Dox (+) group. E : Bioluminescence imaging of nude mice injected via the tail vein with BGC-IRF1-LUC cells at 0, 2, 3, and 4 weeks post-injection. F : Quantification of lung fluorescence intensity in both groups, demonstrating significantly lower fluorescence intensity in the IRF1 overexpression group compared to the control group. G : Gross anatomy of lung tissues in nude mice, showing more metastatic nodules in the control group than in the IRF1 overexpression group. H : HE staining and IRF1-specific IHC staining of lung tissues in nude mice, confirming IRF1 overexpression in the Dox-induced group. Scale bar: 100 μm. * P < 0.05, ** P < 0.01, *** P < 0.001
Figure Legend Snippet: Establishment of an Inducible IRF1 expression nude mouse subcutaneous xenograft and lung metastasis model. A : In vivo experiments show that the tumor volume of the IRF1 overexpression group in nude mouse subcutaneous xenografts is significantly smaller than that of the control group (Mean ± SEM). B : Gross anatomy of subcutaneous xenograft tumors in nude mice. C : HE staining of subcutaneous xenograft tumors (tumor tissues from mouse #1 and #2). D : Immunohistochemistry (IHC) analysis of IRF1 expression in subcutaneous xenograft tumors, showing significant IRF1 overexpression in the Dox (+) group. E : Bioluminescence imaging of nude mice injected via the tail vein with BGC-IRF1-LUC cells at 0, 2, 3, and 4 weeks post-injection. F : Quantification of lung fluorescence intensity in both groups, demonstrating significantly lower fluorescence intensity in the IRF1 overexpression group compared to the control group. G : Gross anatomy of lung tissues in nude mice, showing more metastatic nodules in the control group than in the IRF1 overexpression group. H : HE staining and IRF1-specific IHC staining of lung tissues in nude mice, confirming IRF1 overexpression in the Dox-induced group. Scale bar: 100 μm. * P < 0.05, ** P < 0.01, *** P < 0.001

Techniques Used: Expressing, In Vivo, Over Expression, Control, Staining, Immunohistochemistry, Imaging, Injection, Fluorescence

Exploration of IRF1-related mechanisms. A : Schematic diagram of the IRF1 protein structure; DBD: DNA binding domain; IAD: IRF-association domain. B : Validation of successful expression of the pcDNA3.1(+)-IRF1Δ1 recombinant plasmid. C : No significant changes in apoptosis-related protein expression after IRF1Δ1 overexpression. D : Overexpression of IRF1 significantly affects PI3K pathway-related proteins, whereas IRF1Δ1 overexpression shows no apparent changes. E : Bidirectional validation of the interaction between IRF1 and MX2 using HA and Flag magnetic beads. F : Immunofluorescence co-localization analysis confirming the nuclear co-expression of IRF1 and MX2
Figure Legend Snippet: Exploration of IRF1-related mechanisms. A : Schematic diagram of the IRF1 protein structure; DBD: DNA binding domain; IAD: IRF-association domain. B : Validation of successful expression of the pcDNA3.1(+)-IRF1Δ1 recombinant plasmid. C : No significant changes in apoptosis-related protein expression after IRF1Δ1 overexpression. D : Overexpression of IRF1 significantly affects PI3K pathway-related proteins, whereas IRF1Δ1 overexpression shows no apparent changes. E : Bidirectional validation of the interaction between IRF1 and MX2 using HA and Flag magnetic beads. F : Immunofluorescence co-localization analysis confirming the nuclear co-expression of IRF1 and MX2

Techniques Used: Binding Assay, Biomarker Discovery, Expressing, Recombinant, Plasmid Preparation, Over Expression, Magnetic Beads, Immunofluorescence

