antibody anti α sma  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc antibody anti α sma
    Immunofluorescence assay showed that BA reduced the expression of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells: (a) BA reduced the expression of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells (200-fold) and (b) BA reduced the fluorescence intensity of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells. LTD4: 150 nM LTD4-induced type II AEC cells and BA: baicalin. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the LTD4 group, # P < 0.05 and ## P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.
    Antibody Anti α Sma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Baicalin Ameliorates Radiation-Induced Lung Injury by Inhibiting the CysLTs/CysLT1 Signaling Pathway"

    Article Title: Baicalin Ameliorates Radiation-Induced Lung Injury by Inhibiting the CysLTs/CysLT1 Signaling Pathway

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2022/2765354

    Immunofluorescence assay showed that BA reduced the expression of α -SMA in LTD4-induced type II AEC cells: (a) BA reduced the expression of α -SMA in LTD4-induced type II AEC cells (200-fold) and (b) BA reduced the fluorescence intensity of α -SMA in LTD4-induced type II AEC cells. LTD4: 150 nM LTD4-induced type II AEC cells and BA: baicalin. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the LTD4 group, # P < 0.05 and ## P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.
    Figure Legend Snippet: Immunofluorescence assay showed that BA reduced the expression of α -SMA in LTD4-induced type II AEC cells: (a) BA reduced the expression of α -SMA in LTD4-induced type II AEC cells (200-fold) and (b) BA reduced the fluorescence intensity of α -SMA in LTD4-induced type II AEC cells. LTD4: 150 nM LTD4-induced type II AEC cells and BA: baicalin. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the LTD4 group, # P < 0.05 and ## P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.

    Techniques Used: Immunofluorescence, Expressing, Fluorescence

    BA reduced the expression of CysLT1 mRNA, CysLT1, and α -SMA in lung tissue and type II AEC cells: (a) BA reduced the expression of CysLT1 mRNA in mice lung tissues and type II AEC cells and (b) and (c) BA reduced the expression of CysLT1 and α -SMA protein in mice lung tissues and type II AEC cells. IR: irradiation, BA: baicalin, DXM: dexamethasone, and LTD4: 150 nM LTD4-induced type II AEC cells. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the IR or LTD4 group, # P < 0.05 and ## P < 0.01; and compared with the LTD4 + BA 80 μ g/mL group, ★ P < 0.05 and ★★ P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.
    Figure Legend Snippet: BA reduced the expression of CysLT1 mRNA, CysLT1, and α -SMA in lung tissue and type II AEC cells: (a) BA reduced the expression of CysLT1 mRNA in mice lung tissues and type II AEC cells and (b) and (c) BA reduced the expression of CysLT1 and α -SMA protein in mice lung tissues and type II AEC cells. IR: irradiation, BA: baicalin, DXM: dexamethasone, and LTD4: 150 nM LTD4-induced type II AEC cells. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the IR or LTD4 group, # P < 0.05 and ## P < 0.01; and compared with the LTD4 + BA 80 μ g/mL group, ★ P < 0.05 and ★★ P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.

    Techniques Used: Expressing, Irradiation

    α msa antibody 19245s  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc α msa antibody 19245s
    α Msa Antibody 19245s, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    antibody anti α sma  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc antibody anti α sma
    Immunofluorescence assay showed that BA reduced the expression of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells: (a) BA reduced the expression of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells (200-fold) and (b) BA reduced the fluorescence intensity of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells. LTD4: 150 nM LTD4-induced type II AEC cells and BA: baicalin. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the LTD4 group, # P < 0.05 and ## P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.
    Antibody Anti α Sma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/antibody anti α sma/product/Cell Signaling Technology Inc
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    antibody anti α sma - by Bioz Stars, 2023-02
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    Images

    1) Product Images from "Baicalin Ameliorates Radiation-Induced Lung Injury by Inhibiting the CysLTs/CysLT1 Signaling Pathway"

    Article Title: Baicalin Ameliorates Radiation-Induced Lung Injury by Inhibiting the CysLTs/CysLT1 Signaling Pathway

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2022/2765354

    Immunofluorescence assay showed that BA reduced the expression of α -SMA in LTD4-induced type II AEC cells: (a) BA reduced the expression of α -SMA in LTD4-induced type II AEC cells (200-fold) and (b) BA reduced the fluorescence intensity of α -SMA in LTD4-induced type II AEC cells. LTD4: 150 nM LTD4-induced type II AEC cells and BA: baicalin. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the LTD4 group, # P < 0.05 and ## P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.
    Figure Legend Snippet: Immunofluorescence assay showed that BA reduced the expression of α -SMA in LTD4-induced type II AEC cells: (a) BA reduced the expression of α -SMA in LTD4-induced type II AEC cells (200-fold) and (b) BA reduced the fluorescence intensity of α -SMA in LTD4-induced type II AEC cells. LTD4: 150 nM LTD4-induced type II AEC cells and BA: baicalin. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the LTD4 group, # P < 0.05 and ## P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.

    Techniques Used: Immunofluorescence, Expressing, Fluorescence

    BA reduced the expression of CysLT1 mRNA, CysLT1, and α -SMA in lung tissue and type II AEC cells: (a) BA reduced the expression of CysLT1 mRNA in mice lung tissues and type II AEC cells and (b) and (c) BA reduced the expression of CysLT1 and α -SMA protein in mice lung tissues and type II AEC cells. IR: irradiation, BA: baicalin, DXM: dexamethasone, and LTD4: 150 nM LTD4-induced type II AEC cells. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the IR or LTD4 group, # P < 0.05 and ## P < 0.01; and compared with the LTD4 + BA 80 μ g/mL group, ★ P < 0.05 and ★★ P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.
    Figure Legend Snippet: BA reduced the expression of CysLT1 mRNA, CysLT1, and α -SMA in lung tissue and type II AEC cells: (a) BA reduced the expression of CysLT1 mRNA in mice lung tissues and type II AEC cells and (b) and (c) BA reduced the expression of CysLT1 and α -SMA protein in mice lung tissues and type II AEC cells. IR: irradiation, BA: baicalin, DXM: dexamethasone, and LTD4: 150 nM LTD4-induced type II AEC cells. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the IR or LTD4 group, # P < 0.05 and ## P < 0.01; and compared with the LTD4 + BA 80 μ g/mL group, ★ P < 0.05 and ★★ P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.

    Techniques Used: Expressing, Irradiation

    α sma  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc α sma
    25-OH D ameliorates TGF- β 1 induces EMT of BPH-1 cells and proliferation of WPMY-1 cells via blocking TGF- β signaling. (a) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (b) Transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (c) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (d) transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (e) EMT of BPH-1 cells were evaluated by observing elongated fibroblast-like morphology with scattered distribution. (f) The mRNA and protein levels of EMT biomarkers including <t>α</t> <t>-SMA,</t> E-cadherin, and N-cadherin were detected by qRT-PCR and western blot assays. (g) Proliferation ability of WPMY-1 cells was assessed by CCK8 assays. (h) The mRNA and protein expressions of cell cycle-related genes including CCND1 and p21 were analyzed by qRT-PCR and western blot assays. ∗ P < 0.05.
    α Sma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99/100 stars

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    1) Product Images from "Therapeutic Effects of 25-Hydroxyvitamin D on the Pathological Process of Benign Prostatic Hyperplasia: An In Vitro Evidence"

    Article Title: Therapeutic Effects of 25-Hydroxyvitamin D on the Pathological Process of Benign Prostatic Hyperplasia: An In Vitro Evidence

    Journal: Disease Markers

    doi: 10.1155/2021/4029470

    25-OH D ameliorates TGF- β 1 induces EMT of BPH-1 cells and proliferation of WPMY-1 cells via blocking TGF- β signaling. (a) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (b) Transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (c) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (d) transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (e) EMT of BPH-1 cells were evaluated by observing elongated fibroblast-like morphology with scattered distribution. (f) The mRNA and protein levels of EMT biomarkers including α -SMA, E-cadherin, and N-cadherin were detected by qRT-PCR and western blot assays. (g) Proliferation ability of WPMY-1 cells was assessed by CCK8 assays. (h) The mRNA and protein expressions of cell cycle-related genes including CCND1 and p21 were analyzed by qRT-PCR and western blot assays. ∗ P < 0.05.
    Figure Legend Snippet: 25-OH D ameliorates TGF- β 1 induces EMT of BPH-1 cells and proliferation of WPMY-1 cells via blocking TGF- β signaling. (a) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (b) Transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (c) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (d) transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (e) EMT of BPH-1 cells were evaluated by observing elongated fibroblast-like morphology with scattered distribution. (f) The mRNA and protein levels of EMT biomarkers including α -SMA, E-cadherin, and N-cadherin were detected by qRT-PCR and western blot assays. (g) Proliferation ability of WPMY-1 cells was assessed by CCK8 assays. (h) The mRNA and protein expressions of cell cycle-related genes including CCND1 and p21 were analyzed by qRT-PCR and western blot assays. ∗ P < 0.05.

