Cargando…
Renewable, recombinant antibodies to histone post-translational modifications
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 wi...
| Autores principales: | , , , , , , , , , , , , , |
|---|---|
| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
2013
|
| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3828030/ https://www.ncbi.nlm.nih.gov/pubmed/23955773 http://dx.doi.org/10.1038/nmeth.2605 |
| _version_ | 1782291178660560896 |
|---|---|
| author | Hattori, Takamitsu Taft, Joseph M. Swist, Kalina M. Luo, Hao Witt, Heather Slattery, Matthew Koide, Akiko Ruthenburg, Alexander J. Krajewski, Krzysztof Strahl, Brian D. White, Kevin P. Farnham, Peggy J. Zhao, Yingming Koide, Shohei |
| author_facet | Hattori, Takamitsu Taft, Joseph M. Swist, Kalina M. Luo, Hao Witt, Heather Slattery, Matthew Koide, Akiko Ruthenburg, Alexander J. Krajewski, Krzysztof Strahl, Brian D. White, Kevin P. Farnham, Peggy J. Zhao, Yingming Koide, Shohei |
| author_sort | Hattori, Takamitsu |
| collection | PubMed |
| description | 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. |
| format | Online Article Text |
| id | pubmed-3828030 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 2013 |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-38280302014-04-01 Renewable, recombinant antibodies to histone post-translational modifications Hattori, Takamitsu Taft, Joseph M. Swist, Kalina M. Luo, Hao Witt, Heather Slattery, Matthew Koide, Akiko Ruthenburg, Alexander J. Krajewski, Krzysztof Strahl, Brian D. White, Kevin P. Farnham, Peggy J. Zhao, Yingming Koide, Shohei Nat Methods Article 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. 2013-08-18 2013-10 /pmc/articles/PMC3828030/ /pubmed/23955773 http://dx.doi.org/10.1038/nmeth.2605 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
| spellingShingle | Article Hattori, Takamitsu Taft, Joseph M. Swist, Kalina M. Luo, Hao Witt, Heather Slattery, Matthew Koide, Akiko Ruthenburg, Alexander J. Krajewski, Krzysztof Strahl, Brian D. White, Kevin P. Farnham, Peggy J. Zhao, Yingming Koide, Shohei Renewable, recombinant antibodies to histone post-translational modifications |
| title | Renewable, recombinant antibodies to histone post-translational modifications |
| title_full | Renewable, recombinant antibodies to histone post-translational modifications |
| title_fullStr | Renewable, recombinant antibodies to histone post-translational modifications |
| title_full_unstemmed | Renewable, recombinant antibodies to histone post-translational modifications |
| title_short | Renewable, recombinant antibodies to histone post-translational modifications |
| title_sort | renewable, recombinant antibodies to histone post-translational modifications |
| topic | Article |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3828030/ https://www.ncbi.nlm.nih.gov/pubmed/23955773 http://dx.doi.org/10.1038/nmeth.2605 |
| work_keys_str_mv | AT hattoritakamitsu renewablerecombinantantibodiestohistoneposttranslationalmodifications AT taftjosephm renewablerecombinantantibodiestohistoneposttranslationalmodifications AT swistkalinam renewablerecombinantantibodiestohistoneposttranslationalmodifications AT luohao renewablerecombinantantibodiestohistoneposttranslationalmodifications AT wittheather renewablerecombinantantibodiestohistoneposttranslationalmodifications AT slatterymatthew renewablerecombinantantibodiestohistoneposttranslationalmodifications AT koideakiko renewablerecombinantantibodiestohistoneposttranslationalmodifications AT ruthenburgalexanderj renewablerecombinantantibodiestohistoneposttranslationalmodifications AT krajewskikrzysztof renewablerecombinantantibodiestohistoneposttranslationalmodifications AT strahlbriand renewablerecombinantantibodiestohistoneposttranslationalmodifications AT whitekevinp renewablerecombinantantibodiestohistoneposttranslationalmodifications AT farnhampeggyj renewablerecombinantantibodiestohistoneposttranslationalmodifications AT zhaoyingming renewablerecombinantantibodiestohistoneposttranslationalmodifications AT koideshohei renewablerecombinantantibodiestohistoneposttranslationalmodifications |