MX2-related functions in gastric cancer. A : Schematic diagram of MX2 functional domain fragments. B : Co-IP assay validating the interaction between IRF1-HA and MX2-Flag, showing that IRF1 loses interaction with MX2-FlagΔ1. C : Schematic of MX2 site-directed mutations. K131A: GTP-binding defective, unable to enter the nucleus; NLS: nuclear localization signal; BSE: bundle signaling element. D : WB validation of MX2 site-directed mutant overexpression plasmids. E : MX2 overexpression promotes AGS cell migration and invasion. F : MX2 overexpression promotes BGC-823 cell migration and invasion. G : After transfecting MX2 and its mutants into BGC-823 cells and incubating for 48 h, nuclear localization site mutations in MX2 result in the loss of its pro-migratory and pro-invasive effects. H : Immunofluorescence localization of MX2 and its mutants in gastric cancer cells. After transfection with MX2-ΔN or MX2-K131A, MX2 is retained in the cytoplasm, losing its nuclear localization ability. I : WB validation of MX2’s pro-migratory function through EMT pathway analysis. Scale bar: 10 μm. * P < 0.05, ** P < 0.01, *** P < 0.001
Figure Legend Snippet: MX2-related functions in gastric cancer. A : Schematic diagram of MX2 functional domain fragments. B : Co-IP assay validating the interaction between IRF1-HA and MX2-Flag, showing that IRF1 loses interaction with MX2-FlagΔ1. C : Schematic of MX2 site-directed mutations. K131A: GTP-binding defective, unable to enter the nucleus; NLS: nuclear localization signal; BSE: bundle signaling element. D : WB validation of MX2 site-directed mutant overexpression plasmids. E : MX2 overexpression promotes AGS cell migration and invasion. F : MX2 overexpression promotes BGC-823 cell migration and invasion. G : After transfecting MX2 and its mutants into BGC-823 cells and incubating for 48 h, nuclear localization site mutations in MX2 result in the loss of its pro-migratory and pro-invasive effects. H : Immunofluorescence localization of MX2 and its mutants in gastric cancer cells. After transfection with MX2-ΔN or MX2-K131A, MX2 is retained in the cytoplasm, losing its nuclear localization ability. I : WB validation of MX2’s pro-migratory function through EMT pathway analysis. Scale bar: 10 μm. * P < 0.05, ** P < 0.01, *** P < 0.001

Techniques Used: Functional Assay, Co-Immunoprecipitation Assay, Binding Assay, Biomarker Discovery, Mutagenesis, Over Expression, Migration, Immunofluorescence, Transfection

Functional model of the IRF1-MX2 protein complex
Figure Legend Snippet: Functional model of the IRF1-MX2 protein complex

Techniques Used: Functional Assay

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Article Title: IRF1 suppresses gastric tumorigenesis via dual PI3K/AKT-ERK pathway modulation and functional antagonism of oncogenic MX2.
Article Snippet: .. The IRF1 gene coding sequence (CDS) was retrieved from the National Center for Biotechnology Information (NCBI), selecting the longest transcript. .. The BamHI and EcoRI restriction enzyme sites were used for cloning, with the following primer sequences: Forward primer (FP): C G C G G A T C C G C C A C C A T G C C C A T C A C T C G G A T, Reverse primer (RP): C C G G A A T T C T T A T C A A G C G T A G T C T G G G A C G T C G T A T G G G T A C T A C G G T G C A C A G G G A A T G. For MX2 overexpression plasmid, BamHI and XhoI restriction sites were used, with the following primers: Forward primer (FP): C G C G G A T C C G C C A C C A T G T C T A A G G C C C A C A A G, FLAG-tag Reverse primer (RP): C C G C T C G A G T T A T C A C T T G T C A T C G T C G T C C T T G T A A T C G T G G A T C T C T T T G C T G, HA-tag Reverse primer (RP): C C G C T C G A G T T A T C A A G C G T A G T C T G G G A C G T C G T A T G G G T A G T G G A T C T C T T T G C T G. Using Vazyme 2× Phanta Evo HS Master Mix high-fidelity DNA polymerase, the cDNA of AGS gastric cancer cells was used as a template.

Article Title: IRF1 suppresses gastric tumorigenesis via dual PI3K/AKT-ERK pathway modulation and functional antagonism of oncogenic MX2
Article Snippet: .. The IRF1 gene coding sequence (CDS) was retrieved from the National Center for Biotechnology Information (NCBI), selecting the longest transcript. ..



