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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/anti+srf/pm41861925-89-9-11
    Average 86 stars, based on 1 article reviews
    anti srf - by Bioz Stars, 2026-10
    86/100 stars

    Images

    Related Articles

    Immunoprecipitation:

    Article Title: Zinc finger transcription factor Egf1 promotes non-alcoholic fatty liver disease
    Article Snippet: .. Aliquots of lysates containing 100 lg of protein were used for each immunoprecipitation reaction with anti-SRF (Cell Signaling Tech, Danvers, MA, USA, 5147), anti-Egr1 (Cell Signaling Tech, 4154), anti-NGFI-A binding protein 1 (Nab1) (Novus Biologicals, Minneapolis, MN, USA, NBP1-71838), antiacetyl H3K9 (Millipore, Burlington, MA, USA, 07-352), anti-acetyl H3K27 (Millipore, Burlington, MA, USA 07-360), anti-acetyl H3K14 (Millipore, Burlington, MA, USA, 07-353), anti-acetyl H3K18 (Millipore, 07-354), or IgG followed by adsorption to protein A/G PLUS-agarose beads (Santa Cruz Biotechnology, Santa Cruz, CA, USA). ..

    Binding Assay:

    Article Title: Zinc finger transcription factor Egf1 promotes non-alcoholic fatty liver disease
    Article Snippet: .. Aliquots of lysates containing 100 lg of protein were used for each immunoprecipitation reaction with anti-SRF (Cell Signaling Tech, Danvers, MA, USA, 5147), anti-Egr1 (Cell Signaling Tech, 4154), anti-NGFI-A binding protein 1 (Nab1) (Novus Biologicals, Minneapolis, MN, USA, NBP1-71838), antiacetyl H3K9 (Millipore, Burlington, MA, USA, 07-352), anti-acetyl H3K27 (Millipore, Burlington, MA, USA 07-360), anti-acetyl H3K14 (Millipore, Burlington, MA, USA, 07-353), anti-acetyl H3K18 (Millipore, 07-354), or IgG followed by adsorption to protein A/G PLUS-agarose beads (Santa Cruz Biotechnology, Santa Cruz, CA, USA). ..

    Adsorption:

    Article Title: Zinc finger transcription factor Egf1 promotes non-alcoholic fatty liver disease
    Article Snippet: .. Aliquots of lysates containing 100 lg of protein were used for each immunoprecipitation reaction with anti-SRF (Cell Signaling Tech, Danvers, MA, USA, 5147), anti-Egr1 (Cell Signaling Tech, 4154), anti-NGFI-A binding protein 1 (Nab1) (Novus Biologicals, Minneapolis, MN, USA, NBP1-71838), antiacetyl H3K9 (Millipore, Burlington, MA, USA, 07-352), anti-acetyl H3K27 (Millipore, Burlington, MA, USA 07-360), anti-acetyl H3K14 (Millipore, Burlington, MA, USA, 07-353), anti-acetyl H3K18 (Millipore, 07-354), or IgG followed by adsorption to protein A/G PLUS-agarose beads (Santa Cruz Biotechnology, Santa Cruz, CA, USA). ..

    Incubation:

    Article Title: SRF fusion oncogenes encode constitutively activated chimeric transcription factors in myoid soft tissue tumors
    Article Snippet: Samples (30 μg) were mixed with 4x Laemmli buffer (0.2 M Tris-HCl pH 6.8, 8% SDS, 0.4% bromophenol blue, 40% glycerol, 2.8% β-mercaptoethanol), boiled for 5 min, and analyzed by western blot using Novex Tris-Glycine 4–12% gels (Thermo Fisher Scientific) and PVDF membranes (Amersham Hybond P, GE Healthcare). .. Membranes were blocked in 5% milk for 1 h at room temperature, then incubated overnight at 4°C with the indicated primary antibodies : anti-HA-tag (#3724, Cell Signaling Technology, Danvers, MA, USA), anti-Myc-Tag (#2272, Cell Signaling Technology), anti-phospho-STAT1 (#9167, Cell Signaling Technology), anti-STAT1 (#610115, BD BioSciences), anti-phospho-STAT3 (#9145, Cell Signaling Technology), anti-STAT3 (#12640, Cell Signaling Technology), anti-phospho-STAT5 (#9351, Cell Signaling Technology), anti-STAT5 (#94205, Cell Signaling Technology), anti-SRF (#5147, Cell Signaling Technology), anti-phospho-PDGFRβ (#3170, Cell Signaling Technology), anti-PDGFRB (#3169, Cell Signaling Technology), anti-β-actin (#A5441, Sigma-Aldrich). .. Detection was performed using chemiluminescence (Fusion Solo S, Vilber).

    Article Title: circFAM53B-1 and circFAM53B-2 drive VSMC phenotypic modulation via ISG15-mediated suppression of SRF.
    Article Snippet: Although circRNAs have been widely studied in various disease contexts, their roles in vascular smooth muscle cells (VSMCs) phenotypic modulation remain incompletely understood.. This study aims to investigate the regulatory functions and molecular mechanisms of two newly identified circRNAs, circFAM53B-1 and circFAM53B2, in VSMCs phenotypic switching.. Here, we show that both circFAM53B-1 and circFAM53B-2 were upregulated by PDGF-BB in a KLF4-dependent manner.

    Article Title: Single-molecule analysis reveals that IPMK enhances the DNA-binding activity of the transcription factor SRF.
    Article Snippet: For western blotting analysis, TMR-positive cells were sorted with FACS (Bio-Rad S3e). .. For chromatin immunoprecipitation (ChIP) assay, magnetic beads were washed with radioimmunoprecipitation assay (RIPA) wash buffer and incubated with either normal rabbit IgG (Cell Signaling Technology, 2729) or anti-SRF (Cell Signaling Technology, 5147) antibodies. ..