    Techniques Used: Blocking Assay, Western Blot, Activity Assay, Luciferase, Quantitative RT-PCR

    antimouse α sma  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc antimouse α sma
    Antimouse α Sma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 1 article reviews
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    antimouse α sma - by Bioz Stars, 2023-02
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    α smooth muscle actin α sma  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc α smooth muscle actin α sma
    Mechanical ventilation induces pulmonary fibrosis. Mice lung tissue were acquired at Day 7 after 2 h of MV. A , lung injury was accessed and scored by Hematoxylin and Eosin staining. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. B , collagen deposition was assessed with Masson's trichrome staining and evaluated through Ashcroft fibrosis score. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. C-E , fibrosis was also quantified by determination of collagen-I α1 (COL1A1) ( C ), <t>α</t> <t>smooth</t> muscle <t>actin</t> <t>(α-SMA)</t> ( D ) in lung tissues (n = 3 in sham group and n = 9 in MV group) and type I procollagen carboxy-terminal peptide (PICP) levels in bronchoalveolar lavage fluid (BALF) ( E, n = 6 per group). F , lung tissues were stained with fluorophore-labeled antibodies against fibroblast marker fibronectin (FN) (Alexa Fluor 568, red) and collagen-I (fluorescein isothiocyanate, green). 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue). Original magnification × 400, Scale bars correspond to 20 µm. Data are expressed as means ± SEM. * p < 0.05, **p < 0.01, *** p < 0.001 (t test).
    α Smooth Muscle Actin α Sma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Integrin β3-PKM2 pathway-mediated aerobic glycolysis contributes to mechanical ventilation-induced pulmonary fibrosis"

    Article Title: Integrin β3-PKM2 pathway-mediated aerobic glycolysis contributes to mechanical ventilation-induced pulmonary fibrosis

    Journal: Theranostics

    doi: 10.7150/thno.72328

    Mechanical ventilation induces pulmonary fibrosis. Mice lung tissue were acquired at Day 7 after 2 h of MV. A , lung injury was accessed and scored by Hematoxylin and Eosin staining. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. B , collagen deposition was assessed with Masson's trichrome staining and evaluated through Ashcroft fibrosis score. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. C-E , fibrosis was also quantified by determination of collagen-I α1 (COL1A1) ( C ), α smooth muscle actin (α-SMA) ( D ) in lung tissues (n = 3 in sham group and n = 9 in MV group) and type I procollagen carboxy-terminal peptide (PICP) levels in bronchoalveolar lavage fluid (BALF) ( E, n = 6 per group). F , lung tissues were stained with fluorophore-labeled antibodies against fibroblast marker fibronectin (FN) (Alexa Fluor 568, red) and collagen-I (fluorescein isothiocyanate, green). 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue). Original magnification × 400, Scale bars correspond to 20 µm. Data are expressed as means ± SEM. * p < 0.05, **p < 0.01, *** p < 0.001 (t test).
    Figure Legend Snippet: Mechanical ventilation induces pulmonary fibrosis. Mice lung tissue were acquired at Day 7 after 2 h of MV. A , lung injury was accessed and scored by Hematoxylin and Eosin staining. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. B , collagen deposition was assessed with Masson's trichrome staining and evaluated through Ashcroft fibrosis score. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. C-E , fibrosis was also quantified by determination of collagen-I α1 (COL1A1) ( C ), α smooth muscle actin (α-SMA) ( D ) in lung tissues (n = 3 in sham group and n = 9 in MV group) and type I procollagen carboxy-terminal peptide (PICP) levels in bronchoalveolar lavage fluid (BALF) ( E, n = 6 per group). F , lung tissues were stained with fluorophore-labeled antibodies against fibroblast marker fibronectin (FN) (Alexa Fluor 568, red) and collagen-I (fluorescein isothiocyanate, green). 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue). Original magnification × 400, Scale bars correspond to 20 µm. Data are expressed as means ± SEM. * p < 0.05, **p < 0.01, *** p < 0.001 (t test).

    Techniques Used: Staining, Labeling, Marker

    PKM2 knockdown alleviates aerobic glycolysis and MV-induced pulmonary fibrosis. Mice were treated intratracheally with vector-AAV or shPKM-AAV 4 weeks before mechanical ventilation (MV), for the duration of 2 h. Lung tissues were harvested 7 days after intubation. A , lung fibrosis was quantified by Masson's trichrome staining. Original magnification × 200, Scale bars correspond to 100 µm, n = 6, 3, 6, 5, respectively in each group. B , pyruvate kinase M2 (PKM2), lactic dehydrogenase (LDHA), α smooth muscle actin (α-SMA) and collagen I α1 (COL1A1) expression was quantified by western blot analysis, n = 3 per group. C , lung tissues were stained with fluorophore labeled antibodies against fibroblast marker fibronectin (FN) (red) and collagen I (green), 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue), Original magnification × 400, Scale bars correspond to 20 µm. D and E , lactate (Lac) and type I procollagen carboxy-terminal peptide (PICP) in bronchoalveolar lavage fluid (BALF) was tested, n = 6, 3, 6, 5, respectively in each group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).
    Figure Legend Snippet: PKM2 knockdown alleviates aerobic glycolysis and MV-induced pulmonary fibrosis. Mice were treated intratracheally with vector-AAV or shPKM-AAV 4 weeks before mechanical ventilation (MV), for the duration of 2 h. Lung tissues were harvested 7 days after intubation. A , lung fibrosis was quantified by Masson's trichrome staining. Original magnification × 200, Scale bars correspond to 100 µm, n = 6, 3, 6, 5, respectively in each group. B , pyruvate kinase M2 (PKM2), lactic dehydrogenase (LDHA), α smooth muscle actin (α-SMA) and collagen I α1 (COL1A1) expression was quantified by western blot analysis, n = 3 per group. C , lung tissues were stained with fluorophore labeled antibodies against fibroblast marker fibronectin (FN) (red) and collagen I (green), 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue), Original magnification × 400, Scale bars correspond to 20 µm. D and E , lactate (Lac) and type I procollagen carboxy-terminal peptide (PICP) in bronchoalveolar lavage fluid (BALF) was tested, n = 6, 3, 6, 5, respectively in each group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).

    Techniques Used: Plasmid Preparation, Staining, Expressing, Western Blot, Labeling, Marker

    PKM2 inhibitor alleviates aerobic glycolysis and MV-induced pulmonary fibrosis. Mice were treated with PKM2 inhibitor shikonin 10 mg/kg in 100ul corn oil daily for 3 consecutive days before being subjected to MV for 2 h. Lung tissues were harvested 7 days after intubation. A , lung fibrosis was accessed by Masson's trichrome staining, Original magnification × 200, Scale bars correspond to 100 µm, n = 6, 3, 6, 3, respectively in each group. B , lactic dehydrogenase (LDHA), α smooth muscle actin (α-SMA) and collagen I α1 (COL1A1) expression was quantified by western blot analysis, n = 3 per group. C , lung tissues were stained with fluorophore-labeled antibodies against fibroblast marker fibronectin (FN) (red) and collagen I (green), 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue), original magnification × 400, Scale bars correspond to 20 µm. D and E , lactate (Lac) and type I procollagen carboxy-terminal peptide (PICP) levels in BALF was tested, n = 6, 3, 6, 3, respectively in each group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).
    Figure Legend Snippet: PKM2 inhibitor alleviates aerobic glycolysis and MV-induced pulmonary fibrosis. Mice were treated with PKM2 inhibitor shikonin 10 mg/kg in 100ul corn oil daily for 3 consecutive days before being subjected to MV for 2 h. Lung tissues were harvested 7 days after intubation. A , lung fibrosis was accessed by Masson's trichrome staining, Original magnification × 200, Scale bars correspond to 100 µm, n = 6, 3, 6, 3, respectively in each group. B , lactic dehydrogenase (LDHA), α smooth muscle actin (α-SMA) and collagen I α1 (COL1A1) expression was quantified by western blot analysis, n = 3 per group. C , lung tissues were stained with fluorophore-labeled antibodies against fibroblast marker fibronectin (FN) (red) and collagen I (green), 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue), original magnification × 400, Scale bars correspond to 20 µm. D and E , lactate (Lac) and type I procollagen carboxy-terminal peptide (PICP) levels in BALF was tested, n = 6, 3, 6, 3, respectively in each group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).