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Biotechnology Information irf1 gene coding sequence cds
Expression of <t>IRF1</t> and Type I interferon pathway-related proteins in gastric cancer cells. A : Simulation of type I interferon response in gastric cancer cells by incubating with interferon, showing increased expression of interferon pathway protein IRF1. B : Protein expression in gastric cancer cells after transfection with pcDNA3.1(+) -IRF1-HA.1 C : Protein expression in gastric cancer cells after transfection with siRNA-IRF1. D : Changes in the expression of interferon pathway proteins after overexpression or inhibition of IRF1 in gastric cancer cells
Irf1 Gene Coding Sequence Cds, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/irf1+gene+coding+sequence+cds/cds+coding+gene+irf1+sequence/pmc12799679-114-1-13
Average 86 stars, based on 1 article reviews
irf1 gene coding sequence cds - by Bioz Stars, 2026-10
86/100 stars
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Expression of IRF1 and Type I interferon pathway-related proteins in gastric cancer cells. A : Simulation of type I interferon response in gastric cancer cells by incubating with interferon, showing increased expression of interferon pathway protein IRF1. B : Protein expression in gastric cancer cells after transfection with pcDNA3.1(+) -IRF1-HA.1 C : Protein expression in gastric cancer cells after transfection with siRNA-IRF1. D : Changes in the expression of interferon pathway proteins after overexpression or inhibition of IRF1 in gastric cancer cells

Journal: Cellular Oncology (Dordrecht, Netherlands)

Article Title: IRF1 suppresses gastric tumorigenesis via dual PI3K/AKT-ERK pathway modulation and functional antagonism of oncogenic MX2

doi: 10.1007/s13402-025-01134-w

Figure Lengend Snippet: Expression of IRF1 and Type I interferon pathway-related proteins in gastric cancer cells. A : Simulation of type I interferon response in gastric cancer cells by incubating with interferon, showing increased expression of interferon pathway protein IRF1. B : Protein expression in gastric cancer cells after transfection with pcDNA3.1(+) -IRF1-HA.1 C : Protein expression in gastric cancer cells after transfection with siRNA-IRF1. D : Changes in the expression of interferon pathway proteins after overexpression or inhibition of IRF1 in gastric cancer cells

Article Snippet: The IRF1 gene coding sequence (CDS) was retrieved from the National Center for Biotechnology Information (NCBI), selecting the longest transcript.

Techniques: Expressing, Transfection, Over Expression, Inhibition

Expression characteristics and clinical relevance of IRF1 in gastric cancer tissues. A : IRF1 expression is significantly higher in gastric cancer tissues compared to adjacent normal tissues ( P < 0.001). B : Paired analysis shows that IRF1 expression is significantly upregulated in gastric cancer tissues compared to matched adjacent tissues ( P = 0.002). C : Survival analysis indicates that high IRF1 expression is associated with a relatively better prognosis in gastric cancer patients (Log-rank P = 0.030). D : Representative immunohistochemistry (IHC) images showing high and low IRF1 expression in tumor tissues. E : Differential expression analysis confirms that IRF1 is significantly upregulated in tumor tissues ( P = 0.021). F : Paired analysis of tumor and adjacent normal tissues demonstrates significantly higher IRF1 expression in tumors ( P < 0.001). G : Survival analysis further supports that high IRF1 expression correlates with a better prognosis in gastric cancer patients (Log-rank P = 0.010). * P < 0.05, ** P < 0.01, *** P < 0.001, *** P < 0.0001

Journal: Cellular Oncology (Dordrecht, Netherlands)

Article Title: IRF1 suppresses gastric tumorigenesis via dual PI3K/AKT-ERK pathway modulation and functional antagonism of oncogenic MX2

doi: 10.1007/s13402-025-01134-w

Figure Lengend Snippet: Expression characteristics and clinical relevance of IRF1 in gastric cancer tissues. A : IRF1 expression is significantly higher in gastric cancer tissues compared to adjacent normal tissues ( P < 0.001). B : Paired analysis shows that IRF1 expression is significantly upregulated in gastric cancer tissues compared to matched adjacent tissues ( P = 0.002). C : Survival analysis indicates that high IRF1 expression is associated with a relatively better prognosis in gastric cancer patients (Log-rank P = 0.030). D : Representative immunohistochemistry (IHC) images showing high and low IRF1 expression in tumor tissues. E : Differential expression analysis confirms that IRF1 is significantly upregulated in tumor tissues ( P = 0.021). F : Paired analysis of tumor and adjacent normal tissues demonstrates significantly higher IRF1 expression in tumors ( P < 0.001). G : Survival analysis further supports that high IRF1 expression correlates with a better prognosis in gastric cancer patients (Log-rank P = 0.010). * P < 0.05, ** P < 0.01, *** P < 0.001, *** P < 0.0001

