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Active Motif nuclear extracts hela, hepg2 u-937 cells
Origin of cell lines used for screening of mammary gland-specific complex (MGSC) binding to the −941/−930 palindromic site
Nuclear Extracts Hela, Hepg2 U 937 Cells, supplied by Active Motif, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/nuclear extracts hela, hepg2 u-937 cells/product/Active Motif
Average 90 stars, based on 1 article reviews
nuclear extracts hela, hepg2 u-937 cells - by Bioz Stars, 2026-02
90/100 stars

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1) Product Images from "A 5′ distal palindrome within the mouse mammary tumor virus-long terminal repeat recruits a mammary gland-specific complex and is required for a synergistic response to progesterone plus prolactin"

Article Title: A 5′ distal palindrome within the mouse mammary tumor virus-long terminal repeat recruits a mammary gland-specific complex and is required for a synergistic response to progesterone plus prolactin

Journal: Journal of molecular endocrinology

doi: 10.1677/JME-08-0027

Origin of cell lines used for screening of mammary gland-specific complex (MGSC) binding to the −941/−930 palindromic site
Figure Legend Snippet: Origin of cell lines used for screening of mammary gland-specific complex (MGSC) binding to the −941/−930 palindromic site

Techniques Used: Binding Assay



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Image Search Results


Origin of cell lines used for screening of mammary gland-specific complex (MGSC) binding to the −941/−930 palindromic site

Journal: Journal of molecular endocrinology

Article Title: A 5′ distal palindrome within the mouse mammary tumor virus-long terminal repeat recruits a mammary gland-specific complex and is required for a synergistic response to progesterone plus prolactin

doi: 10.1677/JME-08-0027

Figure Lengend Snippet: Origin of cell lines used for screening of mammary gland-specific complex (MGSC) binding to the −941/−930 palindromic site

Article Snippet: The exceptions were nuclear extracts from HeLa, HepG2 and U-937 cells that were purchased from Active Motif (Carlsbad, CA, USA).

Techniques: Binding Assay

(A–C) HepG2 (A), Hep3B (B) and HuH7 (C) hepatoma tumor cells were treated with different concentrations of resveratrol (5 µM, 10 µM, 20 µM, 50 µM and 100 µM) or solvent as control and monitored for an additional time period of 96 h. Cellular impedance was measured over the entire observation time using the xCELLigence™ SP system and calculated by the RTCA Software 1.2.1.1002. All cell index (CI) values were normalized when treatment started. Displayed are normalized CI values every 5 h. As a positive control for cell death, Triton X-100 0.1% was used. (D–F) Sulforhodamine B (SRB) assay of HepG2 (D), Hep3B (E) and HuH7 (F) cells treated with increasing concentrations of resveratrol (5 µM, 10 µM, 20 µM, 50 µM and 100 µM) or solvent as control for 96 h. Shown are mean ± SD of three independent experiments, each performed in triplicates (A–F); One-way ANOVA Dunnetts multiple comparison test, * P <0.01 (D–F).

Journal: PLoS ONE

Article Title: Resveratrol as a Pan-HDAC Inhibitor Alters the Acetylation Status of Jistone Proteins in Human-Derived Hepatoblastoma Cells

doi: 10.1371/journal.pone.0073097

Figure Lengend Snippet: (A–C) HepG2 (A), Hep3B (B) and HuH7 (C) hepatoma tumor cells were treated with different concentrations of resveratrol (5 µM, 10 µM, 20 µM, 50 µM and 100 µM) or solvent as control and monitored for an additional time period of 96 h. Cellular impedance was measured over the entire observation time using the xCELLigence™ SP system and calculated by the RTCA Software 1.2.1.1002. All cell index (CI) values were normalized when treatment started. Displayed are normalized CI values every 5 h. As a positive control for cell death, Triton X-100 0.1% was used. (D–F) Sulforhodamine B (SRB) assay of HepG2 (D), Hep3B (E) and HuH7 (F) cells treated with increasing concentrations of resveratrol (5 µM, 10 µM, 20 µM, 50 µM and 100 µM) or solvent as control for 96 h. Shown are mean ± SD of three independent experiments, each performed in triplicates (A–F); One-way ANOVA Dunnetts multiple comparison test, * P <0.01 (D–F).

Article Snippet: For HepG2 HDAC inhibition determination, nuclear extract of HepG2 cells (Active Motif) was used.

Techniques: Solvent, Control, Software, Positive Control, Sulforhodamine B Assay, Comparison

(A) Detection of intracellular acetylated protein levels in HepG2, Hep3B and HuH7 hepatoma cells after incubation of resveratrol (5 µM, 10 µM, 20 µM, 50 µM and 100 µM) or solvent as control for 6 h. (B) Overall HDAC inhibition in nuclear extracts of HepG2 cells by increasing concentrations of resveratrol (5 µM, 10 µM, 20 µM, 50 µM and 100 µM) or solvent as control. As a reference inhibitor suberoylanilide hydroxamic acid (SAHA; 100 µM) was used. (C) Western blot analysis of acetylated histone complex H3 in HepG2 tumor cells treated with 50 µM and 100 µM of resveratrol or solvent as control. Acetylation of H3 was examined using cellular lysates. Equal protein loading was verified by vinculin staining (upper row). As a reference and positive control for hyperacetylation the cells were treated with 2 µM SAHA. Acetylation levels were calculated performing a densitometric analysis. Shown are mean ± SD of three independent experiments, each performed in triplicates (A and B); One-way ANOVA Dunnetts multiple comparison test, * P <0.01, n.s. indicates not significant (A and B).

Journal: PLoS ONE

Article Title: Resveratrol as a Pan-HDAC Inhibitor Alters the Acetylation Status of Jistone Proteins in Human-Derived Hepatoblastoma Cells

doi: 10.1371/journal.pone.0073097

Figure Lengend Snippet: (A) Detection of intracellular acetylated protein levels in HepG2, Hep3B and HuH7 hepatoma cells after incubation of resveratrol (5 µM, 10 µM, 20 µM, 50 µM and 100 µM) or solvent as control for 6 h. (B) Overall HDAC inhibition in nuclear extracts of HepG2 cells by increasing concentrations of resveratrol (5 µM, 10 µM, 20 µM, 50 µM and 100 µM) or solvent as control. As a reference inhibitor suberoylanilide hydroxamic acid (SAHA; 100 µM) was used. (C) Western blot analysis of acetylated histone complex H3 in HepG2 tumor cells treated with 50 µM and 100 µM of resveratrol or solvent as control. Acetylation of H3 was examined using cellular lysates. Equal protein loading was verified by vinculin staining (upper row). As a reference and positive control for hyperacetylation the cells were treated with 2 µM SAHA. Acetylation levels were calculated performing a densitometric analysis. Shown are mean ± SD of three independent experiments, each performed in triplicates (A and B); One-way ANOVA Dunnetts multiple comparison test, * P <0.01, n.s. indicates not significant (A and B).

Article Snippet: For HepG2 HDAC inhibition determination, nuclear extract of HepG2 cells (Active Motif) was used.

Techniques: Incubation, Solvent, Control, Inhibition, Western Blot, Staining, Positive Control, Comparison