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Anti h3k4me1

Manufactured by Merck Group
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Anti-H3K4me1 is a laboratory reagent used to detect the histone modification H3K4me1 (monomethylation of lysine 4 on histone H3) in various experimental techniques, such as chromatin immunoprecipitation (ChIP) and immunoblotting. This reagent can be used to investigate the epigenetic regulation of gene expression.

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Lab products found in correlation

Anti h3k4me3, by Merck Group (11 mentions) Anti h3k4me2, by Merck Group (8 mentions) Anti h3k9me2, by Merck Group (4 mentions) Anti h3k4me3, by Abcam (3 mentions) Anti pcna, by Santa Cruz Biotechnology (3 mentions) Anti h3, by Abcam (3 mentions) Anti h3k27me1, by Merck Group (3 mentions) Anti h3k27me3, by Merck Group (3 mentions) Ab9050, by Abcam (2 mentions) Anti kdm4a, by Abcam (2 mentions) Cell tak, by BD (2 mentions) Anti total h3, by Merck Group (2 mentions) Anti tubulin, by Merck Group (2 mentions) Anti rad51, by Santa Cruz Biotechnology (2 mentions) Anti h3k36me3, by Abcam (2 mentions) Nextera barcode, by Illumina (2 mentions) Anti h3k27ac, by Abcam (2 mentions) Millipore chip kit, by Merck Group (2 mentions) Hiseq 4000, by Illumina (2 mentions) Anti ha, by Abcam (2 mentions)

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H3K4me1 (27 citations)

21 protocols using anti h3k4me1

1

Histone Demethylation Assay with LSD1 Enzymes

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The in vitro demethylation assay was performed as previously described with minor modifications [51 (link)]. Briefly, a quantity of 7 μg of calf thymus histones (Sigma-Aldrich H9250, Shanghai, China) was incubated with affinity-purified GST-HsLSD1 (10 μg), GST-GmFLD (10 μg), GmLDL1a (10 μg), GmLDL1b (10 μg), or GST (10 μg) in 100 μL of reaction buffer (50 mM Tris, pH 8.5, 50 mM KCl, 5 mM MgCl2, 5% glycerol, and complete EDTA-free protease inhibitors) at 37 °C for 4 h. The reaction product was analyzed by immunoblotting with anti-H3K4me3 (Abcam ab8580, Cambridge, UK), anti-H3K4me2 (Millipore 07-030, Darmstadt, Germany), anti-H3K4me1 (Millipore 07-436, Darmstadt, Germany), anti-H3K9me2 (Abcam ab1220, Cambridge, UK), anti-H3K27me3 (Millipore 07-449, Darmstadt, Germany), anti-H3K36me3 (Abcam ab9050, Cambridge, UK), and anti-H3 (Abcam ab1791, Cambridge, UK). The relative intensity of the Western blot was quantified by ImageJ 1.8.0 (National Institutes of Health, Dickerson, FL, USA).
Liu M., Jiang J., Han Y., Shi M., Li X., Wang Y., Dong Z, & Yang C. (2022). Functional Characterization of the Lysine-Specific Histone Demethylases Family in Soybean. Plants, 11(11), 1398.
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2

Antibody Validation for Epigenetic Analysis

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Antibodies were purchased from the following companies: anti‐H3K27me1, anti‐H3K27me3, anti‐H3K79me1, anti‐H3K79me2, anti‐histone H3, anti‐hnRNP I, anti‐KDM4A, anti‐KDM5A, anti‐KDM5C, anti‐snRNP70, anti‐tubulin, and anti‐U2AF2 from Abcam (Cambridge, MA, USA); anti‐hnRNP A2/B1 from Acris (San Diego, CA, USA); anti‐SR protein‐specific kinases (SRPK)1 and anti‐SRPK2 from BD Biosciences (San Diego, CA, USA); anti‐AKT, anti‐H3K27me2, anti‐protein phosphatase‐1 (PP1), anti‐phospho‐PP1 at Thr320, anti‐phospho‐AKT at Ser473, and anti‐cleaved‐CASPASE‐3 from Cell Signaling Technology (Billerica, MA, USA); anti‐H3K4me1, anti‐H3K4me2, anti‐H3K4me3, and anti‐H3K36me3 from Millipore; anti‐pro‐CASPASE‐3 and anti‐KDM7A from GeneTex (SanAntonio, TX, USA); anti‐hnRNP C1/C2, anti‐BAX, and anti‐BCL2L1 from Santa Cruz Biotechnology (Santa Cruz, CA, USA); anti‐hnRNP A1 from Sigma; and anti‐SRSF1 and anti‐SRSF3 from Zymed (San Francisco, CA, USA).
Lee C., Chang W., Chang Y., Yang J., Chang C., Hsu K., Chen Y., Liu T., Chen Y., Lin S., Wu Y, & Chang J. (2019). Alternative splicing in human cancer cells is modulated by the amiloride derivative 3,5‐diamino‐6‐chloro‐N‐(N‐(2,6‐dichlorobenzoyl)carbamimidoyl)pyrazine‐2‐carboxide. Molecular Oncology, 13(8), 1744-1762.
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3

