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recombinant human tgfb3  (MedChemExpress)


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    Structured Review

    MedChemExpress recombinant human tgfb3
    (A) Schematic of the multilayer perceptron with eight input nodes (BMP4, CD248, GRP, LGR4, MGP, <t>TGFB3,</t> ERBB3, ETS2), a five-node hidden layer and a two-node output layer encoding Control (normal) and Treatment (GC). (B) Receiver operating characteristic (ROC) curve and area under the curve (AUC) in the training cohort (TCGA-STAD). (C) ROC curve and AUC in the independent validation cohort ( GSE54129 ).
    Recombinant Human Tgfb3, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+human+tgf/Animal-Free+TGF+beta+3%2FTGFB3%2C+Human/pmc13381258-176-7-21
    Average 94 stars, based on 1 article reviews
    recombinant human tgfb3 - by Bioz Stars, 2026-10
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    Images

    1) Product Images from "From proteome-wide Mendelian randomization and multi-omics integration to functional validation: TGFB3 as a prioritized candidate in gastric adenocarcinoma"

    Article Title: From proteome-wide Mendelian randomization and multi-omics integration to functional validation: TGFB3 as a prioritized candidate in gastric adenocarcinoma

    Journal: Frontiers in Oncology

    doi: 10.3389/fonc.2026.1883227

    (A) Schematic of the multilayer perceptron with eight input nodes (BMP4, CD248, GRP, LGR4, MGP, TGFB3, ERBB3, ETS2), a five-node hidden layer and a two-node output layer encoding Control (normal) and Treatment (GC). (B) Receiver operating characteristic (ROC) curve and area under the curve (AUC) in the training cohort (TCGA-STAD). (C) ROC curve and AUC in the independent validation cohort ( GSE54129 ).
    Figure Legend Snippet: (A) Schematic of the multilayer perceptron with eight input nodes (BMP4, CD248, GRP, LGR4, MGP, TGFB3, ERBB3, ETS2), a five-node hidden layer and a two-node output layer encoding Control (normal) and Treatment (GC). (B) Receiver operating characteristic (ROC) curve and area under the curve (AUC) in the training cohort (TCGA-STAD). (C) ROC curve and AUC in the independent validation cohort ( GSE54129 ).

    Techniques Used: Control, Biomarker Discovery

    Kaplan–Meier analysis of OS in gastric cancer patients stratified by mRNA expression of network-prioritized genes: (A) BMP4, (B) CD248, (C) GRP, (D) LGR4, (E) MGP, (F) TGFB3, (G) ERBB3 and (H) ETS2.
    Figure Legend Snippet: Kaplan–Meier analysis of OS in gastric cancer patients stratified by mRNA expression of network-prioritized genes: (A) BMP4, (B) CD248, (C) GRP, (D) LGR4, (E) MGP, (F) TGFB3, (G) ERBB3 and (H) ETS2.

