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anti srf  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc anti srf
    Anti Srf, 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
    https://www.bioz.com/product/srf+antibody/pm41861925-89-9-11
    Average 86 stars, based on 1 article reviews
    anti srf - by Bioz Stars, 2026-10
    86/100 stars

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    Related Articles

    Chromatin Immunoprecipitation:

    Article Title: Nutrient regulation of the islet epigenome controls adaptive insulin secretion
    Article Snippet: Lsd1 ChIP of islets from fed or fasted mice was performed as described (69) following nuclear isolation of 1,000 dissociated islets using 30 μL of Dynabeads Protein A beads (Life Technologies) conjugated to 4 μg anti-Lsd1 antibody (ab17721, Abcam) in a total volume of 120 μL. .. The same protocol was followed for Srf ChIP-Seq in Min6 cells with the following modifications: 1.25 × 107 cells were used for immunoprecipitation using 4 μl of Srf antibody (5147, Cell Signaling Technology) in a total volume of 120 μL. .. Libraries were constructed from purified DNA using the KAPA DNA Library Preparation Kit for Illumina (Kapa Biosystems).

    Article Title: Profiles of novel high-molecular-weight synthetic antioxidants in urine and associated child exposure in China.
    Article Snippet: 1 Introduction The ability to regulate nutrient metabolism in response to feeding and fasting is necessary for metabolic homeostasis.. Nutrient utilization is acutely regulated by hormones and metabolites that change in response to feeding state (1).. If an energy state persists, adaptive control mechanisms increasingly influence nutrient metabolism.

    Article Title: Nutrient regulation of the islet epigenome controls adaptive insulin secretion
    Article Snippet: Lsd1 ChIP of islets from fed or fasted mice was performed as described ( ) following nuclear isolation of 1,000 dissociated islets using 30 μL of Dynabeads Protein A beads (Life Technologies) conjugated to 4 μg anti-Lsd1 antibody (ab17721, Abcam) in a total volume of 120 μL. .. The same protocol was followed for Srf ChIP-Seq in Min6 cells with the following modifications: 1.25 × 10 7 cells were used for immunoprecipitation using 4 μl of Srf antibody (5147, Cell Signaling Technology) in a total volume of 120 μL. .. Libraries were constructed from purified DNA using the KAPA DNA Library Preparation Kit for Illumina (Kapa Biosystems).

    Immunoprecipitation:

    Article Title: Nutrient regulation of the islet epigenome controls adaptive insulin secretion
    Article Snippet: Lsd1 ChIP of islets from fed or fasted mice was performed as described (69) following nuclear isolation of 1,000 dissociated islets using 30 μL of Dynabeads Protein A beads (Life Technologies) conjugated to 4 μg anti-Lsd1 antibody (ab17721, Abcam) in a total volume of 120 μL. .. The same protocol was followed for Srf ChIP-Seq in Min6 cells with the following modifications: 1.25 × 107 cells were used for immunoprecipitation using 4 μl of Srf antibody (5147, Cell Signaling Technology) in a total volume of 120 μL. .. Libraries were constructed from purified DNA using the KAPA DNA Library Preparation Kit for Illumina (Kapa Biosystems).

    Article Title: Profiles of novel high-molecular-weight synthetic antioxidants in urine and associated child exposure in China.
    Article Snippet: 1 Introduction The ability to regulate nutrient metabolism in response to feeding and fasting is necessary for metabolic homeostasis.. Nutrient utilization is acutely regulated by hormones and metabolites that change in response to feeding state (1).. If an energy state persists, adaptive control mechanisms increasingly influence nutrient metabolism.