Article Snippet: The IRF1 gene coding sequence (CDS) was retrieved from the National Center for Biotechnology Information (NCBI), selecting the longest transcript.

Techniques: Expressing, Immunohistochemistry, Quantitative Proteomics

Effects of IRF1 expression on gastric cancer cell function. A - B : CCK8 cytotoxicity assay showing inhibition of AGS and BGC-823 cell proliferation after transfection with IRF1-HA overexpression plasmid. C - D : Transwell migration and invasion assay showing suppression of AGS and BGC-823 cell migration and invasion 48 h after transfection with IRF1-HA overexpression plasmid. E - F : CCK8 cytotoxicity assay showing promotion of AGS and BGC-823 cell proliferation after transfection with siRNA-IRF1. G - H : Transwell migration and invasion assay showing enhanced migration and invasion of AGS and BGC-823 cells 48 h after transfection with siRNA-IRF1. I : Flow cytometry apoptosis assay showing increased apoptosis in gastric cancer cells 48 h after Dox-induced IRF1 overexpression in stable cell lines. J : Changes in apoptosis-related protein expression 48 h after Dox-induced IRF1 overexpression in gastric cancer cell stable lines. K : Immunofluorescence localization experiment confirming nuclear localization of IRF1 in gastric cancer cells. Scale bar: 10 μm. * P < 0.05, ** P < 0.01, ** P < 0.001

Journal: Cellular Oncology (Dordrecht, Netherlands)

Article Title: IRF1 suppresses gastric tumorigenesis via dual PI3K/AKT-ERK pathway modulation and functional antagonism of oncogenic MX2

doi: 10.1007/s13402-025-01134-w

Figure Lengend Snippet: Effects of IRF1 expression on gastric cancer cell function. A - B : CCK8 cytotoxicity assay showing inhibition of AGS and BGC-823 cell proliferation after transfection with IRF1-HA overexpression plasmid. C - D : Transwell migration and invasion assay showing suppression of AGS and BGC-823 cell migration and invasion 48 h after transfection with IRF1-HA overexpression plasmid. E - F : CCK8 cytotoxicity assay showing promotion of AGS and BGC-823 cell proliferation after transfection with siRNA-IRF1. G - H : Transwell migration and invasion assay showing enhanced migration and invasion of AGS and BGC-823 cells 48 h after transfection with siRNA-IRF1. I : Flow cytometry apoptosis assay showing increased apoptosis in gastric cancer cells 48 h after Dox-induced IRF1 overexpression in stable cell lines. J : Changes in apoptosis-related protein expression 48 h after Dox-induced IRF1 overexpression in gastric cancer cell stable lines. K : Immunofluorescence localization experiment confirming nuclear localization of IRF1 in gastric cancer cells. Scale bar: 10 μm. * P < 0.05, ** P < 0.01, ** P < 0.001

Article Snippet: The IRF1 gene coding sequence (CDS) was retrieved from the National Center for Biotechnology Information (NCBI), selecting the longest transcript.

Techniques: Expressing, Cell Function Assay, Cytotoxicity Assay, Inhibition, Transfection, Over Expression, Plasmid Preparation, Migration, Invasion Assay, Flow Cytometry, Apoptosis Assay, Stable Transfection, Immunofluorescence

