Recombinant antibodies to histone post-translational modifications

Takamitsu Hattori, Joseph M. Taft, Kalina M. Swist, Hao Luo, Heather Witt, Matthew Slattery, Akiko Koide, Alexander J. Ruthenburg, Krzysztof Krajewski, Brian D. Strahl, Kevin P. White, Peggy J. Farnham, Yingming Zhao, Shohei Koide

Research output: Contribution to journalArticle

41 Scopus citations

Abstract

Variability in the quality of antibodies to histone post-translational modifications (PTMs) is a widely recognized hindrance in epigenetics research. Here, we produced recombinant antibodies to the trimethylated lysine residues of histone H3 with high specificity and affinity and no lot-to-lot variation. These recombinant antibodies performed well in common epigenetics applications, and enabled us to identify positive and negative correlations among histone PTMs.

Original languageEnglish (US)
Pages (from-to)992-995
Number of pages4
JournalNature Methods
Volume10
Issue number10
DOIs
StatePublished - Oct 2013
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology
  • Biochemistry
  • Cell Biology

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  • Cite this

    Hattori, T., Taft, J. M., Swist, K. M., Luo, H., Witt, H., Slattery, M., Koide, A., Ruthenburg, A. J., Krajewski, K., Strahl, B. D., White, K. P., Farnham, P. J., Zhao, Y., & Koide, S. (2013). Recombinant antibodies to histone post-translational modifications. Nature Methods, 10(10), 992-995. https://doi.org/10.1038/nmeth.2605