    Techniques Used: Expressing

    Multiplex immunofluorescence validation of hub gene expression in the gastric cancer tumor microenvironment. (A) Representative staining of BMP4 (red) and Pan-CK (green) in gastric cancer showing predominant localization of BMP4 to Pan-CK + tumor epithelial nests. (B) CD248 (red) colocalizes with FAP + cancer-associated fibroblasts (CAF; green) within the stromal compartment. (C) TGFB3 (red) is enriched in the FAP + CAF-rich stroma. (D) LGR4 (red) is detected both in FAP + CAFs (green) and in Pan-CK + tumor epithelial cells (yellow). (E) MGP (red) is present in CD31 + endothelial structures (yellow) and in FAP + CAF-rich stromal regions (green). Nuclei are counterstained with DAPI (blue). Left panels show merged images; right panels display the corresponding single-channel views. Scale bars, 100 μm. Integrating the proteome-wide MR screen with PPI topology, survival analysis, and compartment-resolved expression patterns, we prioritized ERBB3, LGR4, BMP4, CD248, MGP, TGFB3, GRP, and ETS2 as network-prioritized candidates for downstream contextualization. Among them, TGFB3 was selected for focused computational and cellular characterization on the basis of several convergent prioritization features, including its nominal MR association, network-topology ranking, association with overall survival, fibroblast-enriched expression pattern, and spatial organization in gastric cancer tissues. These observations provided a rationale for additional investigation. Accordingly, subsequent virtual screening, molecular docking, molecular dynamics simulation, and recombinant-TGFB3 perturbation experiments were performed as exploratory analyses to evaluate structural plausibility and cellular responses associated with TGFB3 exposure.
    Figure Legend Snippet: Multiplex immunofluorescence validation of hub gene expression in the gastric cancer tumor microenvironment. (A) Representative staining of BMP4 (red) and Pan-CK (green) in gastric cancer showing predominant localization of BMP4 to Pan-CK + tumor epithelial nests. (B) CD248 (red) colocalizes with FAP + cancer-associated fibroblasts (CAF; green) within the stromal compartment. (C) TGFB3 (red) is enriched in the FAP + CAF-rich stroma. (D) LGR4 (red) is detected both in FAP + CAFs (green) and in Pan-CK + tumor epithelial cells (yellow). (E) MGP (red) is present in CD31 + endothelial structures (yellow) and in FAP + CAF-rich stromal regions (green). Nuclei are counterstained with DAPI (blue). Left panels show merged images; right panels display the corresponding single-channel views. Scale bars, 100 μm. Integrating the proteome-wide MR screen with PPI topology, survival analysis, and compartment-resolved expression patterns, we prioritized ERBB3, LGR4, BMP4, CD248, MGP, TGFB3, GRP, and ETS2 as network-prioritized candidates for downstream contextualization. Among them, TGFB3 was selected for focused computational and cellular characterization on the basis of several convergent prioritization features, including its nominal MR association, network-topology ranking, association with overall survival, fibroblast-enriched expression pattern, and spatial organization in gastric cancer tissues. These observations provided a rationale for additional investigation. Accordingly, subsequent virtual screening, molecular docking, molecular dynamics simulation, and recombinant-TGFB3 perturbation experiments were performed as exploratory analyses to evaluate structural plausibility and cellular responses associated with TGFB3 exposure.

    Techniques Used: Multiplex Assay, Immunofluorescence, Biomarker Discovery, Gene Expression, Staining, Expressing, Recombinant

    Molecular docking of TGFB3 with candidate ligands. The left panel in each subfigure depicts the three-dimensional ligand orientation within the TGFB3 binding pocket; the right panel presents a two-dimensional interaction diagram, highlighting hydrogen bonds and hydrophobic contacts. (A) Docking pose of TGFB3 with proflavine hemisulfate. (B) Docking pose of TGFB3 with hydroxychloroquine sulfate. (C) Docking pose of TGFB3 with rizatriptan benzoate. (D) Docking pose of TGFB3 with L-histidine. (E) Docking pose of TGFB3 with retigabine. (F) Heatmap of binding affinities (kcal/mol) obtained from molecular docking analyses between TGFB3 and the five ligands (proflavine hemisulfate, hydroxychloroquine sulfate, rizatriptan benzoate, L-histidine and retigabine).
    Figure Legend Snippet: Molecular docking of TGFB3 with candidate ligands. The left panel in each subfigure depicts the three-dimensional ligand orientation within the TGFB3 binding pocket; the right panel presents a two-dimensional interaction diagram, highlighting hydrogen bonds and hydrophobic contacts. (A) Docking pose of TGFB3 with proflavine hemisulfate. (B) Docking pose of TGFB3 with hydroxychloroquine sulfate. (C) Docking pose of TGFB3 with rizatriptan benzoate. (D) Docking pose of TGFB3 with L-histidine. (E) Docking pose of TGFB3 with retigabine. (F) Heatmap of binding affinities (kcal/mol) obtained from molecular docking analyses between TGFB3 and the five ligands (proflavine hemisulfate, hydroxychloroquine sulfate, rizatriptan benzoate, L-histidine and retigabine).

