Published in

Nature Research, Nature Methods, 10(10), p. 992-995, 2013

DOI: 10.1038/nmeth.2605

Links

Tools

Export citation

Search in Google Scholar

Recombinant antibodies to histone post-translational modifications

Journal article published in 2013 by 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 ORCID, Yingming Zhao, Shohei Koide
This paper is available in a repository.
This paper is available in a repository.

Full text: Download

Green circle
Preprint: archiving allowed
Upload
Orange circle
Postprint: archiving restricted
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

Abstract

Variability in the quality of antibodies to histone post-translational modifications (PTMs) presents widely recognized hindrance in epigenetics research. Here, by using antibody engineering technologies we produced recombinant antibodies directed 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 their high specificity enabled us to identify positive and negative correlations among histone PTMs.