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Bioss β actin
FRA1 expression in MRL/lpr mouse kidneys. Representative H&E staining of kidney sections from 20-week-old (A) MRL/lpr mice and (B) MRL/MPJ controls, showing tubulointerstitial inflammation and damage in MRL/lpr mice. MRL/lpr mice exhibit diffuse and extensive tubulointerstitial inflammation and structural damage. (C-H) FRA1 expression in mouse kidney sections. (C, E and G) Three independent mice from the MRL/lpr group, all demonstrating elevated FRA1 levels in the tubular epithelium. (D, F and H) Three independent mice from the control group, displaying baseline FRA1 immunoreactivity. (I) Quantification of FRA1-positive area from IHC images. (J) Western blot analysis of FRA1 protein levels from MRL/lpr and control mice. (K) Densitometric quantification of FRA1 bands normalized to <t>β-actin.</t> Scale bar, 50 µm; Data are plotted as the mean ± SEM; n=3 per group; group comparisons were performed using two-sided Welch's t-tests; ***P<0.001.
β Actin, supplied by Bioss, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech anti β actin
FRA1 expression in MRL/lpr mouse kidneys. Representative H&E staining of kidney sections from 20-week-old (A) MRL/lpr mice and (B) MRL/MPJ controls, showing tubulointerstitial inflammation and damage in MRL/lpr mice. MRL/lpr mice exhibit diffuse and extensive tubulointerstitial inflammation and structural damage. (C-H) FRA1 expression in mouse kidney sections. (C, E and G) Three independent mice from the MRL/lpr group, all demonstrating elevated FRA1 levels in the tubular epithelium. (D, F and H) Three independent mice from the control group, displaying baseline FRA1 immunoreactivity. (I) Quantification of FRA1-positive area from IHC images. (J) Western blot analysis of FRA1 protein levels from MRL/lpr and control mice. (K) Densitometric quantification of FRA1 bands normalized to <t>β-actin.</t> Scale bar, 50 µm; Data are plotted as the mean ± SEM; n=3 per group; group comparisons were performed using two-sided Welch's t-tests; ***P<0.001.
Anti β Actin, supplied by Proteintech, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech rabbit anti integrin β1
FRA1 expression in MRL/lpr mouse kidneys. Representative H&E staining of kidney sections from 20-week-old (A) MRL/lpr mice and (B) MRL/MPJ controls, showing tubulointerstitial inflammation and damage in MRL/lpr mice. MRL/lpr mice exhibit diffuse and extensive tubulointerstitial inflammation and structural damage. (C-H) FRA1 expression in mouse kidney sections. (C, E and G) Three independent mice from the MRL/lpr group, all demonstrating elevated FRA1 levels in the tubular epithelium. (D, F and H) Three independent mice from the control group, displaying baseline FRA1 immunoreactivity. (I) Quantification of FRA1-positive area from IHC images. (J) Western blot analysis of FRA1 protein levels from MRL/lpr and control mice. (K) Densitometric quantification of FRA1 bands normalized to <t>β-actin.</t> Scale bar, 50 µm; Data are plotted as the mean ± SEM; n=3 per group; group comparisons were performed using two-sided Welch's t-tests; ***P<0.001.
Rabbit Anti Integrin β1, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech β catenin
MXMoS 2 activates Wnt signaling pathways to promote osteogenic differentiation and enhance bone regeneration. (A) GO pathway enrichment analysis of differentially expressed genes between the experimental and control groups. (B) KEGG pathway enrichment analysis of differentially expressed genes between the experimental and control groups. (C) Heatmap of inflammation-related gene expression. (D) GSEA of GO analysis in the experimental and control groups, demonstrating pathways such as osteoblast differentiation, regulation of macrophage activation, cell adhesion, positive regulation of cell migration,cell-cell junction. (E) PPI analyses identifying four distinct gene clusters (modules). (F) Bubble chart showed the various network topology metrics for the 4 modules weighted and quantified to obtain an overall score. (G) GO analysis of the genes in module 2 showed that they are associated with osteoblast differentiation and the Wnt signaling pathway. (H) Box plot of representative Wnt signaling pathway genes significantly upregulated in the MXMoS 2 group. (I) The six genes mentioned above were predicted for their upstream transcription factor regulation. (J) Schematic illustration of the mechanism of MXMoS 2 regulating macrophage polarization. (K) Representative Western blot images of WNT4 <t>and</t> <t>β-Catenin</t> expression in control group (LPS), MXMoS 2 group (LPS + MXMoS 2 ) and MXMoS 2 +siRNA group (LPS + MXMoS 2 +siRNA-WNT4). (L – M) Quantification of WNT4 and β-Catenin protein levels corresponding to (K) . ∗∗p < 0.01, ∗∗∗p < 0.001, and ∗∗∗∗p < 0.0001.
