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recombinant human tgf β1 protein  (R&D Systems)


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    R&D Systems recombinant human tgf β1 protein
    Exercise <t>modulates</t> <t>TGF-β1</t> 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.
    Recombinant Human Tgf β1 Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 97/100, based on 1985 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+human+tgf+%CE%B21+protein/Recombinant+Human+TGF-beta+1+Protein/pmc13054092-88-8-15
    Average 97 stars, based on 1985 article reviews
    recombinant human tgf β1 protein - by Bioz Stars, 2026-09
    97/100 stars

    Images

    1) Product Images from "TGF-β1 modulates PFC glial cell activation to facilitate exercise-induced analgesia in mice with spared nerve injury"

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

    Journal: IBRO Neuroscience Reports

    doi: 10.1016/j.ibneur.2026.03.009

    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.
    Figure Legend 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.

    Techniques Used: 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.
    Figure Legend 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.

    Techniques Used: 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.
    Figure Legend 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.

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

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    Sterility:

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    Fibrotic changes and increased Krt20 expression in mice after UUO modeling. ( A, B ) Transcriptomic sequencing data from public databases indicate upregulation of Krt20 expression following UUO modeling. ( C ) Expression of EMT-related genes during fibrosis. ( D, E ) Schematic of experimental design: in vivo UUO mouse modeling and in vitro TGF-β1 stimulation of HK2 cells. ( F ) Representative images of H&E, Masson’s trichrome, Sirius red, Krt20 IHC, and TUNEL staining. ( G-I ) Quantitative analysis of Masson’s trichrome, Sirius red staining, TUNEL-positive nuclei, and IHC. ( K, L ) Serum creatinine and blood urea nitrogen (BUN) levels in UUO model mice. ( M ) Increased Krt20 expression in UUO model. ( N, O ) mRNA and protein level changes of Krt20 in UUO model. * p < 0.05, ** p < 0.01, *** p < 0.001 compared to the indicated group

    Journal: Biology Direct

    Article Title: JUNB transcriptional regulation of KRT20 via ITGB1 activates PI3K/AKT signaling pathway against fibrosis-induced by renal injury

    doi: 10.1186/s13062-026-00804-5

    Figure Lengend Snippet: Fibrotic changes and increased Krt20 expression in mice after UUO modeling. ( A, B ) Transcriptomic sequencing data from public databases indicate upregulation of Krt20 expression following UUO modeling. ( C ) Expression of EMT-related genes during fibrosis. ( D, E ) Schematic of experimental design: in vivo UUO mouse modeling and in vitro TGF-β1 stimulation of HK2 cells. ( F ) Representative images of H&E, Masson’s trichrome, Sirius red, Krt20 IHC, and TUNEL staining. ( G-I ) Quantitative analysis of Masson’s trichrome, Sirius red staining, TUNEL-positive nuclei, and IHC. ( K, L ) Serum creatinine and blood urea nitrogen (BUN) levels in UUO model mice. ( M ) Increased Krt20 expression in UUO model. ( N, O ) mRNA and protein level changes of Krt20 in UUO model. * p < 0.05, ** p < 0.01, *** p < 0.001 compared to the indicated group

    Article Snippet: Recombinant human mature TGF-β1 protein was purchased from MedChemExpress (MCE, TGF beta 1/TGFB1 Protein, Human, HEK293).

    Techniques: Expressing, Sequencing, In Vivo, In Vitro, TUNEL Assay, Staining

    Induction of renal fibrosis in HK2 cells stimulated with TGF-β1. ( A ) Changes in mRNA levels of fibrosis markers in HK2 cells stimulated with TGF-β1. ( B, C ) Changes in protein levels of fibrosis markers in HK2 cells stimulated with TGF-β1. ( D ) Immunofluorescence staining shows upregulated expression of fibrosis-related proteins and increased KRT20 expression after TGF-β1 stimulation. ( E ) Relative fluorescence intensity of immunofluorescence staining. ( F, G ) Expression of proteins associated with epithelial-mesenchymal transition (EMT) under TGF-β1 stimulation. ( H-J ) mRNA and protein expression levels of KRT20 in HK2 cells after TGF-β1 stimulation. ( K-M ) Construction of HK2 cell lines with KRT20 knockdown via siRNA, showing mRNA ( K ) and protein ( L, M ) levels. ( N, O ) aggravated EMT observed in TGF-β1-stimulated HK2 cells following KRT20 knockdown, with panel ( O ) Representing the corresponding quantitative expression. The numbers above the bars in Figure Oindicate statistically significant differences ( p < 0.05) between experimental groups. The groups were numbered sequentially from left to right as 1 to 4. Each number above a bar represents the group number with which that bar shows a statistically significant difference. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared to the indicated group