    Techniques Used: Staining, Expressing, Western Blot, Labeling, Marker

    Integrin β3 inhibition ameliorates PKM2-mediated aerobic glycolysis and MV-induced pulmonary fibrosis. A and B , both wild-type and integrin β3-deficient (β3 +/- ) mice were subjected to mechanical ventilation (MV) for 2 h. Lung tissues were harvested at day 7. A , lung fibrosis was quantified by Masson's trichrome staining, original magnification × 200, scale bars correspond to 100μm, n = 6, 5, 6, 6, respectively in each group. B , integrin β3, pyruvate kinase M2 (PKM2), lactic dehydrogenase (LDHA), collagen I α1 (COL1A1) and α smooth muscle actin (α-SMA) expression was quantified by western blot analysis, n = 3 per group. C and D , mice were treated intraperitoneally with integrin β3 inhibitor cilengitide 4 mg/kg once a day for 3 consecutive days before being subjected to MV for 2 h. Lung tissues were harvested 7 days after intubation. C , lung fibrosis was quantified by Masson's trichrome staining, original magnification × 200, scale bars correspond to 100 µm, n = 6 per group. D , integrin β3, PKM2, LDHA and COL1A1 expression was quantified by western blot analysis, n = 3 per group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).
    Figure Legend Snippet: Integrin β3 inhibition ameliorates PKM2-mediated aerobic glycolysis and MV-induced pulmonary fibrosis. A and B , both wild-type and integrin β3-deficient (β3 +/- ) mice were subjected to mechanical ventilation (MV) for 2 h. Lung tissues were harvested at day 7. A , lung fibrosis was quantified by Masson's trichrome staining, original magnification × 200, scale bars correspond to 100μm, n = 6, 5, 6, 6, respectively in each group. B , integrin β3, pyruvate kinase M2 (PKM2), lactic dehydrogenase (LDHA), collagen I α1 (COL1A1) and α smooth muscle actin (α-SMA) expression was quantified by western blot analysis, n = 3 per group. C and D , mice were treated intraperitoneally with integrin β3 inhibitor cilengitide 4 mg/kg once a day for 3 consecutive days before being subjected to MV for 2 h. Lung tissues were harvested 7 days after intubation. C , lung fibrosis was quantified by Masson's trichrome staining, original magnification × 200, scale bars correspond to 100 µm, n = 6 per group. D , integrin β3, PKM2, LDHA and COL1A1 expression was quantified by western blot analysis, n = 3 per group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).

    Techniques Used: Inhibition, Staining, Expressing, Western Blot

    alpha smooth muscle actin  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc alpha smooth muscle actin
    Alpha Smooth Muscle Actin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti α sma antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti α sma antibody
    EC-SMC cross talk via exosome-delivered miR-483-3p. (a) A representative electron microscopy image of HUVEC-derived exosomes. Scale bar, 100 nm. (b) A nanoparticle tracking analysis of the size distribution of exosomes. (c) Immunofluorescence images of HASMCs stained with <t>α</t> <t>-SMA</t> (red) and DAPI (blue). HASMCs were treated with HUVEC-derived exosomes (PKH67-label, green) for 0 or 24 hours. Laser scanning confocal images are shown. Scale bar, 20 μ m. (d) The qPCR analysis of miR-483-3p levels in HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p for 48 hours. (e) Exosomes isolated from HUVECs were identified by CD81 and CD63 immunostaining. (f) miR-483-3p levels in exosomes isolated from HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p. (g–i) HASMCs were incubated with HUVEC-derived exosomes for 24 hours. The qPCR analysis of (g) miR-483-3p and ACE1, TGF- β , and (h) CTGF in HASMCs. (i) Western blotting analysis of these proteins in HASMCs. Data are shown as mean ± SEM. Student's two-tailed t test was used for statistical analysis of data. ∗ P < 0.05; ∗∗∗ P < 0.001.
    Anti α Sma Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Endothelial MicroRNA-483-3p Is Hypertension-Protective"

    Article Title: Endothelial MicroRNA-483-3p Is Hypertension-Protective

    Journal: Oxidative Medicine and Cellular Longevity

    doi: 10.1155/2022/3698219

    EC-SMC cross talk via exosome-delivered miR-483-3p. (a) A representative electron microscopy image of HUVEC-derived exosomes. Scale bar, 100 nm. (b) A nanoparticle tracking analysis of the size distribution of exosomes. (c) Immunofluorescence images of HASMCs stained with α -SMA (red) and DAPI (blue). HASMCs were treated with HUVEC-derived exosomes (PKH67-label, green) for 0 or 24 hours. Laser scanning confocal images are shown. Scale bar, 20 μ m. (d) The qPCR analysis of miR-483-3p levels in HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p for 48 hours. (e) Exosomes isolated from HUVECs were identified by CD81 and CD63 immunostaining. (f) miR-483-3p levels in exosomes isolated from HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p. (g–i) HASMCs were incubated with HUVEC-derived exosomes for 24 hours. The qPCR analysis of (g) miR-483-3p and ACE1, TGF- β , and (h) CTGF in HASMCs. (i) Western blotting analysis of these proteins in HASMCs. Data are shown as mean ± SEM. Student's two-tailed t test was used for statistical analysis of data. ∗ P < 0.05; ∗∗∗ P < 0.001.
    Figure Legend Snippet: EC-SMC cross talk via exosome-delivered miR-483-3p. (a) A representative electron microscopy image of HUVEC-derived exosomes. Scale bar, 100 nm. (b) A nanoparticle tracking analysis of the size distribution of exosomes. (c) Immunofluorescence images of HASMCs stained with α -SMA (red) and DAPI (blue). HASMCs were treated with HUVEC-derived exosomes (PKH67-label, green) for 0 or 24 hours. Laser scanning confocal images are shown. Scale bar, 20 μ m. (d) The qPCR analysis of miR-483-3p levels in HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p for 48 hours. (e) Exosomes isolated from HUVECs were identified by CD81 and CD63 immunostaining. (f) miR-483-3p levels in exosomes isolated from HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p. (g–i) HASMCs were incubated with HUVEC-derived exosomes for 24 hours. The qPCR analysis of (g) miR-483-3p and ACE1, TGF- β , and (h) CTGF in HASMCs. (i) Western blotting analysis of these proteins in HASMCs. Data are shown as mean ± SEM. Student's two-tailed t test was used for statistical analysis of data. ∗ P < 0.05; ∗∗∗ P < 0.001.

    Techniques Used: Electron Microscopy, Derivative Assay, Immunofluorescence, Staining, Transfection, Isolation, Immunostaining, Incubation, Western Blot, Two Tailed Test

    α sma  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc α sma
    Primers used for RT-qPCR.
    α Sma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Jieduquyuzishen Prescription Attenuates Renal Fibrosis in MRL/lpr Mice via Inhibiting EMT and TGF- β 1/Smad2/3 Pathway"

    Article Title: Jieduquyuzishen Prescription Attenuates Renal Fibrosis in MRL/lpr Mice via Inhibiting EMT and TGF- β 1/Smad2/3 Pathway

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2022/4987323

    Primers used for RT-qPCR.
    Figure Legend Snippet: Primers used for RT-qPCR.

    Techniques Used: Sequencing

    JP-Treated Serum inhibited the EMT process of HK-2 cells stimulated by TGF- β 1. (a) The protein bands of E-Cadherin, Vimentin and α -SMA in HK-2 cells stimulated by TGF- β 1. (b–d) Quantitative analysis of protein expression alteration HK-2 cells stimulated by TGF- β 1. (e) The mRNA expressions of E-Cadherin, Vimentin and α -SMA in HK-2 cells stimulated by TGF- β 1. Data were expressed as mean ± SD ( n = 3). ∗ P < 0.05 and ∗∗ P < 0.01, compared with the Control group; ## P < 0.01, compared with the TGF- β 1 group.
    Figure Legend Snippet: JP-Treated Serum inhibited the EMT process of HK-2 cells stimulated by TGF- β 1. (a) The protein bands of E-Cadherin, Vimentin and α -SMA in HK-2 cells stimulated by TGF- β 1. (b–d) Quantitative analysis of protein expression alteration HK-2 cells stimulated by TGF- β 1. (e) The mRNA expressions of E-Cadherin, Vimentin and α -SMA in HK-2 cells stimulated by TGF- β 1. Data were expressed as mean ± SD ( n = 3). ∗ P < 0.05 and ∗∗ P < 0.01, compared with the Control group; ## P < 0.01, compared with the TGF- β 1 group.

