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Purification of full-length recombinant human huntingtin proteins with allelic series of polyglutamine lengths

Huntington's disease (HD) is an autosomal dominant neurodegenerative disorder caused by the polyglutamine (polyQ) expansion in huntingtin (HTT) protein. The challenge of obtaining full-length HTT proteins with high purity limits the understanding of the HTT protein function. Here, we provide a...

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Autores principales: Kim, Hyeongju, Hyun, Kyung-gi, Lloret, Alejandro, Seong, Ihn Sik, Song, Ji-Joon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8551504/
https://www.ncbi.nlm.nih.gov/pubmed/34746859
http://dx.doi.org/10.1016/j.xpro.2021.100886
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author Kim, Hyeongju
Hyun, Kyung-gi
Lloret, Alejandro
Seong, Ihn Sik
Song, Ji-Joon
author_facet Kim, Hyeongju
Hyun, Kyung-gi
Lloret, Alejandro
Seong, Ihn Sik
Song, Ji-Joon
author_sort Kim, Hyeongju
collection PubMed
description Huntington's disease (HD) is an autosomal dominant neurodegenerative disorder caused by the polyglutamine (polyQ) expansion in huntingtin (HTT) protein. The challenge of obtaining full-length HTT proteins with high purity limits the understanding of the HTT protein function. Here, we provide a protocol to generate and purify full-length recombinant human HTT proteins with various polyQ lengths, which is key to investigate the biochemical function of HTT proteins and the molecular mechanism underlying HD pathology. For complete details on the use and execution of this protocol, please refer to Jung et al. (2020).
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spelling pubmed-85515042021-11-04 Purification of full-length recombinant human huntingtin proteins with allelic series of polyglutamine lengths Kim, Hyeongju Hyun, Kyung-gi Lloret, Alejandro Seong, Ihn Sik Song, Ji-Joon STAR Protoc Protocol Huntington's disease (HD) is an autosomal dominant neurodegenerative disorder caused by the polyglutamine (polyQ) expansion in huntingtin (HTT) protein. The challenge of obtaining full-length HTT proteins with high purity limits the understanding of the HTT protein function. Here, we provide a protocol to generate and purify full-length recombinant human HTT proteins with various polyQ lengths, which is key to investigate the biochemical function of HTT proteins and the molecular mechanism underlying HD pathology. For complete details on the use and execution of this protocol, please refer to Jung et al. (2020). Elsevier 2021-10-16 /pmc/articles/PMC8551504/ /pubmed/34746859 http://dx.doi.org/10.1016/j.xpro.2021.100886 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Protocol
Kim, Hyeongju
Hyun, Kyung-gi
Lloret, Alejandro
Seong, Ihn Sik
Song, Ji-Joon
Purification of full-length recombinant human huntingtin proteins with allelic series of polyglutamine lengths
title Purification of full-length recombinant human huntingtin proteins with allelic series of polyglutamine lengths
title_full Purification of full-length recombinant human huntingtin proteins with allelic series of polyglutamine lengths
title_fullStr Purification of full-length recombinant human huntingtin proteins with allelic series of polyglutamine lengths
title_full_unstemmed Purification of full-length recombinant human huntingtin proteins with allelic series of polyglutamine lengths
title_short Purification of full-length recombinant human huntingtin proteins with allelic series of polyglutamine lengths
title_sort purification of full-length recombinant human huntingtin proteins with allelic series of polyglutamine lengths
topic Protocol
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8551504/
https://www.ncbi.nlm.nih.gov/pubmed/34746859
http://dx.doi.org/10.1016/j.xpro.2021.100886
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