    Techniques Used: Binding Assay

    Molecular dynamics analysis of the TGFB3–proflavine hemisulfate complex over 100 ns. (A) Temporal evolution of the RMSD of the protein–ligand complex. (B) Time-dependent changes in the overall Rg and its axis-specific components (Rg_x, Rg_y, Rg_z). (C) SASA as a function of simulation time. (D) Two-dimensional Gibbs free energy landscape derived from principal component analysis (PC1–PC2), with the color gradient indicating free energy magnitude (kJ/mol). (E) Covariance matrix heatmap of atomic motions, where color intensity reflects the strength and direction (positive or negative) of residue–residue correlations. (F) Three-dimensional Gibbs free energy surface and its projected contour map on the PC1/PC2 plane, visually depicting the energy distribution along the principal components.
    Figure Legend Snippet: Molecular dynamics analysis of the TGFB3–proflavine hemisulfate complex over 100 ns. (A) Temporal evolution of the RMSD of the protein–ligand complex. (B) Time-dependent changes in the overall Rg and its axis-specific components (Rg_x, Rg_y, Rg_z). (C) SASA as a function of simulation time. (D) Two-dimensional Gibbs free energy landscape derived from principal component analysis (PC1–PC2), with the color gradient indicating free energy magnitude (kJ/mol). (E) Covariance matrix heatmap of atomic motions, where color intensity reflects the strength and direction (positive or negative) of residue–residue correlations. (F) Three-dimensional Gibbs free energy surface and its projected contour map on the PC1/PC2 plane, visually depicting the energy distribution along the principal components.

    Techniques Used: Derivative Assay, Residue

    (A) NicheNet ligand–receptor analysis using fibroblasts as sender cells and epithelial cells as receiver cells, with TGFB3 specified as the ligand of interest. Candidate receptors associated with TGFB3 are displayed. (B) Scatter plot showing the relationship between TGFB3 and TGFBR2 expression. The Spearman correlation coefficient and corresponding P value are indicated in the panel. (C) Manifold-alignment plot generated after in silico knockout of TGFBR2 in epithelial cells using scTenifoldKnk. Each point represents one gene and selected genes are labeled. (D) Ranking of genes affected following virtual TGFBR2 knockout according to the perturbation statistics generated by scTenifoldKnk. (E) Functional enrichment analysis result of genes affected by virtual TGFBR2 knockout.
    Figure Legend Snippet: (A) NicheNet ligand–receptor analysis using fibroblasts as sender cells and epithelial cells as receiver cells, with TGFB3 specified as the ligand of interest. Candidate receptors associated with TGFB3 are displayed. (B) Scatter plot showing the relationship between TGFB3 and TGFBR2 expression. The Spearman correlation coefficient and corresponding P value are indicated in the panel. (C) Manifold-alignment plot generated after in silico knockout of TGFBR2 in epithelial cells using scTenifoldKnk. Each point represents one gene and selected genes are labeled. (D) Ranking of genes affected following virtual TGFBR2 knockout according to the perturbation statistics generated by scTenifoldKnk. (E) Functional enrichment analysis result of genes affected by virtual TGFBR2 knockout.

    Techniques Used: Expressing, Generated, In Silico, Knock-Out, Labeling, Functional Assay

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    Article Snippet: .. For experimental treatments, recombinant human TGF (transforming growth factor) β1 (MedChemExpress, P01137 ) was applied under standardized conditions (10 ng/mL). ..

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    Article Snippet: The lentivirus encoding miR-200a mimics or its negative control was purchased from the GenePharma (Shanghai, China). .. Recombinant human TGF- 1 was provided by the MedChemExpress (China). miR-200a mimics and the negative control (mimics NC), and miR-200a inhibitor and the negative control (inhibitor NC) were synthetized by the RiBoBio Co. (Guangzhou, China). .. Masson trichrome staining kit, DAB reagent and hematoxylin were obtained from the Solarbio (Beijing, China).

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    Image Search Results


    (A) Schematic of the multilayer perceptron with eight input nodes (BMP4, CD248, GRP, LGR4, MGP, TGFB3, ERBB3, ETS2), a five-node hidden layer and a two-node output layer encoding Control (normal) and Treatment (GC). (B) Receiver operating characteristic (ROC) curve and area under the curve (AUC) in the training cohort (TCGA-STAD). (C) ROC curve and AUC in the independent validation cohort ( GSE54129 ).

    Journal: Frontiers in Oncology

    Article Title: From proteome-wide Mendelian randomization and multi-omics integration to functional validation: TGFB3 as a prioritized candidate in gastric adenocarcinoma

    doi: 10.3389/fonc.2026.1883227

    Figure Lengend Snippet: (A) Schematic of the multilayer perceptron with eight input nodes (BMP4, CD248, GRP, LGR4, MGP, TGFB3, ERBB3, ETS2), a five-node hidden layer and a two-node output layer encoding Control (normal) and Treatment (GC). (B) Receiver operating characteristic (ROC) curve and area under the curve (AUC) in the training cohort (TCGA-STAD). (C) ROC curve and AUC in the independent validation cohort ( GSE54129 ).