    Article Title: Nutrient regulation of the islet epigenome controls adaptive insulin secretion
    Article Snippet: Lsd1 ChIP of islets from fed or fasted mice was performed as described ( ) following nuclear isolation of 1,000 dissociated islets using 30 μL of Dynabeads Protein A beads (Life Technologies) conjugated to 4 μg anti-Lsd1 antibody (ab17721, Abcam) in a total volume of 120 μL. .. The same protocol was followed for Srf ChIP-Seq in Min6 cells with the following modifications: 1.25 × 10 7 cells were used for immunoprecipitation using 4 μl of Srf antibody (5147, Cell Signaling Technology) in a total volume of 120 μL. .. Libraries were constructed from purified DNA using the KAPA DNA Library Preparation Kit for Illumina (Kapa Biosystems).

    Article Title: Inhibition of TRPM7 blocks MRTF/SRF-dependent transcriptional and tumorigenic activity.
    Article Snippet: Myocardin-related transcription factors A and B (MRTFs) are coactivators of Serum Response Factor (SRF) that mediates the expression of genes involved in cell proliferation, migration and differentiation.. There is mounting evidence that MRTFs and SRF represent promising targets for hepatocellular carcinoma (HCC) growth.. Since MRTF-A nuclear localization is a prerequisite for its transcriptional activity and oncogenic properties, we searched for pharmacologically active compounds able to redistribute MRTF-A to the cytoplasm.

    Cell-Signaling:

    Article Title: Human umbilical cord/placenta-derived mesenchymal stem cell secretome attenuates intestinal fibrosis
    Article Snippet: The following antibodies were used: procollagen1A1 (Procol1A1) antibody (SP1D8, Developmental Studies Hybridoma Bank, Iowa City, IA) and bronectin (FN) antibody (ab2413, Abcam, Cambridge, MA). .. Other include α-smooth muscle actin (α-SMA) antibody (A2547, Sigma), phospho-Smad2 (Ser465/467) antibody (#3108, Cell Signaling), RhoA antibody (#sc-418, Santa Cruz Biotechnology, Dallas, TX), GAPDH antibody (#2118, Cell Signaling), Mkl1(MRTF-A) antibody (21166-1-AP, ProteinTech), SRF antibody (#5147, Cell Signaling), and HDAC1 antibody (#5356, Cell Signaling). ..

    Article Title: Human umbilical cord/placenta mesenchymal stem cell conditioned medium attenuates intestinal fibrosis in vivo and in vitro
    Article Snippet: The following antibodies were used: procollagen1A1 (Procol1A1) antibody (SP1D8, Developmental Studies Hybridoma Bank, Iowa City, IA) and fibronectin (FN) antibody (ab2413, Abcam, Cambridge, MA). .. Others include α-smooth muscle actin (α-SMA) antibody (A2547, Sigma), phospho-Smad2 (Ser465/467) antibody (#3108, Cell Signaling), RhoA antibody (#sc-418, Santa Cruz Biotechnology, Dallas, TX), GAPDH antibody (#2118, Cell Signaling), Mkl1(MRTF-A) antibody (21166-1-AP, ProteinTech), SRF antibody (#5147, Cell Signaling), and HDAC1 antibody (#5356, Cell Signaling). ..



