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Characterization of a polyclonal antibody that is highly selective for the d-isoAsp-25 variant of mammalian histone H2B
Approximately 12% of histone H2B molecules in mammalian brain contain a modification wherein Asp25 is present as the d-enantiomer, and is mostly linked to Gly26 via the side-chain carboxyl. Here we (1) demonstrate the high specificity of a polyclonal antibody to this modification, and (2) use this A...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Springer Vienna
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10140013/ https://www.ncbi.nlm.nih.gov/pubmed/36717395 http://dx.doi.org/10.1007/s00726-023-03242-z |
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author | Aswad, Dana W. O’Leary, Kevin S. Williams, Katherine |
author_facet | Aswad, Dana W. O’Leary, Kevin S. Williams, Katherine |
author_sort | Aswad, Dana W. |
collection | PubMed |
description | Approximately 12% of histone H2B molecules in mammalian brain contain a modification wherein Asp25 is present as the d-enantiomer, and is mostly linked to Gly26 via the side-chain carboxyl. Here we (1) demonstrate the high specificity of a polyclonal antibody to this modification, and (2) use this Ab to demonstrate that this modification is enriched in brain relative to liver, thymus, and HeLa cells. |
format | Online Article Text |
id | pubmed-10140013 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Springer Vienna |
record_format | MEDLINE/PubMed |
spelling | pubmed-101400132023-04-29 Characterization of a polyclonal antibody that is highly selective for the d-isoAsp-25 variant of mammalian histone H2B Aswad, Dana W. O’Leary, Kevin S. Williams, Katherine Amino Acids Short Communication Approximately 12% of histone H2B molecules in mammalian brain contain a modification wherein Asp25 is present as the d-enantiomer, and is mostly linked to Gly26 via the side-chain carboxyl. Here we (1) demonstrate the high specificity of a polyclonal antibody to this modification, and (2) use this Ab to demonstrate that this modification is enriched in brain relative to liver, thymus, and HeLa cells. Springer Vienna 2023-01-30 2023 /pmc/articles/PMC10140013/ /pubmed/36717395 http://dx.doi.org/10.1007/s00726-023-03242-z Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Short Communication Aswad, Dana W. O’Leary, Kevin S. Williams, Katherine Characterization of a polyclonal antibody that is highly selective for the d-isoAsp-25 variant of mammalian histone H2B |
title | Characterization of a polyclonal antibody that is highly selective for the d-isoAsp-25 variant of mammalian histone H2B |
title_full | Characterization of a polyclonal antibody that is highly selective for the d-isoAsp-25 variant of mammalian histone H2B |
title_fullStr | Characterization of a polyclonal antibody that is highly selective for the d-isoAsp-25 variant of mammalian histone H2B |
title_full_unstemmed | Characterization of a polyclonal antibody that is highly selective for the d-isoAsp-25 variant of mammalian histone H2B |
title_short | Characterization of a polyclonal antibody that is highly selective for the d-isoAsp-25 variant of mammalian histone H2B |
title_sort | characterization of a polyclonal antibody that is highly selective for the d-isoasp-25 variant of mammalian histone h2b |
topic | Short Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10140013/ https://www.ncbi.nlm.nih.gov/pubmed/36717395 http://dx.doi.org/10.1007/s00726-023-03242-z |
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