β Catenin, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech tgf β1
Smad3-OE reversed the fibrosis suppression resulting from RMST-KO. (A) QPCR confirmed the upregulating effect of Smad3-OE lentivirus. (B) Representative blot of Smad3 under the effect of Smad3-OE and/or RMST-KO. (C) Statistical analysis of the immunoblot bands. (D) H&E and Masson staining of the wounds as indicated. (E–F) Statistical analysis of the (E) thickness and (F) area of neogenic fibrous tissue 21 dps. (G–I) qPCR detection of fibrosis markers and proteins in classical fibrosis pathways, including COL1, α-SMA, and <t>TGF-β1.</t> (J–M). Representative blot of COL1, α-SMA, and TGF-β1. (N–O) qPCR detection of inflammatory cytokines TNF-α and IL-1β. (P–R) Representative blot of TNF-α and IL-1β. Data were shown as mean ± SD, n = 6, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
Tgf β1, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech β actin
Smad3-OE reversed the fibrosis suppression resulting from RMST-KO. (A) QPCR confirmed the upregulating effect of Smad3-OE lentivirus. (B) Representative blot of Smad3 under the effect of Smad3-OE and/or RMST-KO. (C) Statistical analysis of the immunoblot bands. (D) H&E and Masson staining of the wounds as indicated. (E–F) Statistical analysis of the (E) thickness and (F) area of neogenic fibrous tissue 21 dps. (G–I) qPCR detection of fibrosis markers and proteins in classical fibrosis pathways, including COL1, α-SMA, and <t>TGF-β1.</t> (J–M). Representative blot of COL1, α-SMA, and TGF-β1. (N–O) qPCR detection of inflammatory cytokines TNF-α and IL-1β. (P–R) Representative blot of TNF-α and IL-1β. Data were shown as mean ± SD, n = 6, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
β Actin, supplied by Proteintech, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech il 1β
RMST-KO reduces fibrosis in mouse skin wound healing. (A) Differences of RMST expression between unwounded skin and the 21 dps group. (B) Agarose gel electrophoresis confirmed the successful knockout of RMST. (C) QPCR assay showing the expression of RMST 21 dps. (D) H&E and Masson staining of the wounds 21 dps as indicated. (E–F) RMST-KO reduced the (E) thickness and (F) area of neogenic fibrous tissue at 21 dps. (G–H) QPCR showing the COL1A1 and α-SMA levels were significantly decreased in the RMST-KO group compared to the WT group 21 dps. (I) Representative blot of COL1A1 and α-SMA 21 dps. (J–K) Statistical analysis of the immunoblot bands indicated that RMST-KO significantly suppressed the expression of COL1A1 and α-SMA 21 dps. Data were shown as mean ± SD, n = 6, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
Il 1β, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech anti phospho β catenin ser33
RMST-KO reduces fibrosis in mouse skin wound healing. (A) Differences of RMST expression between unwounded skin and the 21 dps group. (B) Agarose gel electrophoresis confirmed the successful knockout of RMST. (C) QPCR assay showing the expression of RMST 21 dps. (D) H&E and Masson staining of the wounds 21 dps as indicated. (E–F) RMST-KO reduced the (E) thickness and (F) area of neogenic fibrous tissue at 21 dps. (G–H) QPCR showing the COL1A1 and α-SMA levels were significantly decreased in the RMST-KO group compared to the WT group 21 dps. (I) Representative blot of COL1A1 and α-SMA 21 dps. (J–K) Statistical analysis of the immunoblot bands indicated that RMST-KO significantly suppressed the expression of COL1A1 and α-SMA 21 dps. Data were shown as mean ± SD, n = 6, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
Anti Phospho β Catenin Ser33, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti phospho β catenin ser33 - by Bioz Stars, 2026-03
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Proteintech rabbit anti β actin
RMST-KO reduces fibrosis in mouse skin wound healing. (A) Differences of RMST expression between unwounded skin and the 21 dps group. (B) Agarose gel electrophoresis confirmed the successful knockout of RMST. (C) QPCR assay showing the expression of RMST 21 dps. (D) H&E and Masson staining of the wounds 21 dps as indicated. (E–F) RMST-KO reduced the (E) thickness and (F) area of neogenic fibrous tissue at 21 dps. (G–H) QPCR showing the COL1A1 and α-SMA levels were significantly decreased in the RMST-KO group compared to the WT group 21 dps. (I) Representative blot of COL1A1 and α-SMA 21 dps. (J–K) Statistical analysis of the immunoblot bands indicated that RMST-KO significantly suppressed the expression of COL1A1 and α-SMA 21 dps. Data were shown as mean ± SD, n = 6, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
Rabbit Anti β Actin, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