    Techniques Used: Expressing

    JP-treated serum inhibited the EMT process of HK-2 cells induced by coculture of M2c macrophages. (a) The mRNA expression trend of iNOS, CD163 and CD206 in THP-1 cells after IL-10 induction. (b–d) Bar graphs depict the fold changes of mRNA expression of iNOS, CD163 and CD206 assessed by quantitative RT-qPCR. (a–d) In the graphs, the THP-1 cells untreated with IL-10 as control group, and 0 h, 12 h and 24 h group represent the THP-1 cells induced with IL-10 for 0 h 12 h and 24 h respectively ( ∗∗ P < 0.01 compared with the Control group; ## P < 0.01 compared with the 0 h group; n = 3). (e) The protein bands of E-Cadherin, Vimentin and α -SMA in HK-2 cells induced by coculture of M2c macrophages. ((f)-(h)) Quantitative analysis of protein expression alteration HK-2 cells induced by coculture of M2c macrophages. ∗∗ P < 0.01, compared with the Control group; ## P < 0.01, compared with the B group; n = 3.
    Figure Legend Snippet: JP-treated serum inhibited the EMT process of HK-2 cells induced by coculture of M2c macrophages. (a) The mRNA expression trend of iNOS, CD163 and CD206 in THP-1 cells after IL-10 induction. (b–d) Bar graphs depict the fold changes of mRNA expression of iNOS, CD163 and CD206 assessed by quantitative RT-qPCR. (a–d) In the graphs, the THP-1 cells untreated with IL-10 as control group, and 0 h, 12 h and 24 h group represent the THP-1 cells induced with IL-10 for 0 h 12 h and 24 h respectively ( ∗∗ P < 0.01 compared with the Control group; ## P < 0.01 compared with the 0 h group; n = 3). (e) The protein bands of E-Cadherin, Vimentin and α -SMA in HK-2 cells induced by coculture of M2c macrophages. ((f)-(h)) Quantitative analysis of protein expression alteration HK-2 cells induced by coculture of M2c macrophages. ∗∗ P < 0.01, compared with the Control group; ## P < 0.01, compared with the B group; n = 3.

    Techniques Used: Expressing, Quantitative RT-PCR

    JP inhibited the process of renal EMT in MRL/lpr mice. (a) The protein bands of E-Cadherin, Vimentin and α -SMA in the renal. (b) The mRNA expressions of E-Cadherin, Vimentin and α -SMA in the renal. (c–e) Graphic presentation of western blot analyses in the four groups as indicated. (f) Representative micrographs showed that the down-expression of E-cadherin in model group was increased by JP. Scale bar, 20 μ m. (g) Representative micrographs showed that the up-expression of α -SMA in model group was decreased by JP. Scale bar, 20 μ m. ∗ P < 0.05 and ∗∗ P < 0.01, compared with the Control group; ## P < 0.01, compared with the Model group; n = 3. Magnification ((f), (g) are 40×).
    Figure Legend Snippet: JP inhibited the process of renal EMT in MRL/lpr mice. (a) The protein bands of E-Cadherin, Vimentin and α -SMA in the renal. (b) The mRNA expressions of E-Cadherin, Vimentin and α -SMA in the renal. (c–e) Graphic presentation of western blot analyses in the four groups as indicated. (f) Representative micrographs showed that the down-expression of E-cadherin in model group was increased by JP. Scale bar, 20 μ m. (g) Representative micrographs showed that the up-expression of α -SMA in model group was decreased by JP. Scale bar, 20 μ m. ∗ P < 0.05 and ∗∗ P < 0.01, compared with the Control group; ## P < 0.01, compared with the Model group; n = 3. Magnification ((f), (g) are 40×).

    Techniques Used: Western Blot, Expressing

    anti α sma  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti α sma
    The <t>α</t> <t>-SMA</t> and SIRT7 expression in ox-LDL-treated HAVSMCs. (a) Immunofluorescence staining was used to detect <t>α</t> <t>-SMA</t> in HAVSMCs stimulated with ox-LDL. Nuclei were stained with DAPI (blue), 200× magnification. (b) The protein expression level of <t>α</t> <t>-SMA</t> was measured by Western blot. ∗∗∗ P < 0.001 versus VSMCs. The protein level of SIRT7 was measured by Western blot (c) and RT-qPCR (d) in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 versus VSMCs. The expression level of SIRT7 was measured by Western blot (e) and RT-qPCR (f) after silencing of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; # P < 0.05 and ## P < 0.01 versus siRNA-NC. The expression level of SIRT7 was measured by Western blot (g) and RT-qPCR (h) after overexpression of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; ## P < 0.01 and ### P < 0.001 versus Vector-NC.
    Anti α Sma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "SIRT7 Regulates the Vascular Smooth Muscle Cells Proliferation and Migration via Wnt/ β -Catenin Signaling Pathway"

    Article Title: SIRT7 Regulates the Vascular Smooth Muscle Cells Proliferation and Migration via Wnt/ β -Catenin Signaling Pathway

    Journal: BioMed Research International

    doi: 10.1155/2018/4769596

    The α -SMA and SIRT7 expression in ox-LDL-treated HAVSMCs. (a) Immunofluorescence staining was used to detect α -SMA in HAVSMCs stimulated with ox-LDL. Nuclei were stained with DAPI (blue), 200× magnification. (b) The protein expression level of α -SMA was measured by Western blot. ∗∗∗ P < 0.001 versus VSMCs. The protein level of SIRT7 was measured by Western blot (c) and RT-qPCR (d) in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 versus VSMCs. The expression level of SIRT7 was measured by Western blot (e) and RT-qPCR (f) after silencing of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; # P < 0.05 and ## P < 0.01 versus siRNA-NC. The expression level of SIRT7 was measured by Western blot (g) and RT-qPCR (h) after overexpression of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; ## P < 0.01 and ### P < 0.001 versus Vector-NC.
    Figure Legend Snippet: The α -SMA and SIRT7 expression in ox-LDL-treated HAVSMCs. (a) Immunofluorescence staining was used to detect α -SMA in HAVSMCs stimulated with ox-LDL. Nuclei were stained with DAPI (blue), 200× magnification. (b) The protein expression level of α -SMA was measured by Western blot. ∗∗∗ P < 0.001 versus VSMCs. The protein level of SIRT7 was measured by Western blot (c) and RT-qPCR (d) in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 versus VSMCs. The expression level of SIRT7 was measured by Western blot (e) and RT-qPCR (f) after silencing of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; # P < 0.05 and ## P < 0.01 versus siRNA-NC. The expression level of SIRT7 was measured by Western blot (g) and RT-qPCR (h) after overexpression of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; ## P < 0.01 and ### P < 0.001 versus Vector-NC.

    Techniques Used: Expressing, Immunofluorescence, Staining, Western Blot, Quantitative RT-PCR, Over Expression, Plasmid Preparation

    (a) The level of α -SMA after SIRT7 silencing or overexpression in ox-LDL-treated HAVSMCs was measured by immunofluorescence staining. Nuclei were stained with DAPI (blue), 200× magnification. (b) The protein expression level of α -SMA after SIRT7 silencing (b) or overexpression (c) in ox-LDL-treated HAVSMCs was assessed by Western blot. ∗ P < 0.05 and ∗∗ P < 0.01 versus VSMCs; # P < 0.05 versus siRNA-NC or Vector-NC.
    Figure Legend Snippet: (a) The level of α -SMA after SIRT7 silencing or overexpression in ox-LDL-treated HAVSMCs was measured by immunofluorescence staining. Nuclei were stained with DAPI (blue), 200× magnification. (b) The protein expression level of α -SMA after SIRT7 silencing (b) or overexpression (c) in ox-LDL-treated HAVSMCs was assessed by Western blot. ∗ P < 0.05 and ∗∗ P < 0.01 versus VSMCs; # P < 0.05 versus siRNA-NC or Vector-NC.

    Techniques Used: Over Expression, Immunofluorescence, Staining, Expressing, Western Blot, Plasmid Preparation

    α sma  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc α sma
    Primers used for the mRNA analysis.
    α Sma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Schistosoma japonicum Infection in Treg-Specific USP21 Knockout Mice"

    Article Title: Schistosoma japonicum Infection in Treg-Specific USP21 Knockout Mice

    Journal: Journal of Immunology Research

    doi: 10.1155/2021/6613162

    Primers used for the mRNA analysis.
    Figure Legend Snippet: Primers used for the mRNA analysis.

