Antibodies employed were: anti-lamin A/C, goat polyclonal (Byorbit orb37882, Cambridge, UK) used at 1:100 dilution for IF and in situ proximity ligation assay (PLA); anti-lamin A/C (E1, Santa Cruz Biotechnology, Dallas, TX, USA) used at 1:500 dilution for IF and in situ proximity ligation assay (PLA) and 1:2000 for WB; anti-desmin (Abcam Ab15200 Cambridge, UK) used 1:1000 for IF and 1:2000 for PLA and WB; anti-desmin (Chemicon 1:400 for IF; phalloidin (Sigma-Aldrich, St. Louis, MO, USA) 1:1000 for IF; anti H3k9ac (Abcam, Cambridge, UK) 1:200 for IF; anti YAP (Santa Cruz Biotechnology, Dallas, TX, USA) 1:100 for IF; anti-emerin (Monosan, Uden, The Netherlands) 1:100 for IF; anti-FLAG tag (Sigma-Aldrich, St. Louis, MO, USA) 1:1000 for IF; anti-plectin 1 (D6A11, Cell signaling Technology, Danvers, MA, USA) 1:100 for IF and PLA.
Anti h3k9ac
Manufactured by Abcam
Sourced in United States, United Kingdom
Anti-H3K9ac is a primary antibody that specifically recognizes acetylated lysine 9 on histone H3. This antibody can be used to detect and quantify the levels of this histone modification in various cell and tissue samples.
Automatically generated - may contain errors
Lab products found in correlation
Anti h3k27ac, by Abcam (7 mentions)
Anti h3k4me3, by Abcam (6 mentions)
Anti h3k9me3, by Abcam (5 mentions)
Anti h3k36me3, by Abcam (4 mentions)
Anti flag, by Merck Group (3 mentions)
Anti h3, by Abcam (3 mentions)
Anti h3k14ac, by Abcam (3 mentions)
Anti h3k9me2, by Abcam (3 mentions)
Anti β actin, by Abcam (2 mentions)
Anti β actin, by Merck Group (2 mentions)
Anti neun, by Merck Group (2 mentions)
Anti h4k5ac, by Merck Group (2 mentions)
Anti h3k122ac, by Abcam (2 mentions)
Anti h4k12ac, by Abcam (2 mentions)
Anti acss2 t, by Thermo Fisher Scientific (2 mentions)
Anti acss2 cs, by Cell Signaling Technology (2 mentions)
Anti acl, by Proteintech (2 mentions)
Anti kat3a cbp, by Abcam (2 mentions)
Anti map2 c d, by Cell Signaling Technology (2 mentions)
Anti nr4a2, by Santa Cruz Biotechnology (2 mentions)
28 protocols using anti h3k9ac
1
Antibodies Used for Lamin, Desmin, and Chromatin Analysis
2
Chromatin Extraction and Immunoblotting for Histone Marks
3
ChIP-seq Analysis of CTCF Binding
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To investigate the binding of CCCTC-binding factor (CTCF) to chromatin, ChIP analysis was carried out after sonicating the chromatin to an average fragment size of 250-300 bp following the previously described procedure [45 (link), 46 (link)]. The sequences of primers used for qPCR were given in Supplementary Table 5 and their location is depicted in Figure 4B . Although the amplicons are not tiled, the average size of chromatin fragments ensured that CTCF is absent from the entire region under consideration. Epigenetic modifications of histones were studied at nucleosomal level by Nuc-ChIP [31 (link), 32 (link)]. The following antibodies were used: anti-H3K9ac (Abcam, ab-4441); anti-H3K9me3 (Abcam, ab-8898); anti-H3K27ac (Abcam, ab-4729); anti-H3K27me3 (Millipore, 07-449); anti-H3K4me3 (Abcam, ab-8580); anti-H3K36me3 (Abcam, ab-9050); anti-H3K20m (Abcam, ab-9051); anti-β-actin (Abcam, ab-8227).
4
Western Blot Analysis of Protein Expression
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Protein lysates for western blotting were harvested in Laemmli lysis buffer (62.5 mM Tris-HCl, pH 6.8, 20% glycerol, 2% SDS, 2 mM DTT) with proteinase inhibitor freshly added. The following primary antibodies were used for immunoblotting: anti-BRD4 (Bethyl, A301-985-50, dilution 1:5,000), anti-Myogenin (Santa Cruz Biotechnology, sc-576, dilution 1; 500), anti-Troponin-T (Sigma, T6277, dilution 1:2000), anti-β-actin (Sigma, A1978, dilution 1: 10,000), anti-G9a (Cell Signaling, 3306S, dilution 1: 300), anti-H3K9ac (Abcam, ab4441, dilution 1:1,000), and normal rabbit IgG (Santa Cruz Biotech, sc-2027).
5
Yeast Chromatin Immunoprecipitation Assay
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S. cerevisiae (BY4743) and a homozygous diploid S. paradoxus (generated from the CBS432 strain by transient HO inactivation) were used. ChIP antibodies to acetyl K9 of histone H3 (anti-H3K9ac), tri-methyl K4 of histone H3 (anti-H3K4me3), and an unmodified histone H3 were from Abcam (ab4441, ab8580, and ab1791, respectively).