Establishment of an Inducible IRF1 expression nude mouse subcutaneous xenograft and lung metastasis model. A : In vivo experiments show that the tumor volume of the IRF1 overexpression group in nude mouse subcutaneous xenografts is significantly smaller than that of the control group (Mean ± SEM). B : Gross anatomy of subcutaneous xenograft tumors in nude mice. C : HE staining of subcutaneous xenograft tumors (tumor tissues from mouse #1 and #2). D : Immunohistochemistry (IHC) analysis of IRF1 expression in subcutaneous xenograft tumors, showing significant IRF1 overexpression in the Dox (+) group. E : Bioluminescence imaging of nude mice injected via the tail vein with BGC-IRF1-LUC cells at 0, 2, 3, and 4 weeks post-injection. F : Quantification of lung fluorescence intensity in both groups, demonstrating significantly lower fluorescence intensity in the IRF1 overexpression group compared to the control group. G : Gross anatomy of lung tissues in nude mice, showing more metastatic nodules in the control group than in the IRF1 overexpression group. H : HE staining and IRF1-specific IHC staining of lung tissues in nude mice, confirming IRF1 overexpression in the Dox-induced group. Scale bar: 100 μm. * P < 0.05, ** P < 0.01, *** P < 0.001

Journal: Cellular Oncology (Dordrecht, Netherlands)

Article Title: IRF1 suppresses gastric tumorigenesis via dual PI3K/AKT-ERK pathway modulation and functional antagonism of oncogenic MX2

doi: 10.1007/s13402-025-01134-w

Figure Lengend Snippet: Establishment of an Inducible IRF1 expression nude mouse subcutaneous xenograft and lung metastasis model. A : In vivo experiments show that the tumor volume of the IRF1 overexpression group in nude mouse subcutaneous xenografts is significantly smaller than that of the control group (Mean ± SEM). B : Gross anatomy of subcutaneous xenograft tumors in nude mice. C : HE staining of subcutaneous xenograft tumors (tumor tissues from mouse #1 and #2). D : Immunohistochemistry (IHC) analysis of IRF1 expression in subcutaneous xenograft tumors, showing significant IRF1 overexpression in the Dox (+) group. E : Bioluminescence imaging of nude mice injected via the tail vein with BGC-IRF1-LUC cells at 0, 2, 3, and 4 weeks post-injection. F : Quantification of lung fluorescence intensity in both groups, demonstrating significantly lower fluorescence intensity in the IRF1 overexpression group compared to the control group. G : Gross anatomy of lung tissues in nude mice, showing more metastatic nodules in the control group than in the IRF1 overexpression group. H : HE staining and IRF1-specific IHC staining of lung tissues in nude mice, confirming IRF1 overexpression in the Dox-induced group. Scale bar: 100 μm. * P < 0.05, ** P < 0.01, *** P < 0.001

Article Snippet: The IRF1 gene coding sequence (CDS) was retrieved from the National Center for Biotechnology Information (NCBI), selecting the longest transcript.

Techniques: Expressing, In Vivo, Over Expression, Control, Staining, Immunohistochemistry, Imaging, Injection, Fluorescence

Exploration of IRF1-related mechanisms. A : Schematic diagram of the IRF1 protein structure; DBD: DNA binding domain; IAD: IRF-association domain. B : Validation of successful expression of the pcDNA3.1(+)-IRF1Δ1 recombinant plasmid. C : No significant changes in apoptosis-related protein expression after IRF1Δ1 overexpression. D : Overexpression of IRF1 significantly affects PI3K pathway-related proteins, whereas IRF1Δ1 overexpression shows no apparent changes. E : Bidirectional validation of the interaction between IRF1 and MX2 using HA and Flag magnetic beads. F : Immunofluorescence co-localization analysis confirming the nuclear co-expression of IRF1 and MX2

Journal: Cellular Oncology (Dordrecht, Netherlands)

Article Title: IRF1 suppresses gastric tumorigenesis via dual PI3K/AKT-ERK pathway modulation and functional antagonism of oncogenic MX2

doi: 10.1007/s13402-025-01134-w

Figure Lengend Snippet: Exploration of IRF1-related mechanisms. A : Schematic diagram of the IRF1 protein structure; DBD: DNA binding domain; IAD: IRF-association domain. B : Validation of successful expression of the pcDNA3.1(+)-IRF1Δ1 recombinant plasmid. C : No significant changes in apoptosis-related protein expression after IRF1Δ1 overexpression. D : Overexpression of IRF1 significantly affects PI3K pathway-related proteins, whereas IRF1Δ1 overexpression shows no apparent changes. E : Bidirectional validation of the interaction between IRF1 and MX2 using HA and Flag magnetic beads. F : Immunofluorescence co-localization analysis confirming the nuclear co-expression of IRF1 and MX2

Article Snippet: The IRF1 gene coding sequence (CDS) was retrieved from the National Center for Biotechnology Information (NCBI), selecting the longest transcript.

