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 journalArticlepeer-review

49 Scopus citations


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
Issue number10
StatePublished - Oct 2013

Bibliographical note

Funding Information:
Institute for Genomics and Systems Biology High-throughput Genome Analysis facility. This work was supported by US National Institutes of Health grants (R21 DA025725 and RC1 DA028779 to S.K., GM085394 to B.D.S., U01 HG004264 to K.P.W. and U01 ES017154 to P.J.F.), and the University of Chicago Comprehensive Cancer Center (to S.K.).


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