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    Cell Signaling Technology Inc srf
    Contractile Gene Expression Is Downregulated in Chol-Loaded hVSMCs (A, B) Human vascular smooth muscle cells (hVSMCs) were treated with cholesterol (Chol) (5 μg/mL) or 0.2% bovine serum albumin (control [CT]) for 24 hours and 48 hours and gene expression <t>of</t> <t>Acta2</t> , Tagln , Cnn1, Myocd, and <t>Srf</t> were determined by quantitative polymerase chain reaction. (C) hVSMCs were treated with Chol (5 μg/mL) or 0.2% bovine serum albumin (CT) for 24 hours and protein expression of α–smooth muscle actin (α-SMA) and CNN1 were determined by Western blotting (representative blots shown). Densitometry showing the (D) α-SMA and (E) CNN1 band intensities normalized to GAPDH. For data analysis, unpaired Student’s t -testing was performed for comparing the means of 2 groups. For 2 or more independent groups, 1-way analysis of variance followed by Dunnett post hoc test was performed. A P value of ≤0.05 was considered significant. Data are presented as the mean ± SEM of 3 independent experiments, and P values are as indicated (∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗∗ P < 0.0001).
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    Abmart Inc anti srf
    Contractile Gene Expression Is Downregulated in Chol-Loaded hVSMCs (A, B) Human vascular smooth muscle cells (hVSMCs) were treated with cholesterol (Chol) (5 μg/mL) or 0.2% bovine serum albumin (control [CT]) for 24 hours and 48 hours and gene expression <t>of</t> <t>Acta2</t> , Tagln , Cnn1, Myocd, and <t>Srf</t> were determined by quantitative polymerase chain reaction. (C) hVSMCs were treated with Chol (5 μg/mL) or 0.2% bovine serum albumin (CT) for 24 hours and protein expression of α–smooth muscle actin (α-SMA) and CNN1 were determined by Western blotting (representative blots shown). Densitometry showing the (D) α-SMA and (E) CNN1 band intensities normalized to GAPDH. For data analysis, unpaired Student’s t -testing was performed for comparing the means of 2 groups. For 2 or more independent groups, 1-way analysis of variance followed by Dunnett post hoc test was performed. A P value of ≤0.05 was considered significant. Data are presented as the mean ± SEM of 3 independent experiments, and P values are as indicated (∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗∗ P < 0.0001).
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    Abmart Inc rhodamine anti srf
    Contractile Gene Expression Is Downregulated in Chol-Loaded hVSMCs (A, B) Human vascular smooth muscle cells (hVSMCs) were treated with cholesterol (Chol) (5 μg/mL) or 0.2% bovine serum albumin (control [CT]) for 24 hours and 48 hours and gene expression <t>of</t> <t>Acta2</t> , Tagln , Cnn1, Myocd, and <t>Srf</t> were determined by quantitative polymerase chain reaction. (C) hVSMCs were treated with Chol (5 μg/mL) or 0.2% bovine serum albumin (CT) for 24 hours and protein expression of α–smooth muscle actin (α-SMA) and CNN1 were determined by Western blotting (representative blots shown). Densitometry showing the (D) α-SMA and (E) CNN1 band intensities normalized to GAPDH. For data analysis, unpaired Student’s t -testing was performed for comparing the means of 2 groups. For 2 or more independent groups, 1-way analysis of variance followed by Dunnett post hoc test was performed. A P value of ≤0.05 was considered significant. Data are presented as the mean ± SEM of 3 independent experiments, and P values are as indicated (∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗∗ P < 0.0001).
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    Image Search Results


    Contractile Gene Expression Is Downregulated in Chol-Loaded hVSMCs (A, B) Human vascular smooth muscle cells (hVSMCs) were treated with cholesterol (Chol) (5 μg/mL) or 0.2% bovine serum albumin (control [CT]) for 24 hours and 48 hours and gene expression of Acta2 , Tagln , Cnn1, Myocd, and Srf were determined by quantitative polymerase chain reaction. (C) hVSMCs were treated with Chol (5 μg/mL) or 0.2% bovine serum albumin (CT) for 24 hours and protein expression of α–smooth muscle actin (α-SMA) and CNN1 were determined by Western blotting (representative blots shown). Densitometry showing the (D) α-SMA and (E) CNN1 band intensities normalized to GAPDH. For data analysis, unpaired Student’s t -testing was performed for comparing the means of 2 groups. For 2 or more independent groups, 1-way analysis of variance followed by Dunnett post hoc test was performed. A P value of ≤0.05 was considered significant. Data are presented as the mean ± SEM of 3 independent experiments, and P values are as indicated (∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗∗ P < 0.0001).