Immunofluorescence of Key Cellular Proteins

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Primary antibodies were used at the following dilutions: anti-tubulin (1:15,000, Sigma), anti-H3K4me3 (1:5000, Millipore), anti-H3K4me1 (1:5000, Millipore), anti-RAD51 (1:50, Santa Cruz), anti-PCNA (1:2000, Santa Cruz), anti-total H3 (1:1000 Millipore), and anti-Mre11 (1:10,000, gift from J. Petrini, MSKCC). MEFs were prepared for immunofluorescence by growth on 18 mm × 18 mm glass cover slips. Lymphocytes were dropped onto slides coated with CellTak (BD Biosciences). Cells were fixed with methanol and incubated with primary antibody as indicated.
Chaudhuri A.R., Callen E., Ding X., Gogola E., Duarte A.A., Lee J.E., Wong N., Lafarga V., Calvo J.A., Panzarino N.J., John S., Day A., Crespo A.V., Shen B., Starnes L.M., de Ruiter J.R., Daniel J.A., Konstantinopoulos P.A., Cortez D., Cantor S.B., Fernandez-Capetillo O., Ge K., Jonkers J., Rottenberg S., Sharan S.K, & Nussenzweig A. (2016). Replication Fork Stability Confers Chemoresistance in BRCA-deficient Cells. Nature, 535(7612), 382-387.
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4

ChIP-seq protocol for Drosophila and mouse

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For ChIP-seq, Drosophila S2 cells and mouse bone marrow-derived macrophages (BMDM) were cross-linked for 10 min with 1% formaldehyde. ChIP material was prepared independently for each cell type as described previously (Henriques et al. 2013 (link)). To ensure proper normalization between RNAPII ChIP-seq of control and Spt5-depleted cells, S2 cells and BMDM ChIP material were pooled in a 10:1 ratio (Drosophila to mice), and immunoprecipitations were carried out with anti-Rpb3 (Drosophila) and total anti-RNAPII antibody (mice; Santa Cruz Biotechnology, H-224). For the remaining ChIP-seq libraries, separate immunoprecipitations were performed with anti-cohesin (gift from D. Dorsett), anti-H3K4me1 (Millipore, 07-436), anti-H3K4me3 (Millipore, 07-473), anti-H3K27ac (Abcam, ab4729), and anti-H3K36me3 (Abcam, ab9050) antibodies. Immunoprecipitated material was purified using the Qiaquick PCR purification kit, and ChIP-seq libraries were prepared using the NEXTflex ChIP-seq kit (Bioo Scientific) according to the manufacturer's instructions.
Henriques T., Scruggs B.S., Inouye M.O., Muse G.W., Williams L.H., Burkholder A.B., Lavender C.A., Fargo D.C, & Adelman K. (2018). Widespread transcriptional pausing and elongation control at enhancers. Genes & Development, 32(1), 26-41.
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5

Chromatin Immunoprecipitation Antibody Panel

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The following antibodies were used in this study: anti-H3K4me1 (Millipore Sigma 07-436, Burlington, MA, 1:2000), anti-H3K4me2 (Millipore Sigma 07-030, 1:1000), anti-H3K4me3 (Millipore Sigma 07-473 or 04-745, 1:2000), anti-H3 (Abcam 1791, Cambridge, UK, 1:3000), rat monoclonal anti-Ser2P CTD (3E10, Dirk Eick, 1:1000), rat monoclonal anti-Ser5P CTD (3E8, Dirk Eick, 1:3000), mouse monoclonal anti-CTD for total Rpb1 (8WG16, Buratowski lab, 1:1000), anti-Set1 (Santa Cruz, sc-101858, 1:1000), anti-TBP polyclonal antiserum (Buratowski lab, 1:3000), anti-Myc (MMS-150R-500, Covance, 1:2000), anti-β-Actin (Abcam 8224, 1:2000), anti-HA (3F10, Roche and 12CA5, 1:2000), anti-Gal4 DBD (sc-577, Santa Cruz, 1:1000).
Bae H.J., Dubarry M., Jeon J., Soares L.M., Dargemont C., Kim J., Geli V, & Buratowski S. (2020). The Set1 N-terminal domain and Swd2 interact with RNA polymerase II CTD to recruit COMPASS. Nature Communications, 11, 2181.
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6