    Article Snippet: Proflavine hemisulfate (purity > 98%, HY-B0883) and recombinant human TGFB3 (rhTGFB3; purity > 95% by reducing SDS–PAGE, HY-P700152AF) were purchased from MedChemExpress (NJ, USA).

    Techniques: Control, Biomarker Discovery

    Kaplan–Meier analysis of OS in gastric cancer patients stratified by mRNA expression of network-prioritized genes: (A) BMP4, (B) CD248, (C) GRP, (D) LGR4, (E) MGP, (F) TGFB3, (G) ERBB3 and (H) ETS2.

    Journal: Frontiers in Oncology

    Article Title: From proteome-wide Mendelian randomization and multi-omics integration to functional validation: TGFB3 as a prioritized candidate in gastric adenocarcinoma

    doi: 10.3389/fonc.2026.1883227

    Figure Lengend Snippet: Kaplan–Meier analysis of OS in gastric cancer patients stratified by mRNA expression of network-prioritized genes: (A) BMP4, (B) CD248, (C) GRP, (D) LGR4, (E) MGP, (F) TGFB3, (G) ERBB3 and (H) ETS2.

    Article Snippet: Proflavine hemisulfate (purity > 98%, HY-B0883) and recombinant human TGFB3 (rhTGFB3; purity > 95% by reducing SDS–PAGE, HY-P700152AF) were purchased from MedChemExpress (NJ, USA).

    Techniques: Expressing

    Multiplex immunofluorescence validation of hub gene expression in the gastric cancer tumor microenvironment. (A) Representative staining of BMP4 (red) and Pan-CK (green) in gastric cancer showing predominant localization of BMP4 to Pan-CK + tumor epithelial nests. (B) CD248 (red) colocalizes with FAP + cancer-associated fibroblasts (CAF; green) within the stromal compartment. (C) TGFB3 (red) is enriched in the FAP + CAF-rich stroma. (D) LGR4 (red) is detected both in FAP + CAFs (green) and in Pan-CK + tumor epithelial cells (yellow). (E) MGP (red) is present in CD31 + endothelial structures (yellow) and in FAP + CAF-rich stromal regions (green). Nuclei are counterstained with DAPI (blue). Left panels show merged images; right panels display the corresponding single-channel views. Scale bars, 100 μm. Integrating the proteome-wide MR screen with PPI topology, survival analysis, and compartment-resolved expression patterns, we prioritized ERBB3, LGR4, BMP4, CD248, MGP, TGFB3, GRP, and ETS2 as network-prioritized candidates for downstream contextualization. Among them, TGFB3 was selected for focused computational and cellular characterization on the basis of several convergent prioritization features, including its nominal MR association, network-topology ranking, association with overall survival, fibroblast-enriched expression pattern, and spatial organization in gastric cancer tissues. These observations provided a rationale for additional investigation. Accordingly, subsequent virtual screening, molecular docking, molecular dynamics simulation, and recombinant-TGFB3 perturbation experiments were performed as exploratory analyses to evaluate structural plausibility and cellular responses associated with TGFB3 exposure.

    Journal: Frontiers in Oncology

    Article Title: From proteome-wide Mendelian randomization and multi-omics integration to functional validation: TGFB3 as a prioritized candidate in gastric adenocarcinoma

    doi: 10.3389/fonc.2026.1883227

    Figure Lengend Snippet: Multiplex immunofluorescence validation of hub gene expression in the gastric cancer tumor microenvironment. (A) Representative staining of BMP4 (red) and Pan-CK (green) in gastric cancer showing predominant localization of BMP4 to Pan-CK + tumor epithelial nests. (B) CD248 (red) colocalizes with FAP + cancer-associated fibroblasts (CAF; green) within the stromal compartment. (C) TGFB3 (red) is enriched in the FAP + CAF-rich stroma. (D) LGR4 (red) is detected both in FAP + CAFs (green) and in Pan-CK + tumor epithelial cells (yellow). (E) MGP (red) is present in CD31 + endothelial structures (yellow) and in FAP + CAF-rich stromal regions (green). Nuclei are counterstained with DAPI (blue). Left panels show merged images; right panels display the corresponding single-channel views. Scale bars, 100 μm. Integrating the proteome-wide MR screen with PPI topology, survival analysis, and compartment-resolved expression patterns, we prioritized ERBB3, LGR4, BMP4, CD248, MGP, TGFB3, GRP, and ETS2 as network-prioritized candidates for downstream contextualization. Among them, TGFB3 was selected for focused computational and cellular characterization on the basis of several convergent prioritization features, including its nominal MR association, network-topology ranking, association with overall survival, fibroblast-enriched expression pattern, and spatial organization in gastric cancer tissues. These observations provided a rationale for additional investigation. Accordingly, subsequent virtual screening, molecular docking, molecular dynamics simulation, and recombinant-TGFB3 perturbation experiments were performed as exploratory analyses to evaluate structural plausibility and cellular responses associated with TGFB3 exposure.