    Techniques Used:

    Changes in liver fibrosis in USP21 fl/fl FOXP3 cre mice infected with S. japonicum . (a–e) The livers were harvested from the mice on the 42 nd day after the infection and stained with Masson's trichrome ( n = 10 animals/group). (a) Representative images of collagen deposition in the WT-INF and KO-INF mice (original magnification: 100x) were obtained. The blue areas are collagen granules. (b) Comparison of the percentages of the hepatic fibrosis area between the WT-INF and KO-INF groups. The data are presented as the means ± SD, ∗ p = 0.039. (c) Comparison of the levels the α -SMA, Collagen I, and Collagen III mRNAs in the WT and KO mice in the NC and INF groups. The data are presented as the means ± SD. Comparison of the levels of the α -SMA, Collagen I, and Collagen III mRNAs between the infected groups. The data are presented as the means ± SD. In the infection group, α -SMA: ∗∗ p < 0.001; collagen I: ∗∗ p = 0.008, and Collagen III: ∗∗ p = 0.006. (d) Representative images of SMA, Collagen I, and Collagen III protein expression in the WT and KO mice from the NC and INF groups, as determined by Western blotting. (e) Comparison of protein expression between WT and KO mice in the NC and INF groups. The data are presented as the means ± SD. In the infection group, α -SMA: ∗ p = 0.034, Collagen I: ∗∗ p = 0.006, and Collagen III: ∗ p = 0.03.
    Figure Legend Snippet: Changes in liver fibrosis in USP21 fl/fl FOXP3 cre mice infected with S. japonicum . (a–e) The livers were harvested from the mice on the 42 nd day after the infection and stained with Masson's trichrome ( n = 10 animals/group). (a) Representative images of collagen deposition in the WT-INF and KO-INF mice (original magnification: 100x) were obtained. The blue areas are collagen granules. (b) Comparison of the percentages of the hepatic fibrosis area between the WT-INF and KO-INF groups. The data are presented as the means ± SD, ∗ p = 0.039. (c) Comparison of the levels the α -SMA, Collagen I, and Collagen III mRNAs in the WT and KO mice in the NC and INF groups. The data are presented as the means ± SD. Comparison of the levels of the α -SMA, Collagen I, and Collagen III mRNAs between the infected groups. The data are presented as the means ± SD. In the infection group, α -SMA: ∗∗ p < 0.001; collagen I: ∗∗ p = 0.008, and Collagen III: ∗∗ p = 0.006. (d) Representative images of SMA, Collagen I, and Collagen III protein expression in the WT and KO mice from the NC and INF groups, as determined by Western blotting. (e) Comparison of protein expression between WT and KO mice in the NC and INF groups. The data are presented as the means ± SD. In the infection group, α -SMA: ∗ p = 0.034, Collagen I: ∗∗ p = 0.006, and Collagen III: ∗ p = 0.03.

    Techniques Used: Infection, Staining, Expressing, Western Blot

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    Cell Signaling Technology Inc antibody anti α sma
    Immunofluorescence assay showed that BA reduced the expression of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells: (a) BA reduced the expression of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells (200-fold) and (b) BA reduced the fluorescence intensity of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells. LTD4: 150 nM LTD4-induced type II AEC cells and BA: baicalin. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the LTD4 group, # P < 0.05 and ## P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.
    Antibody Anti α Sma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Immunofluorescence assay showed that BA reduced the expression of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells: (a) BA reduced the expression of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells (200-fold) and (b) BA reduced the fluorescence intensity of <t>α</t> <t>-SMA</t> in LTD4-induced type II AEC cells. LTD4: 150 nM LTD4-induced type II AEC cells and BA: baicalin. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the LTD4 group, # P < 0.05 and ## P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.
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    25-OH D ameliorates TGF- β 1 induces EMT of BPH-1 cells and proliferation of WPMY-1 cells via blocking TGF- β signaling. (a) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (b) Transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (c) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (d) transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (e) EMT of BPH-1 cells were evaluated by observing elongated fibroblast-like morphology with scattered distribution. (f) The mRNA and protein levels of EMT biomarkers including <t>α</t> <t>-SMA,</t> E-cadherin, and N-cadherin were detected by qRT-PCR and western blot assays. (g) Proliferation ability of WPMY-1 cells was assessed by CCK8 assays. (h) The mRNA and protein expressions of cell cycle-related genes including CCND1 and p21 were analyzed by qRT-PCR and western blot assays. ∗ P < 0.05.
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    25-OH D ameliorates TGF- β 1 induces EMT of BPH-1 cells and proliferation of WPMY-1 cells via blocking TGF- β signaling. (a) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (b) Transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (c) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (d) transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (e) EMT of BPH-1 cells were evaluated by observing elongated fibroblast-like morphology with scattered distribution. (f) The mRNA and protein levels of EMT biomarkers including <t>α</t> <t>-SMA,</t> E-cadherin, and N-cadherin were detected by qRT-PCR and western blot assays. (g) Proliferation ability of WPMY-1 cells was assessed by CCK8 assays. (h) The mRNA and protein expressions of cell cycle-related genes including CCND1 and p21 were analyzed by qRT-PCR and western blot assays. ∗ P < 0.05.
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    Mechanical ventilation induces pulmonary fibrosis. Mice lung tissue were acquired at Day 7 after 2 h of MV. A , lung injury was accessed and scored by Hematoxylin and Eosin staining. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. B , collagen deposition was assessed with Masson's trichrome staining and evaluated through Ashcroft fibrosis score. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. C-E , fibrosis was also quantified by determination of collagen-I α1 (COL1A1) ( C ), <t>α</t> <t>smooth</t> muscle <t>actin</t> <t>(α-SMA)</t> ( D ) in lung tissues (n = 3 in sham group and n = 9 in MV group) and type I procollagen carboxy-terminal peptide (PICP) levels in bronchoalveolar lavage fluid (BALF) ( E, n = 6 per group). F , lung tissues were stained with fluorophore-labeled antibodies against fibroblast marker fibronectin (FN) (Alexa Fluor 568, red) and collagen-I (fluorescein isothiocyanate, green). 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue). Original magnification × 400, Scale bars correspond to 20 µm. Data are expressed as means ± SEM. * p < 0.05, **p < 0.01, *** p < 0.001 (t test).
    α Smooth Muscle Actin α Sma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Mechanical ventilation induces pulmonary fibrosis. Mice lung tissue were acquired at Day 7 after 2 h of MV. A , lung injury was accessed and scored by Hematoxylin and Eosin staining. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. B , collagen deposition was assessed with Masson's trichrome staining and evaluated through Ashcroft fibrosis score. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. C-E , fibrosis was also quantified by determination of collagen-I α1 (COL1A1) ( C ), <t>α</t> <t>smooth</t> muscle <t>actin</t> <t>(α-SMA)</t> ( D ) in lung tissues (n = 3 in sham group and n = 9 in MV group) and type I procollagen carboxy-terminal peptide (PICP) levels in bronchoalveolar lavage fluid (BALF) ( E, n = 6 per group). F , lung tissues were stained with fluorophore-labeled antibodies against fibroblast marker fibronectin (FN) (Alexa Fluor 568, red) and collagen-I (fluorescein isothiocyanate, green). 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue). Original magnification × 400, Scale bars correspond to 20 µm. Data are expressed as means ± SEM. * p < 0.05, **p < 0.01, *** p < 0.001 (t test).
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    EC-SMC cross talk via exosome-delivered miR-483-3p. (a) A representative electron microscopy image of HUVEC-derived exosomes. Scale bar, 100 nm. (b) A nanoparticle tracking analysis of the size distribution of exosomes. (c) Immunofluorescence images of HASMCs stained with <t>α</t> <t>-SMA</t> (red) and DAPI (blue). HASMCs were treated with HUVEC-derived exosomes (PKH67-label, green) for 0 or 24 hours. Laser scanning confocal images are shown. Scale bar, 20 μ m. (d) The qPCR analysis of miR-483-3p levels in HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p for 48 hours. (e) Exosomes isolated from HUVECs were identified by CD81 and CD63 immunostaining. (f) miR-483-3p levels in exosomes isolated from HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p. (g–i) HASMCs were incubated with HUVEC-derived exosomes for 24 hours. The qPCR analysis of (g) miR-483-3p and ACE1, TGF- β , and (h) CTGF in HASMCs. (i) Western blotting analysis of these proteins in HASMCs. Data are shown as mean ± SEM. Student's two-tailed t test was used for statistical analysis of data. ∗ P < 0.05; ∗∗∗ P < 0.001.
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    The <t>α</t> <t>-SMA</t> and SIRT7 expression in ox-LDL-treated HAVSMCs. (a) Immunofluorescence staining was used to detect <t>α</t> <t>-SMA</t> in HAVSMCs stimulated with ox-LDL. Nuclei were stained with DAPI (blue), 200× magnification. (b) The protein expression level of <t>α</t> <t>-SMA</t> was measured by Western blot. ∗∗∗ P < 0.001 versus VSMCs. The protein level of SIRT7 was measured by Western blot (c) and RT-qPCR (d) in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 versus VSMCs. The expression level of SIRT7 was measured by Western blot (e) and RT-qPCR (f) after silencing of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; # P < 0.05 and ## P < 0.01 versus siRNA-NC. The expression level of SIRT7 was measured by Western blot (g) and RT-qPCR (h) after overexpression of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; ## P < 0.01 and ### P < 0.001 versus Vector-NC.
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    Image Search Results


    Immunofluorescence assay showed that BA reduced the expression of α -SMA in LTD4-induced type II AEC cells: (a) BA reduced the expression of α -SMA in LTD4-induced type II AEC cells (200-fold) and (b) BA reduced the fluorescence intensity of α -SMA in LTD4-induced type II AEC cells. LTD4: 150 nM LTD4-induced type II AEC cells and BA: baicalin. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the LTD4 group, # P < 0.05 and ## P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Baicalin Ameliorates Radiation-Induced Lung Injury by Inhibiting the CysLTs/CysLT1 Signaling Pathway

    doi: 10.1155/2022/2765354

    Figure Lengend Snippet: Immunofluorescence assay showed that BA reduced the expression of α -SMA in LTD4-induced type II AEC cells: (a) BA reduced the expression of α -SMA in LTD4-induced type II AEC cells (200-fold) and (b) BA reduced the fluorescence intensity of α -SMA in LTD4-induced type II AEC cells. LTD4: 150 nM LTD4-induced type II AEC cells and BA: baicalin. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the LTD4 group, # P < 0.05 and ## P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.