FRA1 expression in MRL/lpr mouse kidneys. Representative H&E staining of kidney sections from 20-week-old (A) MRL/lpr mice and (B) MRL/MPJ controls, showing tubulointerstitial inflammation and damage in MRL/lpr mice. MRL/lpr mice exhibit diffuse and extensive tubulointerstitial inflammation and structural damage. (C-H) FRA1 expression in mouse kidney sections. (C, E and G) Three independent mice from the MRL/lpr group, all demonstrating elevated FRA1 levels in the tubular epithelium. (D, F and H) Three independent mice from the control group, displaying baseline FRA1 immunoreactivity. (I) Quantification of FRA1-positive area from IHC images. (J) Western blot analysis of FRA1 protein levels from MRL/lpr and control mice. (K) Densitometric quantification of FRA1 bands normalized to β-actin. Scale bar, 50 µm; Data are plotted as the mean ± SEM; n=3 per group; group comparisons were performed using two-sided Welch's t-tests; ***P<0.001.

Journal: Molecular Medicine Reports

Article Title: Integrative bioinformatics and experimental analysis reveals FRA1 as a key mediator of tubulointerstitial inflammation in lupus nephritis

doi: 10.3892/mmr.2026.13813

Figure Lengend Snippet: FRA1 expression in MRL/lpr mouse kidneys. Representative H&E staining of kidney sections from 20-week-old (A) MRL/lpr mice and (B) MRL/MPJ controls, showing tubulointerstitial inflammation and damage in MRL/lpr mice. MRL/lpr mice exhibit diffuse and extensive tubulointerstitial inflammation and structural damage. (C-H) FRA1 expression in mouse kidney sections. (C, E and G) Three independent mice from the MRL/lpr group, all demonstrating elevated FRA1 levels in the tubular epithelium. (D, F and H) Three independent mice from the control group, displaying baseline FRA1 immunoreactivity. (I) Quantification of FRA1-positive area from IHC images. (J) Western blot analysis of FRA1 protein levels from MRL/lpr and control mice. (K) Densitometric quantification of FRA1 bands normalized to β-actin. Scale bar, 50 µm; Data are plotted as the mean ± SEM; n=3 per group; group comparisons were performed using two-sided Welch's t-tests; ***P<0.001.