    Article Snippet: Proflavine hemisulfate (purity > 98%, HY-B0883) and recombinant human TGFB3 (rhTGFB3; purity > 95% by reducing SDS–PAGE, HY-P700152AF) were purchased from MedChemExpress (NJ, USA).

    Techniques: Multiplex Assay, Immunofluorescence, Biomarker Discovery, Gene Expression, Staining, Expressing, Recombinant

    Molecular docking of TGFB3 with candidate ligands. The left panel in each subfigure depicts the three-dimensional ligand orientation within the TGFB3 binding pocket; the right panel presents a two-dimensional interaction diagram, highlighting hydrogen bonds and hydrophobic contacts. (A) Docking pose of TGFB3 with proflavine hemisulfate. (B) Docking pose of TGFB3 with hydroxychloroquine sulfate. (C) Docking pose of TGFB3 with rizatriptan benzoate. (D) Docking pose of TGFB3 with L-histidine. (E) Docking pose of TGFB3 with retigabine. (F) Heatmap of binding affinities (kcal/mol) obtained from molecular docking analyses between TGFB3 and the five ligands (proflavine hemisulfate, hydroxychloroquine sulfate, rizatriptan benzoate, L-histidine and retigabine).

    Journal: Frontiers in Oncology

    Article Title: From proteome-wide Mendelian randomization and multi-omics integration to functional validation: TGFB3 as a prioritized candidate in gastric adenocarcinoma

    doi: 10.3389/fonc.2026.1883227

    Figure Lengend Snippet: Molecular docking of TGFB3 with candidate ligands. The left panel in each subfigure depicts the three-dimensional ligand orientation within the TGFB3 binding pocket; the right panel presents a two-dimensional interaction diagram, highlighting hydrogen bonds and hydrophobic contacts. (A) Docking pose of TGFB3 with proflavine hemisulfate. (B) Docking pose of TGFB3 with hydroxychloroquine sulfate. (C) Docking pose of TGFB3 with rizatriptan benzoate. (D) Docking pose of TGFB3 with L-histidine. (E) Docking pose of TGFB3 with retigabine. (F) Heatmap of binding affinities (kcal/mol) obtained from molecular docking analyses between TGFB3 and the five ligands (proflavine hemisulfate, hydroxychloroquine sulfate, rizatriptan benzoate, L-histidine and retigabine).

    Article Snippet: Proflavine hemisulfate (purity > 98%, HY-B0883) and recombinant human TGFB3 (rhTGFB3; purity > 95% by reducing SDS–PAGE, HY-P700152AF) were purchased from MedChemExpress (NJ, USA).

    Techniques: Binding Assay

    Molecular dynamics analysis of the TGFB3–proflavine hemisulfate complex over 100 ns. (A) Temporal evolution of the RMSD of the protein–ligand complex. (B) Time-dependent changes in the overall Rg and its axis-specific components (Rg_x, Rg_y, Rg_z). (C) SASA as a function of simulation time. (D) Two-dimensional Gibbs free energy landscape derived from principal component analysis (PC1–PC2), with the color gradient indicating free energy magnitude (kJ/mol). (E) Covariance matrix heatmap of atomic motions, where color intensity reflects the strength and direction (positive or negative) of residue–residue correlations. (F) Three-dimensional Gibbs free energy surface and its projected contour map on the PC1/PC2 plane, visually depicting the energy distribution along the principal components.