    Journal: Biology Direct

    Article Title: JUNB transcriptional regulation of KRT20 via ITGB1 activates PI3K/AKT signaling pathway against fibrosis-induced by renal injury

    doi: 10.1186/s13062-026-00804-5

    Figure Lengend Snippet: Induction of renal fibrosis in HK2 cells stimulated with TGF-β1. ( A ) Changes in mRNA levels of fibrosis markers in HK2 cells stimulated with TGF-β1. ( B, C ) Changes in protein levels of fibrosis markers in HK2 cells stimulated with TGF-β1. ( D ) Immunofluorescence staining shows upregulated expression of fibrosis-related proteins and increased KRT20 expression after TGF-β1 stimulation. ( E ) Relative fluorescence intensity of immunofluorescence staining. ( F, G ) Expression of proteins associated with epithelial-mesenchymal transition (EMT) under TGF-β1 stimulation. ( H-J ) mRNA and protein expression levels of KRT20 in HK2 cells after TGF-β1 stimulation. ( K-M ) Construction of HK2 cell lines with KRT20 knockdown via siRNA, showing mRNA ( K ) and protein ( L, M ) levels. ( N, O ) aggravated EMT observed in TGF-β1-stimulated HK2 cells following KRT20 knockdown, with panel ( O ) Representing the corresponding quantitative expression. The numbers above the bars in Figure Oindicate statistically significant differences ( p < 0.05) between experimental groups. The groups were numbered sequentially from left to right as 1 to 4. Each number above a bar represents the group number with which that bar shows a statistically significant difference. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared to the indicated group

    Article Snippet: Recombinant human mature TGF-β1 protein was purchased from MedChemExpress (MCE, TGF beta 1/TGFB1 Protein, Human, HEK293).

    Techniques: Immunofluorescence, Staining, Expressing, Fluorescence, Knockdown

    Transcriptional regulation of KRT20 by JUNB. ( A ) Identification of candidate transcription factors via intersection analysis of predictions from bulk RNA sequencing, single-cell RNA sequencing data, and the JASPAR database. ( B, C ) UMAP visualization depicting cell cluster identities derived from the GSE175412 UUO single-cell RNA sequencing dataset. ( D ) Comparative expression analysis of JUNB in bulk tissue and single-cell transcriptomic profiles. ( E ) Annotation of cell clusters based on marker gene expression from single-cell RNA sequencing. ( F ) Spatial expression pattern of JUNB across different cell clusters in the single-cell dataset. ( G ) Subpopulation-specific expression of Junb within renal tubular epithelial cells. ( H-J ) Induction of JUNB expression in HK2 cells following TGF-β1 stimulation. Bar graphs quantify the upregulation at the mRNA ( H ) and protein ( I, J ) levels. * p < 0.05, ** p < 0.01, *** p < 0.001 compared to the indicated group

    Journal: Biology Direct

    Article Title: JUNB transcriptional regulation of KRT20 via ITGB1 activates PI3K/AKT signaling pathway against fibrosis-induced by renal injury

    doi: 10.1186/s13062-026-00804-5

    Figure Lengend Snippet: Transcriptional regulation of KRT20 by JUNB. ( A ) Identification of candidate transcription factors via intersection analysis of predictions from bulk RNA sequencing, single-cell RNA sequencing data, and the JASPAR database. ( B, C ) UMAP visualization depicting cell cluster identities derived from the GSE175412 UUO single-cell RNA sequencing dataset. ( D ) Comparative expression analysis of JUNB in bulk tissue and single-cell transcriptomic profiles. ( E ) Annotation of cell clusters based on marker gene expression from single-cell RNA sequencing. ( F ) Spatial expression pattern of JUNB across different cell clusters in the single-cell dataset. ( G ) Subpopulation-specific expression of Junb within renal tubular epithelial cells. ( H-J ) Induction of JUNB expression in HK2 cells following TGF-β1 stimulation. Bar graphs quantify the upregulation at the mRNA ( H ) and protein ( I, J ) levels. * p < 0.05, ** p < 0.01, *** p < 0.001 compared to the indicated group

    Article Snippet: Recombinant human mature TGF-β1 protein was purchased from MedChemExpress (MCE, TGF beta 1/TGFB1 Protein, Human, HEK293).

    Techniques: RNA Sequencing, Single Cell, Derivative Assay, Expressing, Marker, Gene Expression

    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