@article{7193d9d04d554075a2a3f0160c6e84bf,
title = "Recombinant antibodies to histone post-translational modifications",
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.",
author = "Takamitsu Hattori and Taft, {Joseph M.} and Swist, {Kalina M.} and Hao Luo and Heather Witt and Matthew Slattery and Akiko Koide and Ruthenburg, {Alexander J.} and Krzysztof Krajewski and Strahl, {Brian D.} and White, {Kevin P.} and Farnham, {Peggy J.} and Yingming Zhao and Shohei Koide",
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.).",
year = "2013",
month = oct,
doi = "10.1038/nmeth.2605",
language = "English",
volume = "10",
pages = "992--995",
journal = "Nature Methods",
issn = "1548-7091",
publisher = "Nature Publishing Group",
number = "10",
}