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

doi:10.1038/nmeth.2605

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

Biomedical Sciences

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53 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 language	English (US)
Pages (from-to)	992-995
Number of pages	4
Journal	Nature Methods
Volume	10
Issue number	10
DOIs	https://doi.org/10.1038/nmeth.2605
State	Published - 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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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.).",

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AU - Hattori, Takamitsu

AU - Taft, Joseph M.

AU - Swist, Kalina M.

AU - Luo, Hao

AU - Witt, Heather

AU - Slattery, Matthew

AU - Koide, Akiko

AU - Ruthenburg, Alexander J.

AU - Krajewski, Krzysztof

AU - Strahl, Brian D.

AU - White, Kevin P.

AU - Farnham, Peggy J.

AU - Zhao, Yingming

AU - Koide, Shohei

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Recombinant antibodies to histone post-translational modifications

Abstract

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