A Sensitive and Flexible Assay for Determining Histone Deacetylase 1 (HDAC1) Activity

Part of the Methods in Molecular Biology book series (MIMB, volume 1436)


Histones acetylation and deacetylation constitute part of the so-called “histone code” and work in concert with other posttranslational modifications to determine the activity of genes. Deacetylation of histone is carried out by a class of enzymes, known as histone deacetylases (HDACs). The action of HDAC is countered by histone acetyltransferases. Although histone is the best characterized substrate of HDACs, increasing evidence also indicates that non-histone proteins are equally important subtract of HDACs. Since HDACs play an important role in normal physiological and pathophysiological conditions, a sensitive and flexible deacetylation assay that can reliably detect HDAC activity and identify potential novel targets of HDACs is critical.

Key words

HDAC1 Deacetylation Immunoaffinity purification Core histone Posttranslational modification Colorimetric assay 



Work in the authors’ laboratory is supported by grants CA187857 and CA188471 from National Cancer Institute, and McCormick Genomic and Proteomic Center at the George Washington University.


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Copyright information

© Springer Science+Business Media New York 2016

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular MedicineThe George Washington UniversityWashingtonUSA
  2. 2.Department of Molecular and Cellular BiologyBaylor College of MedicineHoustonUSA

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