Antibodies were purchased from the following companies: anti-GLA from Santa Cruz; anti-PP1, Akt, phospho-PP1 at Thr320, phospho-Akt at Ser473, phospho-Akt at Thr308 from Cell Signaling Technology; anti-hnRNP A1 from Sigma; anti-hnRNP A2B1 from Acris; anti-SRp20 and SF2/ASF from Thermo Scientific; anti-H3K4me3, anti-H3K9me3, anti-H3K27me3, anti-H3K36me3, anti-H3K9me3, anti-H3K9A, anti-H3K9A, anti-H3K23A, anti-H3K27A, anti-H3S10P, anti-histone H3, anti-actin, and anti-HSP70 from Abcam; anti-p54nrb/NONO from Affinity Bioreagents; anti-PSIP1 from Bethyl Laboratories.
Anti h3k9me3
Manufactured by Abcam
Sourced in United States, United Kingdom
Anti-H3K9me3 is a primary antibody that recognizes the trimethylated form of histone H3 at lysine 9. It is used for the detection and quantification of this epigenetic histone modification in various applications, such as Western blotting, immunoprecipitation, and chromatin immunoprecipitation (ChIP).
Automatically generated - may contain errors
Lab products found in correlation
Anti h3k4me3, by Abcam (14 mentions)
Anti h3k9me2, by Abcam (11 mentions)
Anti h3, by Abcam (8 mentions)
Anti h3k27me3, by Merck Group (8 mentions)
Anti h3k27ac, by Abcam (7 mentions)
Ab8898, by Abcam (6 mentions)
Anti h3k36me3, by Abcam (5 mentions)
Anti h3k9ac, by Abcam (5 mentions)
Anti lamin b1, by Abcam (5 mentions)
Anti lamin a c, by Santa Cruz Biotechnology (5 mentions)
Anti h3k27me3, by Abcam (4 mentions)
Anti h3k4me3, by Merck Group (4 mentions)
Anti histone h3, by Abcam (4 mentions)
Anti h3k4me1, by Abcam (4 mentions)
Anti flag, by Merck Group (4 mentions)
Anti β actin, by Merck Group (4 mentions)
Anti h3k27me3, by Cell Signaling Technology (4 mentions)
Pvdf membrane, by Merck Group (4 mentions)
Anti gfp, by Abcam (3 mentions)
Anti h3k4me3, by Active Motif (3 mentions)
83 protocols using anti h3k9me3
1
Antibody Immunoblotting for Protein Expression
2
Chromatin Immunoprecipitation of Lung Tumors
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FF lung tumor (LT; 3 mm3) samples consisting of almost 70% tumor tissue were pulverized under liquid nitrogen, fixed with 1% formaldehyde for 10 min, and immediately neutralized with 0.125 M glycine for 5 min. The resulting cells were washed with 1X PBS and treated with lysis buffer (50 mM HEPES-KOH pH 7.5, 140 mM NaCl, 1 mM EDTA pH 8, 1% Triton X-100, 0.1% sodium deoxycholate, and 0.1% SDS) containing 10 ml with protease inhibitors (complete Mini, Roche, Indianapolis, IN, USA).
The chromatin from the FF-LT samples was sonicated for 10 pulses of 20 seconds w/u 60 watts. Then, 10 μg of chromatin was immunoprecipitated (ChIP) using a commercial EZ-Magna ChIP™ G kit (Millipore, Temecula, CA, USA) and 2.5 μg of anti-MEOX2 (Santa Cruz Biotechnology, Dallas, TX, USA) as well as 1 μg of activated anti-H3K27Ac, anti-H3K4me3, anti-H3K27me3, anti-H3K9me3 or anti-RNA Pol II antibodies (Abcam, Cambridge Science Park, Cambridge, U.K.). A 1-μg aliquot of anti-mouse IgG was used as a negative control for ChIP (Millipore, Temecula, CA, USA).