    Article Snippet: Cells were incubated with primary antibody anti- α -SMA (cell signaling, 19245S) overnight at 4°C.

    Techniques: Immunofluorescence, Expressing, Fluorescence

    BA reduced the expression of CysLT1 mRNA, CysLT1, and α -SMA in lung tissue and type II AEC cells: (a) BA reduced the expression of CysLT1 mRNA in mice lung tissues and type II AEC cells and (b) and (c) BA reduced the expression of CysLT1 and α -SMA protein in mice lung tissues and type II AEC cells. IR: irradiation, BA: baicalin, DXM: dexamethasone, and LTD4: 150 nM LTD4-induced type II AEC cells. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the IR or LTD4 group, # P < 0.05 and ## P < 0.01; and compared with the LTD4 + BA 80 μ g/mL group, ★ P < 0.05 and ★★ P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Baicalin Ameliorates Radiation-Induced Lung Injury by Inhibiting the CysLTs/CysLT1 Signaling Pathway

    doi: 10.1155/2022/2765354

    Figure Lengend Snippet: BA reduced the expression of CysLT1 mRNA, CysLT1, and α -SMA in lung tissue and type II AEC cells: (a) BA reduced the expression of CysLT1 mRNA in mice lung tissues and type II AEC cells and (b) and (c) BA reduced the expression of CysLT1 and α -SMA protein in mice lung tissues and type II AEC cells. IR: irradiation, BA: baicalin, DXM: dexamethasone, and LTD4: 150 nM LTD4-induced type II AEC cells. Compared with the control group, ▲ P < 0.05 and ▲▲ P < 0.01; compared with the IR or LTD4 group, # P < 0.05 and ## P < 0.01; and compared with the LTD4 + BA 80 μ g/mL group, ★ P < 0.05 and ★★ P < 0.01. Data are expressed as the mean ± SD ( n = 3) and were analyzed by one-way ANOVA followed by Tukey analysis.

    Article Snippet: Cells were incubated with primary antibody anti- α -SMA (cell signaling, 19245S) overnight at 4°C.

    Techniques: Expressing, Irradiation

    25-OH D ameliorates TGF- β 1 induces EMT of BPH-1 cells and proliferation of WPMY-1 cells via blocking TGF- β signaling. (a) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (b) Transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (c) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (d) transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (e) EMT of BPH-1 cells were evaluated by observing elongated fibroblast-like morphology with scattered distribution. (f) The mRNA and protein levels of EMT biomarkers including α -SMA, E-cadherin, and N-cadherin were detected by qRT-PCR and western blot assays. (g) Proliferation ability of WPMY-1 cells was assessed by CCK8 assays. (h) The mRNA and protein expressions of cell cycle-related genes including CCND1 and p21 were analyzed by qRT-PCR and western blot assays. ∗ P < 0.05.

    Journal: Disease Markers

    Article Title: Therapeutic Effects of 25-Hydroxyvitamin D on the Pathological Process of Benign Prostatic Hyperplasia: An In Vitro Evidence

    doi: 10.1155/2021/4029470

    Figure Lengend Snippet: 25-OH D ameliorates TGF- β 1 induces EMT of BPH-1 cells and proliferation of WPMY-1 cells via blocking TGF- β signaling. (a) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (b) Transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after BPH-1 cells were treated with TGF- β 1 and 25-OH D. (c) Phosphorylation of Smad2 and Smad3 was detected by western blot assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (d) transcriptional activity of Smad2/Smad3/Smad4 complex was analyzed by luciferase assay after WPMY-1 cells were treated with TGF- β 1 and 25-OH D. (e) EMT of BPH-1 cells were evaluated by observing elongated fibroblast-like morphology with scattered distribution. (f) The mRNA and protein levels of EMT biomarkers including α -SMA, E-cadherin, and N-cadherin were detected by qRT-PCR and western blot assays. (g) Proliferation ability of WPMY-1 cells was assessed by CCK8 assays. (h) The mRNA and protein expressions of cell cycle-related genes including CCND1 and p21 were analyzed by qRT-PCR and western blot assays. ∗ P < 0.05.

    Article Snippet: After washing, the membranes were then incubated with secondary antibodies at room temperature for 2 h. Antibodies used for the immunoreactivity were Smad2 [1 : 1000, #5339, Cell Signaling Technology (CST), USA]; Phospho-Smad2 (Ser465/Ser467) (1 : 1000, #18338, CST); Smad3 (1 : 1000, #9523, CST); Phospho-Smad3 (Ser423/425) (1 : 1000, #9520, CST); α -SMA (1 : 1000, #19245, CST); N-cadherin (1 : 1000, #13116, CST); E-cadherin (1 : 50, ab1416, Abcam, USA); CCND1 (1 : 200, ab16663, Abcam); p21 (1 : 1000, ab188224, Abcam); phospho-NF- κ B p65 (Ser536) (1 : 1000, #3033, CST); NF- κ B p65 (1 : 1000, #8242, CST); phospho-Stat3 (Tyr705) (1 : 2000, #9145, CST); Stat3 (1 : 1000, #9139, CST); Nfr2 (1 : 1000, #12721, CST); and GAPDH (1 : 2500, ab9485, Abcam).

    Techniques: Blocking Assay, Western Blot, Activity Assay, Luciferase, Quantitative RT-PCR

    Mechanical ventilation induces pulmonary fibrosis. Mice lung tissue were acquired at Day 7 after 2 h of MV. A , lung injury was accessed and scored by Hematoxylin and Eosin staining. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. B , collagen deposition was assessed with Masson's trichrome staining and evaluated through Ashcroft fibrosis score. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. C-E , fibrosis was also quantified by determination of collagen-I α1 (COL1A1) ( C ), α smooth muscle actin (α-SMA) ( D ) in lung tissues (n = 3 in sham group and n = 9 in MV group) and type I procollagen carboxy-terminal peptide (PICP) levels in bronchoalveolar lavage fluid (BALF) ( E, n = 6 per group). F , lung tissues were stained with fluorophore-labeled antibodies against fibroblast marker fibronectin (FN) (Alexa Fluor 568, red) and collagen-I (fluorescein isothiocyanate, green). 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue). Original magnification × 400, Scale bars correspond to 20 µm. Data are expressed as means ± SEM. * p < 0.05, **p < 0.01, *** p < 0.001 (t test).

    Journal: Theranostics

    Article Title: Integrin β3-PKM2 pathway-mediated aerobic glycolysis contributes to mechanical ventilation-induced pulmonary fibrosis

    doi: 10.7150/thno.72328

    Figure Lengend Snippet: Mechanical ventilation induces pulmonary fibrosis. Mice lung tissue were acquired at Day 7 after 2 h of MV. A , lung injury was accessed and scored by Hematoxylin and Eosin staining. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. B , collagen deposition was assessed with Masson's trichrome staining and evaluated through Ashcroft fibrosis score. Original magnification × 200. Scale bars correspond to 100 µm, n = 12 per group. C-E , fibrosis was also quantified by determination of collagen-I α1 (COL1A1) ( C ), α smooth muscle actin (α-SMA) ( D ) in lung tissues (n = 3 in sham group and n = 9 in MV group) and type I procollagen carboxy-terminal peptide (PICP) levels in bronchoalveolar lavage fluid (BALF) ( E, n = 6 per group). F , lung tissues were stained with fluorophore-labeled antibodies against fibroblast marker fibronectin (FN) (Alexa Fluor 568, red) and collagen-I (fluorescein isothiocyanate, green). 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue). Original magnification × 400, Scale bars correspond to 20 µm. Data are expressed as means ± SEM. * p < 0.05, **p < 0.01, *** p < 0.001 (t test).

