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Characterization of a novel polyclonal anti-hypusine antibody
The translation factor eIF5A is the only protein known to contain the amino acid hypusine, which is formed posttranslationally. Hypusinated eIF5A is necessary for cellular proliferation and responses to extracellular stressors, and has been proposed as a target for pharmacologic therapy. Here, we pr...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer International Publishing
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3765601/ https://www.ncbi.nlm.nih.gov/pubmed/24024105 http://dx.doi.org/10.1186/2193-1801-2-421 |
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author | Nishiki, Yurika Farb, Thomas B Friedrich, Jessica Bokvist, Krister Mirmira, Raghavendra G Maier, Bernhard |
author_facet | Nishiki, Yurika Farb, Thomas B Friedrich, Jessica Bokvist, Krister Mirmira, Raghavendra G Maier, Bernhard |
author_sort | Nishiki, Yurika |
collection | PubMed |
description | The translation factor eIF5A is the only protein known to contain the amino acid hypusine, which is formed posttranslationally. Hypusinated eIF5A is necessary for cellular proliferation and responses to extracellular stressors, and has been proposed as a target for pharmacologic therapy. Here, we provide the first comprehensive characterization of a novel polyclonal antibody (IU-88) that specifically recognizes the hypusinated eIF5A. IU-88 will be useful for the investigation of eIF5A biology and for the development of assays recognizing hypusinated eIF5A. |
format | Online Article Text |
id | pubmed-3765601 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Springer International Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-37656012013-09-10 Characterization of a novel polyclonal anti-hypusine antibody Nishiki, Yurika Farb, Thomas B Friedrich, Jessica Bokvist, Krister Mirmira, Raghavendra G Maier, Bernhard Springerplus Technical Note The translation factor eIF5A is the only protein known to contain the amino acid hypusine, which is formed posttranslationally. Hypusinated eIF5A is necessary for cellular proliferation and responses to extracellular stressors, and has been proposed as a target for pharmacologic therapy. Here, we provide the first comprehensive characterization of a novel polyclonal antibody (IU-88) that specifically recognizes the hypusinated eIF5A. IU-88 will be useful for the investigation of eIF5A biology and for the development of assays recognizing hypusinated eIF5A. Springer International Publishing 2013-08-29 /pmc/articles/PMC3765601/ /pubmed/24024105 http://dx.doi.org/10.1186/2193-1801-2-421 Text en © Nishiki et al.; licensee Springer. 2013 This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Technical Note Nishiki, Yurika Farb, Thomas B Friedrich, Jessica Bokvist, Krister Mirmira, Raghavendra G Maier, Bernhard Characterization of a novel polyclonal anti-hypusine antibody |
title | Characterization of a novel polyclonal anti-hypusine antibody |
title_full | Characterization of a novel polyclonal anti-hypusine antibody |
title_fullStr | Characterization of a novel polyclonal anti-hypusine antibody |
title_full_unstemmed | Characterization of a novel polyclonal anti-hypusine antibody |
title_short | Characterization of a novel polyclonal anti-hypusine antibody |
title_sort | characterization of a novel polyclonal anti-hypusine antibody |
topic | Technical Note |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3765601/ https://www.ncbi.nlm.nih.gov/pubmed/24024105 http://dx.doi.org/10.1186/2193-1801-2-421 |
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