    Journal: JACC: Basic to Translational Science

    Article Title: HDL Regulates TGFβ-Receptor Lipid Raft Partitioning, Restoring Contractile Features of Cholesterol-Loaded Vascular Smooth Muscle Cells

    doi: 10.1016/j.jacbts.2025.101461

    Figure Lengend Snippet: Contractile Gene Expression Is Downregulated in Chol-Loaded hVSMCs (A, B) Human vascular smooth muscle cells (hVSMCs) were treated with cholesterol (Chol) (5 μg/mL) or 0.2% bovine serum albumin (control [CT]) for 24 hours and 48 hours and gene expression of Acta2 , Tagln , Cnn1, Myocd, and Srf were determined by quantitative polymerase chain reaction. (C) hVSMCs were treated with Chol (5 μg/mL) or 0.2% bovine serum albumin (CT) for 24 hours and protein expression of α–smooth muscle actin (α-SMA) and CNN1 were determined by Western blotting (representative blots shown). Densitometry showing the (D) α-SMA and (E) CNN1 band intensities normalized to GAPDH. For data analysis, unpaired Student’s t -testing was performed for comparing the means of 2 groups. For 2 or more independent groups, 1-way analysis of variance followed by Dunnett post hoc test was performed. A P value of ≤0.05 was considered significant. Data are presented as the mean ± SEM of 3 independent experiments, and P values are as indicated (∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗∗ P < 0.0001).

    Article Snippet: The primary antibodies used were as follows: ACTA2 (#A2547, Sigma); CNN1 (#M3556, DAKO); SRF (#5147, Cell Signaling); p38MAPK (#sc-535, Santa Cruz Biotechnology); SMAD2/3 (#8685, Cell Signaling); TUBA (#T-5168, Sigma); and SMAD2 (#3103, Cell Signaling), phospho-SMAD2 (#3101S, Cell Signaling), phospho-p38MAPK (#9211S, Cell Signaling), SMAD4 (#9515, Cell Signaling); CD68 (#MCA1815, AbD Serotec, Bio-Rad); KLF4 (#12173, Cell Signaling); PU.1 (#sc-352, Santa Cruz Biotechnology); TGFβR1 (#3712, Cell Signaling); TGFβR2 (#sc-400, Santa Cruz Biotechnology); Caveolin (#610059, BD Transduction Laboratories); CD71 (#13113, Cell Signaling); GAPDH (#AM4300, Ambion).

    Techniques: Gene Expression, Control, Real-time Polymerase Chain Reaction, Expressing, Western Blot

    Chol-Loading Downregulates TGFβ Signaling in hVSMC hVSMCs were treated with Chol (5 μg/mL) or 0.2% bovine serum albumin (CT; ie, 0 μg/mL cholesterol) for 24 hours in the presence or absence of TGFβ1 ligand (10 pg/mL). Total RNA was isolated and quantitative polymerase chain reaction (qPCR) was performed to determine the pri-Mir143/145 precursor transcripts (A,B) or SMC markers, Acta2 and Tagln (C,D). hVSMCs were treated as in A and B, but either in the presence or absence of TGFβ1 10 pg/mL) and/or nonscrambled (NS) or Mir145 mimic (60 nmol/L). qPCR was performed to determine expression of Acta2 (E) and (F) Srf mRNA. (G) hVSMCs were treated as in A and B, but either in the presence or in absence of TGFβ1 (10 pg/mL) and/or Mir145 inhibitor (60 nmol/L). qPCR was performed to determine expression of Acta2. (H) Immunofluorescence images of total SMAD2/3 (green) in hVSMCs after 24 hours of the indicated treatments. Cytoplasm was stained with phalloidin (red). Nuclei were determined as phalloidin negative area (bar = 50 μm). (I) hVSMCs were treated as in A and B, but with varying amounts of Chol and in the presence or absence of recombinant TGFβ1 (10 pg/mL) for 24 hours. Proteins were extracted for Western blotting to detect phosphorylated (p) SMAD2/3, and α-SMA. Total SMAD2/3 or GAPDH was used as loading CT proteins. Blots are representative of at least 3 independent experiments, and the replicates were quantified by densitometry. For data comparisons of 2 or more independent groups, 1-way or 2-way analysis of variance followed by Dunnett post hoc test was performed. Data are presented as the mean ± SEM of 3 independent experiments, and P values are as indicated (∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, ∗∗∗∗ P < 0.0001). ns = not significant; other abbreviations as in .

