Histone fractions were extracted from cardiomyocytes or the mice’s left ventricle (LV), and then Western blotting was performed [8 (link),37 (link)]. Each loading sample containing the same amount (15 µg/10 µL) of protein was transferred to a Nitrocellulose membrane (Hybond ECL, GE healthcare, Chicago, IL, USA). The membrane was incubated with specific antibodies for anti-acetyl-histone H3K9 (#9649, Cell Signaling Technology, Danvers, MA, USA) and anti-histone H3 (#4499, Cell Signaling Technology) antibodies. Western blotting signals were visualized with an Amersham Imager 680 imager (GE Healthcare, Chicago, IL, USA) and quantified with NIH ImageJ software (version 1.52a).
Anti acetyl histone h3k9
Manufactured by Cell Signaling Technology
Sourced in United States
The Anti-acetyl-histone H3K9 product from Cell Signaling Technology is a laboratory reagent used to detect acetylation of histone H3 at lysine 9 (H3K9ac) through immunochemical techniques. It is a highly specific antibody that binds to the acetylated form of this histone modification.
Automatically generated - may contain errors
Lab products found in correlation
Anti histone h3, by Cell Signaling Technology (4 mentions)
Amersham imager 680, by GE Healthcare (2 mentions)
Amersham imager, by Cytiva (2 mentions)
Hybond ecl, by GE Healthcare (1 mentions)
Hybond, by Cytiva (1 mentions)
Polyvinylidene difluoride membrane, by Merck Group (1 mentions)
Anti grp75, by Abcam (1 mentions)
Anti ndufb8, by Abcam (1 mentions)
Anti sod2, by Abcam (1 mentions)
Anti histone h4, by Merck Group (1 mentions)
Anti acetylated histone h4 k16, by Merck Group (1 mentions)
4 protocols using anti acetyl histone h3k9
1
Histone Extraction and Western Blotting
2
Protein Profiling of Liver and Mitochondrial Lysates
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The liver lysate and mitochondrial lysate proteins were separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. These proteins were then transferred to polyvinylidene difluoride membranes (Millipore, Bedford, MA, USA) and blocked overnight at 4°C with 1–3% skim milk and 0.1% Tween 20 in Tris-buffered saline, which was followed by incubation at room temperature for 1 h with a primary antibody. Anti-rabbit carnitine palmitoyl transferase I (CPT I), anti-rabbit CPT II (Alpha Diagnostic International, San Antonio, TX, USA), anti-rabbit SREBP1 (Santa Cruz Biotechnology Inc., Santa Cruz, CA, USA), or anti-bacterially expressed mouse CCAAT/enhancer-binding protein homology protein (CHOP) fusion protein (Abcam, Cambridge, England) were used for the liver lysate proteins. Anti-SOD2 (Abcam), anti-Grp75 (mitochondrial heat shock protein70; Abcam), or anti-NDUFB8 (mitochondrial complex I) antibody (Abcam) were used for the mitochondrial lysates. The proteins were blocked for 1 h at room temperature and then incubated overnight at 4°C with a Phospho-stat3 (pSTAT3) antibody (Cell Signaling Technology Inc., Danvers, MA, USA) and a Phospho-Smad1/Smad5/Smad8 (pSMAD1/5/8) antibody (Cell Signaling Technology Inc.).The anti-acetylhistoneH3K9 and anti-histoneH3 (Cell Signaling Technology Inc,) were used for the nuclear lysates.
3
Histone Acetylation Analysis in Rat Cells
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Histone fractions were isolated from primary cultured neonatal rats and SD rats as described previously [23 (link),26 (link)]. The fractions were subjected to SDS-PAGE followed by Western blotting. Anti-acetyl-histone H3K9 (#9649, Cell Signaling Technology, Danvers, MA, USA) and anti-histone H3 (#4499, Cell Signaling Technology, USA) antibodies were used for Western blotting. Chemiluminescent signals were visualized using an Amersham Imager 680 (GE Healthcare Life Science, São Paulo, SP, Brazil) and quantified with Image J (1.52v).
4
Histone Extraction and Western Blot Analysis
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Cells were harvested by trypsinization and acid extraction of histone proteins was carried out by lysing cells in PBS with 0.5% Triton X-100, 2 mM phenylmethyl sulphonyl fluoride (PMSF) and 0.02% NaN3. Nuclei were pelleted by centrifugation at 1,000g and the nuclear pellet was incubated at 4 °C overnight in 0.2 N HCl 63 (link). Western blot analysis was carried out as described above using 5 μg of acid-soluble lysate per sample. Antibodies used were as follows: anti-histone H3 (Cell Signaling #9715, 1:1,000), anti-acetyl-histone H3K9 (Cell Signaling #9649P, 1:1,000), anti-histone H4 (Millipore 07-108, 1:250) and anti-acetylated histone H4K16 (Millipore 07-108, 1:500).
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