    Article Snippet: The membrane was washed and blocked with Tris-buffered saline (TBS) containing 0.1% Tween-20 and 10% nonfat dry milk before overnight incubation with appropriate primary antibodies (integrin β3 (SJ1909/NBP2-67416, Novus, USA), PKM2 (AF7244, R&D, USA), collagen-I α-1 (COL1A1, 72026S, CST, USA), α-smooth muscle actin (α-SMA) (CST, 19245), Lactate dehydrogenase (LDHA) (3582, CST, USA) and β-actin (8457, CST, USA)) in blocking buffer at 4 °C.

    Techniques: Staining, Labeling, Marker

    PKM2 knockdown alleviates aerobic glycolysis and MV-induced pulmonary fibrosis. Mice were treated intratracheally with vector-AAV or shPKM-AAV 4 weeks before mechanical ventilation (MV), for the duration of 2 h. Lung tissues were harvested 7 days after intubation. A , lung fibrosis was quantified by Masson's trichrome staining. Original magnification × 200, Scale bars correspond to 100 µm, n = 6, 3, 6, 5, respectively in each group. B , pyruvate kinase M2 (PKM2), lactic dehydrogenase (LDHA), α smooth muscle actin (α-SMA) and collagen I α1 (COL1A1) expression was quantified by western blot analysis, n = 3 per group. C , lung tissues were stained with fluorophore labeled antibodies against fibroblast marker fibronectin (FN) (red) and collagen I (green), 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue), Original magnification × 400, Scale bars correspond to 20 µm. D and E , lactate (Lac) and type I procollagen carboxy-terminal peptide (PICP) in bronchoalveolar lavage fluid (BALF) was tested, n = 6, 3, 6, 5, respectively in each group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).

    Journal: Theranostics

    Article Title: Integrin β3-PKM2 pathway-mediated aerobic glycolysis contributes to mechanical ventilation-induced pulmonary fibrosis

    doi: 10.7150/thno.72328

    Figure Lengend Snippet: PKM2 knockdown alleviates aerobic glycolysis and MV-induced pulmonary fibrosis. Mice were treated intratracheally with vector-AAV or shPKM-AAV 4 weeks before mechanical ventilation (MV), for the duration of 2 h. Lung tissues were harvested 7 days after intubation. A , lung fibrosis was quantified by Masson's trichrome staining. Original magnification × 200, Scale bars correspond to 100 µm, n = 6, 3, 6, 5, respectively in each group. B , pyruvate kinase M2 (PKM2), lactic dehydrogenase (LDHA), α smooth muscle actin (α-SMA) and collagen I α1 (COL1A1) expression was quantified by western blot analysis, n = 3 per group. C , lung tissues were stained with fluorophore labeled antibodies against fibroblast marker fibronectin (FN) (red) and collagen I (green), 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue), Original magnification × 400, Scale bars correspond to 20 µm. D and E , lactate (Lac) and type I procollagen carboxy-terminal peptide (PICP) in bronchoalveolar lavage fluid (BALF) was tested, n = 6, 3, 6, 5, respectively in each group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).

    Article Snippet: The membrane was washed and blocked with Tris-buffered saline (TBS) containing 0.1% Tween-20 and 10% nonfat dry milk before overnight incubation with appropriate primary antibodies (integrin β3 (SJ1909/NBP2-67416, Novus, USA), PKM2 (AF7244, R&D, USA), collagen-I α-1 (COL1A1, 72026S, CST, USA), α-smooth muscle actin (α-SMA) (CST, 19245), Lactate dehydrogenase (LDHA) (3582, CST, USA) and β-actin (8457, CST, USA)) in blocking buffer at 4 °C.

    Techniques: Plasmid Preparation, Staining, Expressing, Western Blot, Labeling, Marker

    PKM2 inhibitor alleviates aerobic glycolysis and MV-induced pulmonary fibrosis. Mice were treated with PKM2 inhibitor shikonin 10 mg/kg in 100ul corn oil daily for 3 consecutive days before being subjected to MV for 2 h. Lung tissues were harvested 7 days after intubation. A , lung fibrosis was accessed by Masson's trichrome staining, Original magnification × 200, Scale bars correspond to 100 µm, n = 6, 3, 6, 3, respectively in each group. B , lactic dehydrogenase (LDHA), α smooth muscle actin (α-SMA) and collagen I α1 (COL1A1) expression was quantified by western blot analysis, n = 3 per group. C , lung tissues were stained with fluorophore-labeled antibodies against fibroblast marker fibronectin (FN) (red) and collagen I (green), 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue), original magnification × 400, Scale bars correspond to 20 µm. D and E , lactate (Lac) and type I procollagen carboxy-terminal peptide (PICP) levels in BALF was tested, n = 6, 3, 6, 3, respectively in each group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).

    Journal: Theranostics

    Article Title: Integrin β3-PKM2 pathway-mediated aerobic glycolysis contributes to mechanical ventilation-induced pulmonary fibrosis

    doi: 10.7150/thno.72328

    Figure Lengend Snippet: PKM2 inhibitor alleviates aerobic glycolysis and MV-induced pulmonary fibrosis. Mice were treated with PKM2 inhibitor shikonin 10 mg/kg in 100ul corn oil daily for 3 consecutive days before being subjected to MV for 2 h. Lung tissues were harvested 7 days after intubation. A , lung fibrosis was accessed by Masson's trichrome staining, Original magnification × 200, Scale bars correspond to 100 µm, n = 6, 3, 6, 3, respectively in each group. B , lactic dehydrogenase (LDHA), α smooth muscle actin (α-SMA) and collagen I α1 (COL1A1) expression was quantified by western blot analysis, n = 3 per group. C , lung tissues were stained with fluorophore-labeled antibodies against fibroblast marker fibronectin (FN) (red) and collagen I (green), 4',6-diamidino-2- phenylindole (DAPI) stain was used to detect nuclei (blue), original magnification × 400, Scale bars correspond to 20 µm. D and E , lactate (Lac) and type I procollagen carboxy-terminal peptide (PICP) levels in BALF was tested, n = 6, 3, 6, 3, respectively in each group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).

    Article Snippet: The membrane was washed and blocked with Tris-buffered saline (TBS) containing 0.1% Tween-20 and 10% nonfat dry milk before overnight incubation with appropriate primary antibodies (integrin β3 (SJ1909/NBP2-67416, Novus, USA), PKM2 (AF7244, R&D, USA), collagen-I α-1 (COL1A1, 72026S, CST, USA), α-smooth muscle actin (α-SMA) (CST, 19245), Lactate dehydrogenase (LDHA) (3582, CST, USA) and β-actin (8457, CST, USA)) in blocking buffer at 4 °C.

    Techniques: Staining, Expressing, Western Blot, Labeling, Marker

    Integrin β3 inhibition ameliorates PKM2-mediated aerobic glycolysis and MV-induced pulmonary fibrosis. A and B , both wild-type and integrin β3-deficient (β3 +/- ) mice were subjected to mechanical ventilation (MV) for 2 h. Lung tissues were harvested at day 7. A , lung fibrosis was quantified by Masson's trichrome staining, original magnification × 200, scale bars correspond to 100μm, n = 6, 5, 6, 6, respectively in each group. B , integrin β3, pyruvate kinase M2 (PKM2), lactic dehydrogenase (LDHA), collagen I α1 (COL1A1) and α smooth muscle actin (α-SMA) expression was quantified by western blot analysis, n = 3 per group. C and D , mice were treated intraperitoneally with integrin β3 inhibitor cilengitide 4 mg/kg once a day for 3 consecutive days before being subjected to MV for 2 h. Lung tissues were harvested 7 days after intubation. C , lung fibrosis was quantified by Masson's trichrome staining, original magnification × 200, scale bars correspond to 100 µm, n = 6 per group. D , integrin β3, PKM2, LDHA and COL1A1 expression was quantified by western blot analysis, n = 3 per group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).