    Journal: Frontiers in Oncology

    Article Title: From proteome-wide Mendelian randomization and multi-omics integration to functional validation: TGFB3 as a prioritized candidate in gastric adenocarcinoma

    doi: 10.3389/fonc.2026.1883227

    Figure Lengend Snippet: Molecular dynamics analysis of the TGFB3–proflavine hemisulfate complex over 100 ns. (A) Temporal evolution of the RMSD of the protein–ligand complex. (B) Time-dependent changes in the overall Rg and its axis-specific components (Rg_x, Rg_y, Rg_z). (C) SASA as a function of simulation time. (D) Two-dimensional Gibbs free energy landscape derived from principal component analysis (PC1–PC2), with the color gradient indicating free energy magnitude (kJ/mol). (E) Covariance matrix heatmap of atomic motions, where color intensity reflects the strength and direction (positive or negative) of residue–residue correlations. (F) Three-dimensional Gibbs free energy surface and its projected contour map on the PC1/PC2 plane, visually depicting the energy distribution along the principal components.

    Article Snippet: Proflavine hemisulfate (purity > 98%, HY-B0883) and recombinant human TGFB3 (rhTGFB3; purity > 95% by reducing SDS–PAGE, HY-P700152AF) were purchased from MedChemExpress (NJ, USA).

    Techniques: Derivative Assay, Residue

    (A) NicheNet ligand–receptor analysis using fibroblasts as sender cells and epithelial cells as receiver cells, with TGFB3 specified as the ligand of interest. Candidate receptors associated with TGFB3 are displayed. (B) Scatter plot showing the relationship between TGFB3 and TGFBR2 expression. The Spearman correlation coefficient and corresponding P value are indicated in the panel. (C) Manifold-alignment plot generated after in silico knockout of TGFBR2 in epithelial cells using scTenifoldKnk. Each point represents one gene and selected genes are labeled. (D) Ranking of genes affected following virtual TGFBR2 knockout according to the perturbation statistics generated by scTenifoldKnk. (E) Functional enrichment analysis result of genes affected by virtual TGFBR2 knockout.

    Journal: Frontiers in Oncology

    Article Title: From proteome-wide Mendelian randomization and multi-omics integration to functional validation: TGFB3 as a prioritized candidate in gastric adenocarcinoma

    doi: 10.3389/fonc.2026.1883227

    Figure Lengend Snippet: (A) NicheNet ligand–receptor analysis using fibroblasts as sender cells and epithelial cells as receiver cells, with TGFB3 specified as the ligand of interest. Candidate receptors associated with TGFB3 are displayed. (B) Scatter plot showing the relationship between TGFB3 and TGFBR2 expression. The Spearman correlation coefficient and corresponding P value are indicated in the panel. (C) Manifold-alignment plot generated after in silico knockout of TGFBR2 in epithelial cells using scTenifoldKnk. Each point represents one gene and selected genes are labeled. (D) Ranking of genes affected following virtual TGFBR2 knockout according to the perturbation statistics generated by scTenifoldKnk. (E) Functional enrichment analysis result of genes affected by virtual TGFBR2 knockout.

    Article Snippet: Proflavine hemisulfate (purity > 98%, HY-B0883) and recombinant human TGFB3 (rhTGFB3; purity > 95% by reducing SDS–PAGE, HY-P700152AF) were purchased from MedChemExpress (NJ, USA).

    Techniques: Expressing, Generated, In Silico, Knock-Out, Labeling, Functional Assay

    Exercise modulates TGF-β1 expression in the prefrontal cortex (PFC) of mice 24 days after spared nerve injury (SNI). (a) Representative Western blot images of TGF-β receptor I (TGF-βR1) and TGF-β1 in the PFC. Tissue lysates from all experimental groups (SHAM, SHAME, SNI, SNIE) and recombinant human TGF-β1 (non-reduced and reduced) were loaded on the same SDS–PAGE gel, transferred to a single membrane, and probed with the same TGF-β1 antibody under identical exposure conditions. The recombinant protein (250 ng per lane) served as a positive control to verify the molecular weights of the dimeric (25 kDa) and monomeric (12.5 kDa) forms of TGF-β1. GAPDH was used as the loading control. (b-d) Quantitative Western blot analyses of (b) TGF-βR1, (c) dimeric TGF-β1 (25 kDa), and (d) monomeric TGF-β1 (12.5 kDa) expression levels in tissue lysates. Data are presented as mean ± SEM (n = 3). ** P < 0.01 vs. SHAM group; ## P < 0.01 vs. SNI group.