Techniques: Binding Assay, Biomarker Discovery, Expressing, Recombinant, Plasmid Preparation, Over Expression, Magnetic Beads, Immunofluorescence

MX2-related functions in gastric cancer. A : Schematic diagram of MX2 functional domain fragments. B : Co-IP assay validating the interaction between IRF1-HA and MX2-Flag, showing that IRF1 loses interaction with MX2-FlagΔ1. C : Schematic of MX2 site-directed mutations. K131A: GTP-binding defective, unable to enter the nucleus; NLS: nuclear localization signal; BSE: bundle signaling element. D : WB validation of MX2 site-directed mutant overexpression plasmids. E : MX2 overexpression promotes AGS cell migration and invasion. F : MX2 overexpression promotes BGC-823 cell migration and invasion. G : After transfecting MX2 and its mutants into BGC-823 cells and incubating for 48 h, nuclear localization site mutations in MX2 result in the loss of its pro-migratory and pro-invasive effects. H : Immunofluorescence localization of MX2 and its mutants in gastric cancer cells. After transfection with MX2-ΔN or MX2-K131A, MX2 is retained in the cytoplasm, losing its nuclear localization ability. I : WB validation of MX2’s pro-migratory function through EMT pathway analysis. Scale bar: 10 μm. * P < 0.05, ** P < 0.01, *** P < 0.001

Journal: Cellular Oncology (Dordrecht, Netherlands)

Article Title: IRF1 suppresses gastric tumorigenesis via dual PI3K/AKT-ERK pathway modulation and functional antagonism of oncogenic MX2

doi: 10.1007/s13402-025-01134-w

Figure Lengend Snippet: MX2-related functions in gastric cancer. A : Schematic diagram of MX2 functional domain fragments. B : Co-IP assay validating the interaction between IRF1-HA and MX2-Flag, showing that IRF1 loses interaction with MX2-FlagΔ1. C : Schematic of MX2 site-directed mutations. K131A: GTP-binding defective, unable to enter the nucleus; NLS: nuclear localization signal; BSE: bundle signaling element. D : WB validation of MX2 site-directed mutant overexpression plasmids. E : MX2 overexpression promotes AGS cell migration and invasion. F : MX2 overexpression promotes BGC-823 cell migration and invasion. G : After transfecting MX2 and its mutants into BGC-823 cells and incubating for 48 h, nuclear localization site mutations in MX2 result in the loss of its pro-migratory and pro-invasive effects. H : Immunofluorescence localization of MX2 and its mutants in gastric cancer cells. After transfection with MX2-ΔN or MX2-K131A, MX2 is retained in the cytoplasm, losing its nuclear localization ability. I : WB validation of MX2’s pro-migratory function through EMT pathway analysis. Scale bar: 10 μm. * P < 0.05, ** P < 0.01, *** P < 0.001

Article Snippet: The IRF1 gene coding sequence (CDS) was retrieved from the National Center for Biotechnology Information (NCBI), selecting the longest transcript.

Techniques: Functional Assay, Co-Immunoprecipitation Assay, Binding Assay, Biomarker Discovery, Mutagenesis, Over Expression, Migration, Immunofluorescence, Transfection

Functional model of the IRF1-MX2 protein complex

Journal: Cellular Oncology (Dordrecht, Netherlands)

Article Title: IRF1 suppresses gastric tumorigenesis via dual PI3K/AKT-ERK pathway modulation and functional antagonism of oncogenic MX2

doi: 10.1007/s13402-025-01134-w

Figure Lengend Snippet: Functional model of the IRF1-MX2 protein complex

Article Snippet: The IRF1 gene coding sequence (CDS) was retrieved from the National Center for Biotechnology Information (NCBI), selecting the longest transcript.

Techniques: Functional Assay