Immunofluorescence of Key Cellular Proteins

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Primary antibodies were used at the following dilutions: anti-tubulin (1:15,000, Sigma), anti-H3K4me3 (1:5000, Millipore), anti-H3K4me1 (1:5000, Millipore), anti-RAD51 (1:50, Santa Cruz), anti-PCNA (1:2000, Santa Cruz), anti-total H3 (1:1000 Millipore), and anti-Mre11 (1:10,000, gift from J. Petrini, MSKCC). MEFs were prepared for immunofluorescence by growth on 18 mm × 18 mm glass cover slips. Lymphocytes were dropped onto slides coated with CellTak (BD Biosciences). Cells were fixed with methanol and incubated with primary antibody as indicated.
Chaudhuri A.R., Callen E., Ding X., Gogola E., Duarte A.A., Lee J.E., Wong N., Lafarga V., Calvo J.A., Panzarino N.J., John S., Day A., Crespo A.V., Shen B., Starnes L.M., de Ruiter J.R., Daniel J.A., Konstantinopoulos P.A., Cortez D., Cantor S.B., Fernandez-Capetillo O., Ge K., Jonkers J., Rottenberg S., Sharan S.K, & Nussenzweig A. (2016). Replication Fork Stability Confers Chemoresistance in BRCA-deficient Cells. Nature, 535(7612), 382-387.
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7

Histone Modification Profiling by ChIP-seq

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1–2 × 106 isolated cells were fixed and nuclei prepared for sonication. Sonication was performed using a Bioruptor sonication water bath. ChIP was performed with anti-H3K4me1 (Millipore) and anti-H3K27Ac (Abcam) using the Millipore ChIP Kit (17–295). ChIP and input sample libraries were prepared by tagmentation coupled to indexing with Illumina Nextera barcodes described above. Samples were analyzed for quality, then sequenced on a HiSeq 4000 (Illumina).
Kennedy D.E., Okoreeh M.K., Maienschein-Cline M., Ai J., Veselits M., McLean K.C., Dhugana Y., Wang H., Peng J., Chi H., Mandal M, & Clark M.R. (2020). Novel specialized cell state and spatial compartments within the germinal center. Nature immunology, 21(6), 660-670.
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8

Histone Extraction and Immunoprecipitation from Embryonic Stem Cells

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ESCs or EBs were lysed with RIPA buffer (Pierce) in the presence of EDTA free protease inhibitor cocktail (Sigma). Histone extraction on EBs was performed using a histone extraction kit (Abcam) as described previously (Khan et al., 2015 (link)). Protein concentration was determined using Pierce BCA protein assay kit (ThermoFisher Scientific). 1.0 μg of histone extracts, or 10 μg of whole cell lysate was resolved on 4%–20% precast gel (Bio-Rad) was transferred to 0.45 μm PVDF membrane (Millipore). For immunoprecipitation, day 2 WT and Wdr5KO EBs were harvested and lysed in RIPA buffer with EDTA free protease inhibitor cocktail (Sigma). 1 mg sonicated cell lysates were subjected to immunoprecipitation using WDR5 antibody (Bethyl). The following primary antibodies were used for probing: anti-HA (1:10,000, Abcam, ab9110), anti-WDR5 (1:5000, R&D), anti-WDR5 (1:5,000, Bethyl), anti-Flag (1:2,000, Sigma), anti-H3 (1:10,000, Abcam), anti-H3K4Me1 (1:5,000, Millipore), anti-H3K4Me2 (1:10,000, Millipore), anti-H3K4Me3 (1:10,000, Abcam), anti-P53 (1:5,000, Cell Signaling), anti-Tubulin (1:10,000, Cell signaling), anti-β-Actin (1:10,000, Cell signaling), anti-Phospho-p53 (Ser15) Antibody (1:5,000, Cell Signaling), anti-Phospho-p53 (Ser392) Antibody (1:5,000, Abcam), anti-Acetyl-p53 (K305) Antibody (1:5,000, Abcam), anti-Actyl-p53 (K379) Antibody (1:5,000, Cell Signaling).
Li Q., Mao F., Zhou B., Huang Y., Zou Z., denDekker A.D., Xu J., Hou S., Liu J., Dou Y, & Rao R.C. (2020). p53 Integrates Temporal WDR5 Inputs during Neuroectoderm and Mesoderm Differentiation of Mouse Embryonic Stem Cells. Cell reports, 30(2), 465-480.e6.
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9