The chromatin from the FF-LT samples was sonicated for 10 pulses of 20 seconds w/u 60 watts. Then, 10 μg of chromatin was immunoprecipitated (ChIP) using a commercial EZ-Magna ChIP™ G kit (Millipore, Temecula, CA, USA) and 2.5 μg of anti-MEOX2 (Santa Cruz Biotechnology, Dallas, TX, USA) as well as 1 μg of activated anti-H3K27Ac, anti-H3K4me3, anti-H3K27me3, anti-H3K9me3 or anti-RNA Pol II antibodies (Abcam, Cambridge Science Park, Cambridge, U.K.). A 1-μg aliquot of anti-mouse IgG was used as a negative control for ChIP (Millipore, Temecula, CA, USA).
3
Immunohistochemical Analysis of HBV-Positive HCC
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Immunohistochemical analyses were performed essentially as described before [10 (link), 11 (link)]. Briefly, twenty-one HBV positive HCC specimens were fixed in 10% buffered formalin. Parallel paraffin sections were stained with anti-HBx and anti-H3K9me3 (Abcam, Cambridge, UK), and then counterstained with hematoxylin. Immunoreaction scores were calculated by multiplying the percentage and intensity scores as our previously described [11 (link)].
4
ChIP-qPCR Analysis of H3K9me3 and H3S10ph
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Three independent samples were made by dissecting neural plates from 30 embryos collected at stages 3 and 5. Cells were cross-linked and sonicated to yield 300– to 800–base pair fragments. Samples were evenly split for rabbit anti-JmjD2A (Abcam, Buenos Aires, Argentina), anti-H3K9me3 (Abcam), anti-H3S10ph (Epigentek, Farmingdale, NY), control rabbit anti–immunoglobulin G (IgG; Abcam), and input. Antibodies were preincubated with protein A magnetic beads (Invitrogen, Buenos Aires, Argentina) before incubation with a sonicated protein–DNA complex. The complexes were magnetically isolated, eluted, and cross-link reversed. The DNA was purified, precipitated, and finally used as a template for qPCR analysis (see Supplemental Table S1 for a list of primers). Every sample was loaded by three replicates each. The results were quantified using the ΔΔCt method, calculated according to manufacturer’s instructions (Applied BioSystems), and expressed as fold enrichment with respect to IgG.
5
Chromatin Immunoprecipitation Antibodies
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6
ChIP-seq Protocol for Histone Modifications
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The chromatin immunoprecipitation (ChIP) assay was performed according to previously published protocols with minor modifications [52 (link)]. Chromatin was sonicated to get fragments of 100 to 700 bp and immunoprecipitated with the following antibodies anti-H3K27me3 (07–449, Millipore), anti-H3K4me3 (39159, Active Motif) and anti-H3K9me3 (ab8898, Abcam). ChIP-seq libraries were prepared using the Illumina ChIP-seq librarary prep kit, according to the manufacturers’ instructions.
7
Epigenetic Analysis of GFP-RNase H1 in Mammalian Cells
8
Immunoblotting Protocol for Protein Analysis
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Cells were lysed by using lysis buffer (containing protease inhibitor cocktail and PMSF) and the lysate was separated at 12,000g, 20 min. As per the requirement, the concentrations of the protein samples were estimated by Bradford assay. The proteins in the lysate are denatured by boiling for 10 min with 2× Laemmli buffer. The protein samples were loaded onto an SDS–PAGE gel and transferred onto a polyvinylidene difluoride membrane (BioRad). The membrane was blocked with 3% BSA at room temperature overnight, followed by incubation with primary antibodies for 1.5 h at room temperature. The secondary horseradish peroxidase (HRP)-conjugated anti-mouse IgG, HRP-conjugated anti-rabbit IgG or HRP-conjugated anti-goat IgG (1:10,000) antibodies were then added to the membrane at room temperature for 1 h. For signal detection, we used the SuperSignal West Dura Extended Duration Substrate (Thermo Scientific) and captured the blots on CLXposure films (Thermo Scientific). The primary antibodies used were anti-V5 (1:1000, ThermoFisher Scientific #R960-25), anti-ACTIN (1:1000, Santa Cruz #sc-10731), anti-FLAG (1:500, Sigma-Aldrich #F1804), anti-ESET (SETDB1) (1:2000, Santa Cruz #sc-66884), anti-SMC1A (1:2000, Bethyl #A300-055A) and anti-H3K9me3 (1:1000, Abcam #ab8898).
9
H3K9me3 Nucleosome Sequencing
10
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).
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