    Journal: JACC: Basic to Translational Science

    Article Title: HDL Regulates TGFβ-Receptor Lipid Raft Partitioning, Restoring Contractile Features of Cholesterol-Loaded Vascular Smooth Muscle Cells

    doi: 10.1016/j.jacbts.2025.101461

    Figure Lengend Snippet: Chol-Loading Downregulates TGFβ Signaling in hVSMC hVSMCs were treated with Chol (5 μg/mL) or 0.2% bovine serum albumin (CT; ie, 0 μg/mL cholesterol) for 24 hours in the presence or absence of TGFβ1 ligand (10 pg/mL). Total RNA was isolated and quantitative polymerase chain reaction (qPCR) was performed to determine the pri-Mir143/145 precursor transcripts (A,B) or SMC markers, Acta2 and Tagln (C,D). hVSMCs were treated as in A and B, but either in the presence or absence of TGFβ1 10 pg/mL) and/or nonscrambled (NS) or Mir145 mimic (60 nmol/L). qPCR was performed to determine expression of Acta2 (E) and (F) Srf mRNA. (G) hVSMCs were treated as in A and B, but either in the presence or in absence of TGFβ1 (10 pg/mL) and/or Mir145 inhibitor (60 nmol/L). qPCR was performed to determine expression of Acta2. (H) Immunofluorescence images of total SMAD2/3 (green) in hVSMCs after 24 hours of the indicated treatments. Cytoplasm was stained with phalloidin (red). Nuclei were determined as phalloidin negative area (bar = 50 μm). (I) hVSMCs were treated as in A and B, but with varying amounts of Chol and in the presence or absence of recombinant TGFβ1 (10 pg/mL) for 24 hours. Proteins were extracted for Western blotting to detect phosphorylated (p) SMAD2/3, and α-SMA. Total SMAD2/3 or GAPDH was used as loading CT proteins. Blots are representative of at least 3 independent experiments, and the replicates were quantified by densitometry. For data comparisons of 2 or more independent groups, 1-way or 2-way analysis of variance followed by Dunnett post hoc test was performed. Data are presented as the mean ± SEM of 3 independent experiments, and P values are as indicated (∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, ∗∗∗∗ P < 0.0001). ns = not significant; other abbreviations as in .

    Article Snippet: The primary antibodies used were as follows: ACTA2 (#A2547, Sigma); CNN1 (#M3556, DAKO); SRF (#5147, Cell Signaling); p38MAPK (#sc-535, Santa Cruz Biotechnology); SMAD2/3 (#8685, Cell Signaling); TUBA (#T-5168, Sigma); and SMAD2 (#3103, Cell Signaling), phospho-SMAD2 (#3101S, Cell Signaling), phospho-p38MAPK (#9211S, Cell Signaling), SMAD4 (#9515, Cell Signaling); CD68 (#MCA1815, AbD Serotec, Bio-Rad); KLF4 (#12173, Cell Signaling); PU.1 (#sc-352, Santa Cruz Biotechnology); TGFβR1 (#3712, Cell Signaling); TGFβR2 (#sc-400, Santa Cruz Biotechnology); Caveolin (#610059, BD Transduction Laboratories); CD71 (#13113, Cell Signaling); GAPDH (#AM4300, Ambion).

    Techniques: Isolation, Real-time Polymerase Chain Reaction, Expressing, Immunofluorescence, Staining, Recombinant, Western Blot