Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Aswad, Dana W., O’Leary, Kevin S., Williams, Katherine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Vienna 2023
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
_version_ 1785033072330145792
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
work_keys_str_mv AT aswaddanaw characterizationofapolyclonalantibodythatishighlyselectiveforthedisoasp25variantofmammalianhistoneh2b
AT olearykevins characterizationofapolyclonalantibodythatishighlyselectiveforthedisoasp25variantofmammalianhistoneh2b
AT williamskatherine characterizationofapolyclonalantibodythatishighlyselectiveforthedisoasp25variantofmammalianhistoneh2b