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S. cerevisiae (BY4743) and a homozygous diploid S. paradoxus (generated from the CBS432 strain by transient HO inactivation) were used. ChIP antibodies to acetyl K9 of histone H3 (anti-H3K9ac), tri-methyl K4 of histone H3 (anti-H3K4me3), and an unmodified histone H3 were from Abcam (ab4441, ab8580, and ab1791, respectively).
6
Profiling Histone Modifications and Neuronal Markers
7
Chromatin Extraction and Immunoblotting for Histone Marks
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For histone marks analyses, whole-cell extracts were prepared as described (Gardner et al., 2005 (link)) with minor changes. Cells from log-phase yeast cultures were harvested by centrifugation and lysed in 400 mL of SUME buffer (8 M urea, 1% SDS, 10 mM MOPS at pH 6.8, 10 mM EDTA, 0.01% bromophenol blue) by mechanical shearing. For RNA Pol II phosphoSer2 and phosphoSer5 analyses, extracts were prepared by treating cell pellets with 0.2M NaOH for 5min and boiling the samples in 2x Laemmli buffer for 5min. Extracts were cleared from debris through centrifugation. Antibodies used in this study were as follows: anti-H3K9ac (Abcam, ab4441), anti-Flag (Sigma, M2), anti-H3K4me3 (Abcam, ab8580), anti-H3K36me3 (Abcam, ab9050), anti-RNA Pol II phosphoSer2 (3E10, Active Motif), anti-RNA Pol II phosphoSer5 (3E8, Active Motif) and anti-Taf4 (gift from P. Anthony Weil).
8
Antibody Characterization for Cell Analysis
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The antibodies used in this study included: anti-BRD9 (Active Motif, Carlsbad, CA, USA, #61537), anti-TUFT1 (Abcam, Cambridge, MA, USA, ab184949), anti-E-cadherin (Cell Signaling Technology, Beverly, MA, USA, #3195), anti-N-cadherin (Cell Signaling Technology, #14215), anti-vimentin (Cell Signaling Technology, #5741), anti-H3K27Ac (Abcam, ab4729), anti-H3K14Ac (Abcam, ab52946), anti-H3K9Ac (Abcam, ab4441), anti-P300 (Abcam, ab10485), anti-AKT (Cell Signaling Technology, #4691), anti-phospho-AKT (Ser-473, Cell Signaling Technology, #4060), anti-MYC (Cell Signaling Technology, #9402), and anti-GAPDH (Santa Cruz Biotechnology, Dallas, TX, USA, sc-47724).
9
Polyclonal Antibodies for Histone Modifications
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Rabbit polyclonal antisera against dNDF and hNDF were generated with purified full-length Escherichia coli synthesized proteins at Pocono Rabbit Farm and Laboratory. The following commercial antibodies were used in this study: anti-H3K56ac (1:450 dilution; Millipore Sigma, 07-677I), anti-H3K56ac (1:1000 dilution; Active Motif, 39281), anti-H3K56ac (1:1000 dilution; Cell Signaling Technology, 4243), anti-H3 (1:4000 dilution; Cell Signaling Technology, 4499), anti-H3K9ac (1:1000 dilution; Abcam, ab8898), anti-H3K36me3 (1:1000 dilution; Abcam, ab9050), anti-his (1:1000 dilution; Santa Cruz Biotechnology, sc-803), and anti-Pol II (1:1000 dilution; Santa Cruz Biotechnology, sc-9001).
10
Placental Histone Modification Analysis
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To explore the histone modification levels in placentas from natural conception and ARTs. Global H3K4me3, H3K9ac, and H3K27ac were compared via IHC on placental tissues. After pre-treatment of formalin-fixed, paraffin-embedded sections, placental tissues were incubated with primary antibodies for 16 h at 4 °C. The primary antibodies included rabbit anti-H3K4me3 (1:100; Abcam, Cambridge, MA, USA, Cat# ab8580; RRID: AB_306649), anti-H3K9ac (1:200, Abcam Cat# ab32129, RRID: AB_732920), anti-H3K27ac (1:2,000; Abcam, Cat# ab177178; RRID: AB_2828007), mouse anti- Polr2A (1:500, OriGene, Rockville, MD, USA, Cat# CF810050), rabbit anti- KDM5A (1:300, Thermo Fisher Scientific, Waltham, MA, USA, Cat# PA5-50741; RRID: AB_2636193). For detection, a horseradish peroxidase-coupled anti-mouse/rabbit polymer system (Zytomed Systems, Berlin, Germany, Cat# POLHRP-100) was used with DAB (Dako, Glostrup, Denmark, Cat# K3468) as the chromogen. The expression of primary antibodies was evaluated by two independent, blinded observers using semi-quantitative IRS [57 (link)]. IRS (range of 0 to 12) was obtained by multiplying the score of intensity (0 = no; 1 = weak; 2 = moderate; or 3 = strong staining) and that of the extent of positive cells (0 = none; 1 = 1–10%; 2 = 11–50%; 3 = 51–80%; 4 = 81–100%).
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