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Related Concept Videos

Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
DNA Isolation01:34

DNA Isolation

DNA from cells is required for many biotechnology and research applications, such as molecular cloning. To remove and purify DNA from cells, researchers use various methods of DNA extraction. While the specifics of different protocols may vary, some general concepts underlie the process of DNA extraction.

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Related Experiment Video

Updated: Jul 14, 2026

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry
10:54

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry

Published on: November 21, 2025

Extraction, purification and analysis of histones.

David Shechter1, Holger L Dormann, C David Allis

  • 1The Laboratory of Chromatin Biology, The Rockefeller University, New York, NY, USA.

Nature Protocols
|June 5, 2007
PubMed
Summary

This study details standard protocols for isolating and analyzing histone proteins and their post-translational modifications. These methods are essential for understanding histone function in crucial cellular processes like gene regulation and cell division.

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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

Published on: May 17, 2016

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Biochemistry

Background:

  • Histone proteins are fundamental components of chromatin, governing eukaryotic genome structure and function.
  • Chromatin serves as the substrate for vital cellular processes including gene regulation, replication, mitosis, and apoptosis.
  • Post-translational modifications of histones significantly impact their biological roles, necessitating accurate identification.

Purpose of the Study:

  • To present standardized biochemical protocols for the extraction, separation, and analysis of histone proteins.
  • To enable the detailed characterization of histone post-translational modifications and variant identification.
  • To provide researchers with reliable methods for studying histone biology.

Main Methods:

  • Histone extraction using acid and salt-based protocols from chromatin.
  • Separation of purified histones via reversed-phase High-Performance Liquid Chromatography (HPLC).
  • Analysis of histone profiles and post-translational modifications using acid urea (AU) gel electrophoresis, Triton AU (TAU) electrophoresis, and 2D TAU electrophoresis.
  • Immunoblotting of isolated histones using modification-specific antibodies.

Main Results:

  • Established protocols for efficient histone protein purification from eukaryotic chromatin.
  • Demonstrated the utility of various electrophoresis techniques for separating canonical and variant histones.
  • Enabled the specific detection and analysis of histone post-translational modifications.
  • Validated methods for comprehensive histone profiling.

Conclusions:

  • The presented protocols offer a robust framework for the comprehensive analysis of histones and their modifications.
  • Accurate characterization of histone proteins and their covalent marks is critical for understanding epigenetics and cellular function.
  • These methods facilitate further research into the biological significance of histone variants and modifications in various biological contexts.