H3k79me1

Manufactured by Cell Signaling Technology

Sourced in United States

H3K79me1 is a histone modification-specific antibody that recognizes monomethylation of lysine 79 on histone H3. This antibody can be used for applications such as chromatin immunoprecipitation (ChIP) and western blotting to study the distribution and regulation of this epigenetic mark.

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3 protocols using h3k79me1

Antibodies for Protein Analysis Techniques

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The following primary antibodies were used in western blotting assays: NPM1 mutant (NB110-61646, Novus, Littleton, USA), NPM1 WT (Thermo scientific, Rockford, USA), NPM1 (Sigma-Aldrich, St. Louis, USA), PBX3 (Abcam, Cambridge, USA), HOXA9 (Abcam, Cambridge, USA), Cleaved caspase 3, Cleaved PARP (Cell Signaling, Danvers, USA), Flag, H3K4me2, H3K9me2, H3K27me2, H3K36me2, H3K79me1, H3K79me2, H3K79me3, H3, DOT1L (Cell Signaling, Danvers, USA), and β-Actin (Sigma, St. Louis, MO, USA).
All antibodies and the following kits applied in flow cytometry analyses were purchased from BD Biosciences (BD Pharmingen™, New Jersey, USA): CD45.1, CD45.2, Mac-1, Gr-1, Sca-1, c-Kit, Mouse Lineage Panel, AnnexinV Apoptosis Detection kit, and BrdU Flow kit.
Immunofluorescence staining was performed with Flag (Cell Signaling, Danvers, USA), H3K79me2 (Cell Signaling, Danvers, USA and PMT-bio, Hangzhou, China), PBX3 (Santa Cruz, California, USA), HOXA9 (Abcam, Cambridge, USA) and NPM1 antibodies as following: NPM1 mutant (Novus, Littleton, USA), NPM1 WT (Thermo scientific, Rockford, USA), NPM1 (Cell Signaling, Danvers, USA).

Zhang W., Zhao C., Zhao J., Zhu Y., Weng X., Chen Q., Sun H., Mi J.Q., Li J., Zhu J., Chen Z., Pandolfi P.P., Chen S., Yan X, & Xu J. (2018). Inactivation of PBX3 and HOXA9 by down-regulating H3K79 methylation represses NPM1-mutated leukemic cell survival. Theranostics, 8(16), 4359-4371.

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Compound Dose-Dependent Protein Analysis

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3 × 10⁶ cells/well were treated with increasing concentrations of a compound for 1 day, and whole proteins were extracted. Equal amounts of proteins were separated on SDS-PAGE and transferred to PVDF membranes. The blots were probed with primary antibodies, followed by anti-rabbit IgG (Thermo Scientific) secondary antibodies. The primary antibodies against ENL (Cell signaling #14893), AF9 (Novusbio #NB100-1565), DOT1L (Cell signaling #77087), AFF4 (Abcam #ab103586), Cyclin T1 (Cell signaling #81464), H3K79me2 (Cell signaling #5427), H3K79me1 (Cell signaling #9398), Histone H3 (Cell signaling #4499), FLAG (Sigma-Aldrich #F1804), β-Actin (Cell signaling #4970) were used in this study.

Li X., Yao Y., Wu F, & Song Y. (2022). A proteolysis-targeting chimera molecule selectively degrades ENL and inhibits malignant gene expression and tumor growth. Journal of Hematology & Oncology, 15, 41.

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Cell Proliferation Assay Protocol

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The CellTiter 96 Aqueous ONE Solution Cell Proliferation Assay was purchased from Promega Corp. (Madison, WI, USA). NVP-AUY922 (AUY922) (>99% purity) was from Selleckchem.com (Houston, TX, USA). Ganetespib (STA9090) (98.79% purity) and SNX2112 (98% purity) were purchased from ApexBio (Houston, TX, USA). AT13387 (>98%) was from MedChem Express (Princeton, NJ, USA), CUDC305 (>98% purity) was from AbMole BioScience (Houston, TX, USA), and dimethyl sulfoxide (DMSO) was from Sigma-Aldrich (St. Louis, MO, USA). AUY922, ganetespib, SNX2112, AT13387, and CUDC305 were dissolved in DMSO separately and stored at −20 °C. Polyclonal antibodies against histone H3, H4, H3K4me3, H3K18ac, and H4K12ac were purchased from Abcam (Cambridge, MA, USA). Monoclonal or polyclonal antibodies against acetyl-histone H3, acetyl-histone H4, and H3K27ac were bought from EMD Millipore Corporation (Billerica, MA, USA). Monoclonal or polyclonal antibodies against histone H3K4me1, H3K4me2, H3K23ac, H3K79me1, H3K79me2, H4K8ac, and H4K20me3 were obtained from Cell Signaling Technology (Danvers, MA, USA). Restore Western Blot Stripping Buffer was from Thermo Scientific (Rockford, IL, USA). All other reagents were from Sigma-Aldrich.

Li Q.Q., Hao J.J., Zhang Z., Krane L.S., Hammerich K.H., Sanford T., Trepel J.B., Neckers L, & Agarwal P.K. (2017). Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics. Scientific Reports, 7, 201.

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