    Journal: Theranostics

    Article Title: Integrin β3-PKM2 pathway-mediated aerobic glycolysis contributes to mechanical ventilation-induced pulmonary fibrosis

    doi: 10.7150/thno.72328

    Figure Lengend Snippet: Integrin β3 inhibition ameliorates PKM2-mediated aerobic glycolysis and MV-induced pulmonary fibrosis. A and B , both wild-type and integrin β3-deficient (β3 +/- ) mice were subjected to mechanical ventilation (MV) for 2 h. Lung tissues were harvested at day 7. A , lung fibrosis was quantified by Masson's trichrome staining, original magnification × 200, scale bars correspond to 100μm, n = 6, 5, 6, 6, respectively in each group. B , integrin β3, pyruvate kinase M2 (PKM2), lactic dehydrogenase (LDHA), collagen I α1 (COL1A1) and α smooth muscle actin (α-SMA) expression was quantified by western blot analysis, n = 3 per group. C and D , mice were treated intraperitoneally with integrin β3 inhibitor cilengitide 4 mg/kg once a day for 3 consecutive days before being subjected to MV for 2 h. Lung tissues were harvested 7 days after intubation. C , lung fibrosis was quantified by Masson's trichrome staining, original magnification × 200, scale bars correspond to 100 µm, n = 6 per group. D , integrin β3, PKM2, LDHA and COL1A1 expression was quantified by western blot analysis, n = 3 per group. Data are expressed as means ± SEM, *p < 0.05, **p < 0.01, *** p < 0.001 (ANOVA).

    Article Snippet: The membrane was washed and blocked with Tris-buffered saline (TBS) containing 0.1% Tween-20 and 10% nonfat dry milk before overnight incubation with appropriate primary antibodies (integrin β3 (SJ1909/NBP2-67416, Novus, USA), PKM2 (AF7244, R&D, USA), collagen-I α-1 (COL1A1, 72026S, CST, USA), α-smooth muscle actin (α-SMA) (CST, 19245), Lactate dehydrogenase (LDHA) (3582, CST, USA) and β-actin (8457, CST, USA)) in blocking buffer at 4 °C.

    Techniques: Inhibition, Staining, Expressing, Western Blot

    EC-SMC cross talk via exosome-delivered miR-483-3p. (a) A representative electron microscopy image of HUVEC-derived exosomes. Scale bar, 100 nm. (b) A nanoparticle tracking analysis of the size distribution of exosomes. (c) Immunofluorescence images of HASMCs stained with α -SMA (red) and DAPI (blue). HASMCs were treated with HUVEC-derived exosomes (PKH67-label, green) for 0 or 24 hours. Laser scanning confocal images are shown. Scale bar, 20 μ m. (d) The qPCR analysis of miR-483-3p levels in HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p for 48 hours. (e) Exosomes isolated from HUVECs were identified by CD81 and CD63 immunostaining. (f) miR-483-3p levels in exosomes isolated from HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p. (g–i) HASMCs were incubated with HUVEC-derived exosomes for 24 hours. The qPCR analysis of (g) miR-483-3p and ACE1, TGF- β , and (h) CTGF in HASMCs. (i) Western blotting analysis of these proteins in HASMCs. Data are shown as mean ± SEM. Student's two-tailed t test was used for statistical analysis of data. ∗ P < 0.05; ∗∗∗ P < 0.001.

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Endothelial MicroRNA-483-3p Is Hypertension-Protective

    doi: 10.1155/2022/3698219

    Figure Lengend Snippet: EC-SMC cross talk via exosome-delivered miR-483-3p. (a) A representative electron microscopy image of HUVEC-derived exosomes. Scale bar, 100 nm. (b) A nanoparticle tracking analysis of the size distribution of exosomes. (c) Immunofluorescence images of HASMCs stained with α -SMA (red) and DAPI (blue). HASMCs were treated with HUVEC-derived exosomes (PKH67-label, green) for 0 or 24 hours. Laser scanning confocal images are shown. Scale bar, 20 μ m. (d) The qPCR analysis of miR-483-3p levels in HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p for 48 hours. (e) Exosomes isolated from HUVECs were identified by CD81 and CD63 immunostaining. (f) miR-483-3p levels in exosomes isolated from HUVECs transfected with pre-miR-Ctrl or pre-miR-483-3p. (g–i) HASMCs were incubated with HUVEC-derived exosomes for 24 hours. The qPCR analysis of (g) miR-483-3p and ACE1, TGF- β , and (h) CTGF in HASMCs. (i) Western blotting analysis of these proteins in HASMCs. Data are shown as mean ± SEM. Student's two-tailed t test was used for statistical analysis of data. ∗ P < 0.05; ∗∗∗ P < 0.001.

    Article Snippet: Cells were incubated with anti- α -SMA antibody (#19245, Cell Signaling Technology) overnight at 4°C, followed by a secondary antibody for 1 hour at room temperature.

    Techniques: Electron Microscopy, Derivative Assay, Immunofluorescence, Staining, Transfection, Isolation, Immunostaining, Incubation, Western Blot, Two Tailed Test

    The α -SMA and SIRT7 expression in ox-LDL-treated HAVSMCs. (a) Immunofluorescence staining was used to detect α -SMA in HAVSMCs stimulated with ox-LDL. Nuclei were stained with DAPI (blue), 200× magnification. (b) The protein expression level of α -SMA was measured by Western blot. ∗∗∗ P < 0.001 versus VSMCs. The protein level of SIRT7 was measured by Western blot (c) and RT-qPCR (d) in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 versus VSMCs. The expression level of SIRT7 was measured by Western blot (e) and RT-qPCR (f) after silencing of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; # P < 0.05 and ## P < 0.01 versus siRNA-NC. The expression level of SIRT7 was measured by Western blot (g) and RT-qPCR (h) after overexpression of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; ## P < 0.01 and ### P < 0.001 versus Vector-NC.

    Journal: BioMed Research International

    Article Title: SIRT7 Regulates the Vascular Smooth Muscle Cells Proliferation and Migration via Wnt/ β -Catenin Signaling Pathway

    doi: 10.1155/2018/4769596

    Figure Lengend Snippet: The α -SMA and SIRT7 expression in ox-LDL-treated HAVSMCs. (a) Immunofluorescence staining was used to detect α -SMA in HAVSMCs stimulated with ox-LDL. Nuclei were stained with DAPI (blue), 200× magnification. (b) The protein expression level of α -SMA was measured by Western blot. ∗∗∗ P < 0.001 versus VSMCs. The protein level of SIRT7 was measured by Western blot (c) and RT-qPCR (d) in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 versus VSMCs. The expression level of SIRT7 was measured by Western blot (e) and RT-qPCR (f) after silencing of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; # P < 0.05 and ## P < 0.01 versus siRNA-NC. The expression level of SIRT7 was measured by Western blot (g) and RT-qPCR (h) after overexpression of SIRT7 in ox-LDL-treated HAVSMCs. ∗∗ P < 0.01 and ∗∗∗ P < 0.001 versus VSMCs; ## P < 0.01 and ### P < 0.001 versus Vector-NC.

    Article Snippet: Anti- α -SMA (1:1000; cat. no. 19245S), anti-SIRT7 (1:1000; cat. no. 5360S), anti- β -catenin (1:1000; cat. no. 8480T), anti-cyclin D1 (1:1000; cat. no. 3300T), and anti-GAPDH (1:1000; cat. no. 5174S) antibodies were purchased from Cell Signaling Technology (Boston, MA, USA).

    Techniques: Expressing, Immunofluorescence, Staining, Western Blot, Quantitative RT-PCR, Over Expression, Plasmid Preparation

    (a) The level of α -SMA after SIRT7 silencing or overexpression in ox-LDL-treated HAVSMCs was measured by immunofluorescence staining. Nuclei were stained with DAPI (blue), 200× magnification. (b) The protein expression level of α -SMA after SIRT7 silencing (b) or overexpression (c) in ox-LDL-treated HAVSMCs was assessed by Western blot. ∗ P < 0.05 and ∗∗ P < 0.01 versus VSMCs; # P < 0.05 versus siRNA-NC or Vector-NC.

    Journal: BioMed Research International

    Article Title: SIRT7 Regulates the Vascular Smooth Muscle Cells Proliferation and Migration via Wnt/ β -Catenin Signaling Pathway

    doi: 10.1155/2018/4769596

    Figure Lengend Snippet: (a) The level of α -SMA after SIRT7 silencing or overexpression in ox-LDL-treated HAVSMCs was measured by immunofluorescence staining. Nuclei were stained with DAPI (blue), 200× magnification. (b) The protein expression level of α -SMA after SIRT7 silencing (b) or overexpression (c) in ox-LDL-treated HAVSMCs was assessed by Western blot. ∗ P < 0.05 and ∗∗ P < 0.01 versus VSMCs; # P < 0.05 versus siRNA-NC or Vector-NC.

    Article Snippet: Anti- α -SMA (1:1000; cat. no. 19245S), anti-SIRT7 (1:1000; cat. no. 5360S), anti- β -catenin (1:1000; cat. no. 8480T), anti-cyclin D1 (1:1000; cat. no. 3300T), and anti-GAPDH (1:1000; cat. no. 5174S) antibodies were purchased from Cell Signaling Technology (Boston, MA, USA).

    Techniques: Over Expression, Immunofluorescence, Staining, Expressing, Western Blot, Plasmid Preparation