    Journal: IBRO Neuroscience Reports

    Article Title: TGF-β1 modulates PFC glial cell activation to facilitate exercise-induced analgesia in mice with spared nerve injury

    doi: 10.1016/j.ibneur.2026.03.009

    Figure Lengend Snippet: Exercise modulates TGF-β1 expression in the prefrontal cortex (PFC) of mice 24 days after spared nerve injury (SNI). (a) Representative Western blot images of TGF-β receptor I (TGF-βR1) and TGF-β1 in the PFC. Tissue lysates from all experimental groups (SHAM, SHAME, SNI, SNIE) and recombinant human TGF-β1 (non-reduced and reduced) were loaded on the same SDS–PAGE gel, transferred to a single membrane, and probed with the same TGF-β1 antibody under identical exposure conditions. The recombinant protein (250 ng per lane) served as a positive control to verify the molecular weights of the dimeric (25 kDa) and monomeric (12.5 kDa) forms of TGF-β1. GAPDH was used as the loading control. (b-d) Quantitative Western blot analyses of (b) TGF-βR1, (c) dimeric TGF-β1 (25 kDa), and (d) monomeric TGF-β1 (12.5 kDa) expression levels in tissue lysates. Data are presented as mean ± SEM (n = 3). ** P < 0.01 vs. SHAM group; ## P < 0.01 vs. SNI group.

    Article Snippet: To validate the specificity of the TGF-β1 antibody, Recombinant human TGF-β1 protein (Catalog # 240-B, R&D Systems, USA) was used as a positive control.

    Techniques: Expressing, Western Blot, Recombinant, SDS Page, Membrane, Positive Control, Control

    At 24 d after SNI, mouse PFC astrocytes were activated and microglia were unchanged. (a)Western blotting analysis of changes in GFAP and Iba1 expression in PFC (n = 3); (b) Quantification of GFAP in PFC; (c) Quantification of Iba1 in PFC; (d) MFI representative images of GFAP in PFC; (e) MFI representative image of Iba1 in PFC; (f) Quantification of GFAP in PFC. Values represent mean ± SEM (Scale bar =75μm, 9 PFC sections from 3 mice per group); (g) Quantification of Iba1 in PFC. Values represent mean ±SEM (Scale bar = 75μm, 9 PFC sections from 3 mice per group). Values represent the mean ±SEM. * P < 0.05, ** P < 0.01, compared with SHAM group; # P < 0.05, ## P < 0.01, compared with SNI group, the difference was statistically significant; (h) Representative MFI images of changes in the colocalization of TGF-β1(red) and astrocytes (green) in the PFC; (i) Quantification of TGF-β1 and astrocytes in PFC. Values represent the mean ± SEM (Scale bar =100μm, nine PFC sections from three mice per group). * P < 0.05 versus the SHAM group; # P < 0.05 versus the SNI group.

    Journal: IBRO Neuroscience Reports

    Article Title: TGF-β1 modulates PFC glial cell activation to facilitate exercise-induced analgesia in mice with spared nerve injury

    doi: 10.1016/j.ibneur.2026.03.009

    Figure Lengend Snippet: At 24 d after SNI, mouse PFC astrocytes were activated and microglia were unchanged. (a)Western blotting analysis of changes in GFAP and Iba1 expression in PFC (n = 3); (b) Quantification of GFAP in PFC; (c) Quantification of Iba1 in PFC; (d) MFI representative images of GFAP in PFC; (e) MFI representative image of Iba1 in PFC; (f) Quantification of GFAP in PFC. Values represent mean ± SEM (Scale bar =75μm, 9 PFC sections from 3 mice per group); (g) Quantification of Iba1 in PFC. Values represent mean ±SEM (Scale bar = 75μm, 9 PFC sections from 3 mice per group). Values represent the mean ±SEM. * P < 0.05, ** P < 0.01, compared with SHAM group; # P < 0.05, ## P < 0.01, compared with SNI group, the difference was statistically significant; (h) Representative MFI images of changes in the colocalization of TGF-β1(red) and astrocytes (green) in the PFC; (i) Quantification of TGF-β1 and astrocytes in PFC. Values represent the mean ± SEM (Scale bar =100μm, nine PFC sections from three mice per group). * P < 0.05 versus the SHAM group; # P < 0.05 versus the SNI group.

    Article Snippet: To validate the specificity of the TGF-β1 antibody, Recombinant human TGF-β1 protein (Catalog # 240-B, R&D Systems, USA) was used as a positive control.