Article Snippet: The primary antibodies used in the present study included: β-actin (1:5,000; cat. no. bs-0061R; BIOSS), FRA1 (1:1,000; cat. no. A5372; ABclonal Biotech Co., Ltd.), IL-1β (1:1,000; cat. no. HA601002 ; clone no. A7F9; HUABIO), IL-8 (1:1,000; cat. no. ab289967; clone no. EPR26511-74; Abcam), RANTES (1:1,000; cat. no. 36467; CST Biological Reagents Co., Ltd.), IL-6 (1:2,000; cat. no. DF6087; Affinity Biosciences, Ltd.), MCP-1 (1:2,000; cat. no. A7277; ABclonal Biotech Co., Ltd.), TNF-α (1:2,000; cat. no. 17590-1-AP; Proteintech Group, Inc.), and TGF-β (1:2,000; cat. no. 81746-2-RR; clone no. 230544B7; Proteintech Group, Inc.).

Techniques: Expressing, Staining, Control, Western Blot

Effect of FRA1 on inflammatory cytokine expression in HK-2 cells. (A) Representative western blots of FRA1 and inflammatory cytokines (IL-1β, IL-6, and IL-8) in HK-2 cells 144 h after transduction with FRA1-OE, FRA1-shRNA or their corresponding controls. (B) Representative western blots of MCP-1, RANTES, TGF-β and TNF-α in HK-2 cells following the same transduction conditions. Densitometric semi-quantification of protein bands normalized to β-actin for: (C) FRA1, (D) IL-1β, (E) IL-6, (F) IL-8, (G) MCP-1, (H) RANTES, (I) TGF-β and (J) TNF-α. Data are presented as the mean ± SEM; n=3 per group; comparisons among subgroups were assessed using the two-sided Kruskal-Wallis test; *P<0.05, **P<0.01 and ***P<0.001. OE, over expression; ns, not significant; sh, short hairpin.

Journal: Molecular Medicine Reports

Article Title: Integrative bioinformatics and experimental analysis reveals FRA1 as a key mediator of tubulointerstitial inflammation in lupus nephritis

doi: 10.3892/mmr.2026.13813

Figure Lengend Snippet: Effect of FRA1 on inflammatory cytokine expression in HK-2 cells. (A) Representative western blots of FRA1 and inflammatory cytokines (IL-1β, IL-6, and IL-8) in HK-2 cells 144 h after transduction with FRA1-OE, FRA1-shRNA or their corresponding controls. (B) Representative western blots of MCP-1, RANTES, TGF-β and TNF-α in HK-2 cells following the same transduction conditions. Densitometric semi-quantification of protein bands normalized to β-actin for: (C) FRA1, (D) IL-1β, (E) IL-6, (F) IL-8, (G) MCP-1, (H) RANTES, (I) TGF-β and (J) TNF-α. Data are presented as the mean ± SEM; n=3 per group; comparisons among subgroups were assessed using the two-sided Kruskal-Wallis test; *P<0.05, **P<0.01 and ***P<0.001. OE, over expression; ns, not significant; sh, short hairpin.

Article Snippet: The primary antibodies used in the present study included: β-actin (1:5,000; cat. no. bs-0061R; BIOSS), FRA1 (1:1,000; cat. no. A5372; ABclonal Biotech Co., Ltd.), IL-1β (1:1,000; cat. no. HA601002 ; clone no. A7F9; HUABIO), IL-8 (1:1,000; cat. no. ab289967; clone no. EPR26511-74; Abcam), RANTES (1:1,000; cat. no. 36467; CST Biological Reagents Co., Ltd.), IL-6 (1:2,000; cat. no. DF6087; Affinity Biosciences, Ltd.), MCP-1 (1:2,000; cat. no. A7277; ABclonal Biotech Co., Ltd.), TNF-α (1:2,000; cat. no. 17590-1-AP; Proteintech Group, Inc.), and TGF-β (1:2,000; cat. no. 81746-2-RR; clone no. 230544B7; Proteintech Group, Inc.).