Histone Extraction and Immunoprecipitation from Embryonic Stem Cells

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ESCs or EBs were lysed with RIPA buffer (Pierce) in the presence of EDTA free protease inhibitor cocktail (Sigma). Histone extraction on EBs was performed using a histone extraction kit (Abcam) as described previously (Khan et al., 2015 (link)). Protein concentration was determined using Pierce BCA protein assay kit (ThermoFisher Scientific). 1.0 μg of histone extracts, or 10 μg of whole cell lysate was resolved on 4%–20% precast gel (Bio-Rad) was transferred to 0.45 μm PVDF membrane (Millipore). For immunoprecipitation, day 2 WT and Wdr5KO EBs were harvested and lysed in RIPA buffer with EDTA free protease inhibitor cocktail (Sigma). 1 mg sonicated cell lysates were subjected to immunoprecipitation using WDR5 antibody (Bethyl). The following primary antibodies were used for probing: anti-HA (1:10,000, Abcam, ab9110), anti-WDR5 (1:5000, R&D), anti-WDR5 (1:5,000, Bethyl), anti-Flag (1:2,000, Sigma), anti-H3 (1:10,000, Abcam), anti-H3K4Me1 (1:5,000, Millipore), anti-H3K4Me2 (1:10,000, Millipore), anti-H3K4Me3 (1:10,000, Abcam), anti-P53 (1:5,000, Cell Signaling), anti-Tubulin (1:10,000, Cell signaling), anti-β-Actin (1:10,000, Cell signaling), anti-Phospho-p53 (Ser15) Antibody (1:5,000, Cell Signaling), anti-Phospho-p53 (Ser392) Antibody (1:5,000, Abcam), anti-Acetyl-p53 (K305) Antibody (1:5,000, Abcam), anti-Actyl-p53 (K379) Antibody (1:5,000, Cell Signaling).
Li Q., Mao F., Zhou B., Huang Y., Zou Z., denDekker A.D., Xu J., Hou S., Liu J., Dou Y, & Rao R.C. (2020). p53 Integrates Temporal WDR5 Inputs during Neuroectoderm and Mesoderm Differentiation of Mouse Embryonic Stem Cells. Cell reports, 30(2), 465-480.e6.
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10

Histone Modification and Signaling Pathway Analysis

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Cells were harvested and lysed in RIPA buffer with protease inhibitors and 2 μM PMSF. Protein extracts were boiled in SDS sample buffer for 5 min, loaded directly onto a 4–12% SDS gel, transferred onto nitrocellulose membranes (Bio-Rad), blocked with 5% milk, and incubated with corresponding primary and secondary antibodies using standard protocols. The following antibodies were used: anti-H3K4me1 (Cat # 07-436, 1:2000 dilution), anti-H3K4me2 (Cat # 07-030, 1:4000 dilution), anti-H3K4me3 (Cat # 07-473, 1:4000 dilution), anti-H3K9me1 (Cat # 07-450, 1:2000 dilution), anti-H3K9me2 (Cat # 07-441, 1:3000 dilution), anti-H3K9me3 (Cat # 07-442, 1:3000 dilution), anti-H3K27me1 (Cat # 07-448, 1:2000 dilution), anti-H3K27me2 (Cat # 07-452, 1:4000 dilution), and anti-H3K27me3 (Cat # 07-449, 1:4000 dilution) from Millipore; rabbit anti-Jmjd3 (Cat # ab1022a, 1:500 dilution) from Abgent; and mouse anti-FLAG (1:5000 dilution), anti-HRP-FLAG (1:5000 dilution), and anti-β-actin (1:5000 dilution) from Sigma; anti-Smad1 (Cat # 6944, 1:500 dilution), anti-Smad2 (Cat # 5339, 1:500 dilution) and anti-Smad3 (Cat # 9523, 1:500 dilution) from Cell Signaling; and anti-Ash2L (Cat # ab50699, 1:500 dilution) from Abcam.
Li Q., Zou J., Wang M., Ding X., Chepelev I., Zhou X., Zhao W., Wei G., Cui J., Zhao K., Wang H.Y, & Wang R.F. (2014). Critical role of histone demethylase Jmjd3 in the regulation of CD4+ T cell differentiation. Nature communications, 5, 5780.
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