    Techniques: Western Blot, Expressing

    TGF-βRI inhibition reverses exercise-induced analgesia and modulates glial activation in the PFC. (a, b) Time course of mechanical and cold hyperalgesia tests (n = 9). The green shading indicates the duration of the exercise intervention, and the green vertical lines denote the timing of intrathecal injections. Data are presented as mean ± SEM. ** P < 0.01 versus the SNIE group, # P < 0.05, ## P < 0.01 vs. SC group. (c) Representative Western blot images of TGF-βR1 and TGF-β1 in the PFC. Tissue lysates from SC and SA groups and recombinant human TGF-β1 (100 ng per lane) (non-reduced and reduced) were loaded on the same SDS–PAGE gel, transferred to a single membrane, and probed with the same TGF-β1 antibody in a single exposure without splicing. The recombinant protein served as a positive control to verify the molecular weights of the dimeric (25 kDa) and monomeric (12.5 kDa) forms of TGF-β1. GAPDH was used as the loading control. (d-f) Quantitative analysis of (d) TGF-βR1, (e) dimeric TGF-β1 (25 kDa), and (f) monomeric TGF-β1 (12.5 kDa) expression levels (n = 3). (g-i) Western blot analysis of glial markers. (g) Representative images of GFAP and Iba1 with GAPDH control. Quantitative analysis of (h) GFAP and (i) Iba1 expression levels (n = 3). (j, k) Representative immunofluorescence images showing the expression of (j) GFAP and (k) Iba1 in the PFC. Scale bar = 75 μm. (l, m) Quantification of the mean fluorescence intensity (MFI) for (l) GFAP and (m) Iba1 (n = 9 sections from 3 mice per group). Data in bar graphs are presented as mean ± SEM. * P < 0.05, ** P < 0.01 vs. SC group. SC: Spared nerve injury with exercise training followed by intrathecal (i.t.) injection of saline; SA: Spared nerve injury with exercise training followed by i.t. injection of the TGF-βRI inhibitor.

    Journal: IBRO Neuroscience Reports

    Article Title: TGF-β1 modulates PFC glial cell activation to facilitate exercise-induced analgesia in mice with spared nerve injury

    doi: 10.1016/j.ibneur.2026.03.009

    Figure Lengend Snippet: TGF-βRI inhibition reverses exercise-induced analgesia and modulates glial activation in the PFC. (a, b) Time course of mechanical and cold hyperalgesia tests (n = 9). The green shading indicates the duration of the exercise intervention, and the green vertical lines denote the timing of intrathecal injections. Data are presented as mean ± SEM. ** P < 0.01 versus the SNIE group, # P < 0.05, ## P < 0.01 vs. SC group. (c) Representative Western blot images of TGF-βR1 and TGF-β1 in the PFC. Tissue lysates from SC and SA groups and recombinant human TGF-β1 (100 ng per lane) (non-reduced and reduced) were loaded on the same SDS–PAGE gel, transferred to a single membrane, and probed with the same TGF-β1 antibody in a single exposure without splicing. The recombinant protein served as a positive control to verify the molecular weights of the dimeric (25 kDa) and monomeric (12.5 kDa) forms of TGF-β1. GAPDH was used as the loading control. (d-f) Quantitative analysis of (d) TGF-βR1, (e) dimeric TGF-β1 (25 kDa), and (f) monomeric TGF-β1 (12.5 kDa) expression levels (n = 3). (g-i) Western blot analysis of glial markers. (g) Representative images of GFAP and Iba1 with GAPDH control. Quantitative analysis of (h) GFAP and (i) Iba1 expression levels (n = 3). (j, k) Representative immunofluorescence images showing the expression of (j) GFAP and (k) Iba1 in the PFC. Scale bar = 75 μm. (l, m) Quantification of the mean fluorescence intensity (MFI) for (l) GFAP and (m) Iba1 (n = 9 sections from 3 mice per group). Data in bar graphs are presented as mean ± SEM. * P < 0.05, ** P < 0.01 vs. SC group. SC: Spared nerve injury with exercise training followed by intrathecal (i.t.) injection of saline; SA: Spared nerve injury with exercise training followed by i.t. injection of the TGF-βRI inhibitor.

    Article Snippet: To validate the specificity of the TGF-β1 antibody, Recombinant human TGF-β1 protein (Catalog # 240-B, R&D Systems, USA) was used as a positive control.

    Techniques: Inhibition, Activation Assay, Western Blot, Recombinant, SDS Page, Membrane, Positive Control, Control, Expressing, Immunofluorescence, Fluorescence, Injection, Saline