Techniques: Expressing, Western Blot, Transduction, shRNA, Over Expression

MXMoS 2 activates Wnt signaling pathways to promote osteogenic differentiation and enhance bone regeneration. (A) GO pathway enrichment analysis of differentially expressed genes between the experimental and control groups. (B) KEGG pathway enrichment analysis of differentially expressed genes between the experimental and control groups. (C) Heatmap of inflammation-related gene expression. (D) GSEA of GO analysis in the experimental and control groups, demonstrating pathways such as osteoblast differentiation, regulation of macrophage activation, cell adhesion, positive regulation of cell migration,cell-cell junction. (E) PPI analyses identifying four distinct gene clusters (modules). (F) Bubble chart showed the various network topology metrics for the 4 modules weighted and quantified to obtain an overall score. (G) GO analysis of the genes in module 2 showed that they are associated with osteoblast differentiation and the Wnt signaling pathway. (H) Box plot of representative Wnt signaling pathway genes significantly upregulated in the MXMoS 2 group. (I) The six genes mentioned above were predicted for their upstream transcription factor regulation. (J) Schematic illustration of the mechanism of MXMoS 2 regulating macrophage polarization. (K) Representative Western blot images of WNT4 and β-Catenin expression in control group (LPS), MXMoS 2 group (LPS + MXMoS 2 ) and MXMoS 2 +siRNA group (LPS + MXMoS 2 +siRNA-WNT4). (L – M) Quantification of WNT4 and β-Catenin protein levels corresponding to (K) . ∗∗p < 0.01, ∗∗∗p < 0.001, and ∗∗∗∗p < 0.0001.

Journal: Bioactive Materials

Article Title: Bacteria-responsive DNAgel system for targeted delivery of photothermally enhanced MXene/MoS 2 in the treatment of pyogenic osteomyelitis

doi: 10.1016/j.bioactmat.2025.10.023

Figure Lengend Snippet: MXMoS 2 activates Wnt signaling pathways to promote osteogenic differentiation and enhance bone regeneration. (A) GO pathway enrichment analysis of differentially expressed genes between the experimental and control groups. (B) KEGG pathway enrichment analysis of differentially expressed genes between the experimental and control groups. (C) Heatmap of inflammation-related gene expression. (D) GSEA of GO analysis in the experimental and control groups, demonstrating pathways such as osteoblast differentiation, regulation of macrophage activation, cell adhesion, positive regulation of cell migration,cell-cell junction. (E) PPI analyses identifying four distinct gene clusters (modules). (F) Bubble chart showed the various network topology metrics for the 4 modules weighted and quantified to obtain an overall score. (G) GO analysis of the genes in module 2 showed that they are associated with osteoblast differentiation and the Wnt signaling pathway. (H) Box plot of representative Wnt signaling pathway genes significantly upregulated in the MXMoS 2 group. (I) The six genes mentioned above were predicted for their upstream transcription factor regulation. (J) Schematic illustration of the mechanism of MXMoS 2 regulating macrophage polarization. (K) Representative Western blot images of WNT4 and β-Catenin expression in control group (LPS), MXMoS 2 group (LPS + MXMoS 2 ) and MXMoS 2 +siRNA group (LPS + MXMoS 2 +siRNA-WNT4). (L – M) Quantification of WNT4 and β-Catenin protein levels corresponding to (K) . ∗∗p < 0.01, ∗∗∗p < 0.001, and ∗∗∗∗p < 0.0001.

Article Snippet: Primary antibodies for immunocytochemistry and immunofluorescence staining—including ARG1 and iNOS, TRAP, β-Catenin, OCN and WNT4—were obtained from Proteintech (China).

Techniques: Protein-Protein interactions, Control, Gene Expression, Activation Assay, Migration, Western Blot, Expressing

Smad3-OE reversed the fibrosis suppression resulting from RMST-KO. (A) QPCR confirmed the upregulating effect of Smad3-OE lentivirus. (B) Representative blot of Smad3 under the effect of Smad3-OE and/or RMST-KO. (C) Statistical analysis of the immunoblot bands. (D) H&E and Masson staining of the wounds as indicated. (E–F) Statistical analysis of the (E) thickness and (F) area of neogenic fibrous tissue 21 dps. (G–I) qPCR detection of fibrosis markers and proteins in classical fibrosis pathways, including COL1, α-SMA, and TGF-β1. (J–M). Representative blot of COL1, α-SMA, and TGF-β1. (N–O) qPCR detection of inflammatory cytokines TNF-α and IL-1β. (P–R) Representative blot of TNF-α and IL-1β. Data were shown as mean ± SD, n = 6, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Journal: Biochemistry and Biophysics Reports