    Article Title: Single-molecule analysis reveals that IPMK enhances the DNA-binding activity of the transcription factor SRF
    Article Snippet: For western blotting analysis, TMR-positive cells were sorted with FACS (Bio-Rad S3e). .. For chromatin immunoprecipitation (ChIP) assay, magnetic beads were washed with radioimmunoprecipitation assay (RIPA) wash buffer and incubated with either normal rabbit IgG (Cell Signaling Technology, 2729) or anti-SRF (Cell Signaling Technology, 5147) antibodies. ..

    Staining:

    Article Title: circFAM53B-1 and circFAM53B-2 drive VSMC phenotypic modulation via ISG15-mediated suppression of SRF.
    Article Snippet: Although circRNAs have been widely studied in various disease contexts, their roles in vascular smooth muscle cells (VSMCs) phenotypic modulation remain incompletely understood.. This study aims to investigate the regulatory functions and molecular mechanisms of two newly identified circRNAs, circFAM53B-1 and circFAM53B2, in VSMCs phenotypic switching.. Here, we show that both circFAM53B-1 and circFAM53B-2 were upregulated by PDGF-BB in a KLF4-dependent manner.

    Chromatin Immunoprecipitation:

    Article Title: Single-molecule analysis reveals that IPMK enhances the DNA-binding activity of the transcription factor SRF.
    Article Snippet: For western blotting analysis, TMR-positive cells were sorted with FACS (Bio-Rad S3e). .. For chromatin immunoprecipitation (ChIP) assay, magnetic beads were washed with radioimmunoprecipitation assay (RIPA) wash buffer and incubated with either normal rabbit IgG (Cell Signaling Technology, 2729) or anti-SRF (Cell Signaling Technology, 5147) antibodies. ..

    Article Title: Single-molecule analysis reveals that IPMK enhances the DNA-binding activity of the transcription factor SRF
    Article Snippet: For western blotting analysis, TMR-positive cells were sorted with FACS (Bio-Rad S3e). .. For chromatin immunoprecipitation (ChIP) assay, magnetic beads were washed with radioimmunoprecipitation assay (RIPA) wash buffer and incubated with either normal rabbit IgG (Cell Signaling Technology, 2729) or anti-SRF (Cell Signaling Technology, 5147) antibodies. ..

    Magnetic Beads:

    Article Title: Single-molecule analysis reveals that IPMK enhances the DNA-binding activity of the transcription factor SRF.
    Article Snippet: For western blotting analysis, TMR-positive cells were sorted with FACS (Bio-Rad S3e). .. For chromatin immunoprecipitation (ChIP) assay, magnetic beads were washed with radioimmunoprecipitation assay (RIPA) wash buffer and incubated with either normal rabbit IgG (Cell Signaling Technology, 2729) or anti-SRF (Cell Signaling Technology, 5147) antibodies. ..

    Article Title: Single-molecule analysis reveals that IPMK enhances the DNA-binding activity of the transcription factor SRF
    Article Snippet: For western blotting analysis, TMR-positive cells were sorted with FACS (Bio-Rad S3e). .. For chromatin immunoprecipitation (ChIP) assay, magnetic beads were washed with radioimmunoprecipitation assay (RIPA) wash buffer and incubated with either normal rabbit IgG (Cell Signaling Technology, 2729) or anti-SRF (Cell Signaling Technology, 5147) antibodies. ..

    Radio Immunoprecipitation:

    Article Title: Single-molecule analysis reveals that IPMK enhances the DNA-binding activity of the transcription factor SRF.
    Article Snippet: For western blotting analysis, TMR-positive cells were sorted with FACS (Bio-Rad S3e). .. For chromatin immunoprecipitation (ChIP) assay, magnetic beads were washed with radioimmunoprecipitation assay (RIPA) wash buffer and incubated with either normal rabbit IgG (Cell Signaling Technology, 2729) or anti-SRF (Cell Signaling Technology, 5147) antibodies. ..

    Article Title: Single-molecule analysis reveals that IPMK enhances the DNA-binding activity of the transcription factor SRF
    Article Snippet: For western blotting analysis, TMR-positive cells were sorted with FACS (Bio-Rad S3e). .. For chromatin immunoprecipitation (ChIP) assay, magnetic beads were washed with radioimmunoprecipitation assay (RIPA) wash buffer and incubated with either normal rabbit IgG (Cell Signaling Technology, 2729) or anti-SRF (Cell Signaling Technology, 5147) antibodies. ..

    Real-time Polymerase Chain Reaction:

    Article Title: Functional screen identifies RBM42 as a mediator of oncogenic mRNA translation specificity.
    Article Snippet: Oncogenic protein dosage is tightly regulated to enable cancer formation but how this is regulated by translational control remains unknown.. The Myc oncogene is a paradigm of an exquisitely regulated oncogene and a driver of pancreatic ductal adenocarcinoma (PDAC).. Here we use a CRISPR interference screen in PDAC cells to identify activators of selective MYC translation.

    Isolation:

    Article Title: Functional screen identifies RBM42 as a mediator of oncogenic mRNA translation specificity.
    Article Snippet: Oncogenic protein dosage is tightly regulated to enable cancer formation but how this is regulated by translational control remains unknown.. The Myc oncogene is a paradigm of an exquisitely regulated oncogene and a driver of pancreatic ductal adenocarcinoma (PDAC).. Here we use a CRISPR interference screen in PDAC cells to identify activators of selective MYC translation.



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    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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    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