Article Title: LncRNA RMST knockout inhibits fibrosis by down-regulating Smad3 during mouse skin wound healing

doi: 10.1016/j.bbrep.2025.102386

Figure Lengend Snippet: Smad3-OE reversed the fibrosis suppression resulting from RMST-KO. (A) QPCR confirmed the upregulating effect of Smad3-OE lentivirus. (B) Representative blot of Smad3 under the effect of Smad3-OE and/or RMST-KO. (C) Statistical analysis of the immunoblot bands. (D) H&E and Masson staining of the wounds as indicated. (E–F) Statistical analysis of the (E) thickness and (F) area of neogenic fibrous tissue 21 dps. (G–I) qPCR detection of fibrosis markers and proteins in classical fibrosis pathways, including COL1, α-SMA, and TGF-β1. (J–M). Representative blot of COL1, α-SMA, and TGF-β1. (N–O) qPCR detection of inflammatory cytokines TNF-α and IL-1β. (P–R) Representative blot of TNF-α and IL-1β. Data were shown as mean ± SD, n = 6, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: TGF-β1 (21898-1-AP) , 1:2000 , Proteintech.

Techniques: Western Blot, Staining

RMST-KO reduces fibrosis in mouse skin wound healing. (A) Differences of RMST expression between unwounded skin and the 21 dps group. (B) Agarose gel electrophoresis confirmed the successful knockout of RMST. (C) QPCR assay showing the expression of RMST 21 dps. (D) H&E and Masson staining of the wounds 21 dps as indicated. (E–F) RMST-KO reduced the (E) thickness and (F) area of neogenic fibrous tissue at 21 dps. (G–H) QPCR showing the COL1A1 and α-SMA levels were significantly decreased in the RMST-KO group compared to the WT group 21 dps. (I) Representative blot of COL1A1 and α-SMA 21 dps. (J–K) Statistical analysis of the immunoblot bands indicated that RMST-KO significantly suppressed the expression of COL1A1 and α-SMA 21 dps. Data were shown as mean ± SD, n = 6, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Journal: Biochemistry and Biophysics Reports

Article Title: LncRNA RMST knockout inhibits fibrosis by down-regulating Smad3 during mouse skin wound healing

doi: 10.1016/j.bbrep.2025.102386

Figure Lengend Snippet: RMST-KO reduces fibrosis in mouse skin wound healing. (A) Differences of RMST expression between unwounded skin and the 21 dps group. (B) Agarose gel electrophoresis confirmed the successful knockout of RMST. (C) QPCR assay showing the expression of RMST 21 dps. (D) H&E and Masson staining of the wounds 21 dps as indicated. (E–F) RMST-KO reduced the (E) thickness and (F) area of neogenic fibrous tissue at 21 dps. (G–H) QPCR showing the COL1A1 and α-SMA levels were significantly decreased in the RMST-KO group compared to the WT group 21 dps. (I) Representative blot of COL1A1 and α-SMA 21 dps. (J–K) Statistical analysis of the immunoblot bands indicated that RMST-KO significantly suppressed the expression of COL1A1 and α-SMA 21 dps. Data were shown as mean ± SD, n = 6, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Il-1β (16806-1-AP) , 1:2000 , Proteintech.

Techniques: Expressing, Agarose Gel Electrophoresis, Knock-Out, Staining, Western Blot

RMST-KO reduced the inflammation during mouse skin wound healing. (A–B) QPCR assay showed the mRNA expression of TNF-α and IL-1β were significantly decreased in the RMST-KO group 21 dps. (C) Representative blot of TNF-α, IL-1β 21 dps. (D–E) Statistical analysis of the immunoblot bands indicated that RMST-KO significantly suppressed TNF-α, IL-1β expression 21 dps. Data were shown as mean ± SD, n = 6, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Journal: Biochemistry and Biophysics Reports

Article Title: LncRNA RMST knockout inhibits fibrosis by down-regulating Smad3 during mouse skin wound healing

doi: 10.1016/j.bbrep.2025.102386

Figure Lengend Snippet: RMST-KO reduced the inflammation during mouse skin wound healing. (A–B) QPCR assay showed the mRNA expression of TNF-α and IL-1β were significantly decreased in the RMST-KO group 21 dps. (C) Representative blot of TNF-α, IL-1β 21 dps. (D–E) Statistical analysis of the immunoblot bands indicated that RMST-KO significantly suppressed TNF-α, IL-1β expression 21 dps. Data were shown as mean ± SD, n = 6, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Il-1β (16806-1-AP) , 1:2000 , Proteintech.

Techniques: Expressing, Western Blot

Smad3 was a downstream molecule of lncRNA RMST. (A) The heatmap shows the upregulated long non-coding RNAs in the GSE28914 dataset. (B) The catRAPID omics v2.1 software was used to predict the proteins interacting with RMST. (C) A Venn diagram displays the intersection of the two groups of data. (D) GO and KEGG pathway analysis was performed for these 273 intersections.

Journal: Biochemistry and Biophysics Reports

Article Title: LncRNA RMST knockout inhibits fibrosis by down-regulating Smad3 during mouse skin wound healing

doi: 10.1016/j.bbrep.2025.102386

Figure Lengend Snippet: Smad3 was a downstream molecule of lncRNA RMST. (A) The heatmap shows the upregulated long non-coding RNAs in the GSE28914 dataset. (B) The catRAPID omics v2.1 software was used to predict the proteins interacting with RMST. (C) A Venn diagram displays the intersection of the two groups of data. (D) GO and KEGG pathway analysis was performed for these 273 intersections.

Article Snippet: Il-1β (16806-1-AP) , 1:2000 , Proteintech.

Techniques: Software

Smad3-OE reversed the fibrosis suppression resulting from RMST-KO. (A) QPCR confirmed the upregulating effect of Smad3-OE lentivirus. (B) Representative blot of Smad3 under the effect of Smad3-OE and/or RMST-KO. (C) Statistical analysis of the immunoblot bands. (D) H&E and Masson staining of the wounds as indicated. (E–F) Statistical analysis of the (E) thickness and (F) area of neogenic fibrous tissue 21 dps. (G–I) qPCR detection of fibrosis markers and proteins in classical fibrosis pathways, including COL1, α-SMA, and TGF-β1. (J–M). Representative blot of COL1, α-SMA, and TGF-β1. (N–O) qPCR detection of inflammatory cytokines TNF-α and IL-1β. (P–R) Representative blot of TNF-α and IL-1β. Data were shown as mean ± SD, n = 6, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Journal: Biochemistry and Biophysics Reports

Article Title: LncRNA RMST knockout inhibits fibrosis by down-regulating Smad3 during mouse skin wound healing

doi: 10.1016/j.bbrep.2025.102386

Figure Lengend Snippet: Smad3-OE reversed the fibrosis suppression resulting from RMST-KO. (A) QPCR confirmed the upregulating effect of Smad3-OE lentivirus. (B) Representative blot of Smad3 under the effect of Smad3-OE and/or RMST-KO. (C) Statistical analysis of the immunoblot bands. (D) H&E and Masson staining of the wounds as indicated. (E–F) Statistical analysis of the (E) thickness and (F) area of neogenic fibrous tissue 21 dps. (G–I) qPCR detection of fibrosis markers and proteins in classical fibrosis pathways, including COL1, α-SMA, and TGF-β1. (J–M). Representative blot of COL1, α-SMA, and TGF-β1. (N–O) qPCR detection of inflammatory cytokines TNF-α and IL-1β. (P–R) Representative blot of TNF-α and IL-1β. Data were shown as mean ± SD, n = 6, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

Article Snippet: Il-1β (16806-1-AP) , 1:2000 , Proteintech.

Techniques: Western Blot, Staining