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

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dc.contributor.authorKim, Hyeongjuko
dc.contributor.authorHyun, Kyung-giko
dc.contributor.authorLloret, Alejandroko
dc.contributor.authorSeong, Ihn Sikko
dc.contributor.authorSong, Ji-Joonko
dc.date.accessioned2022-06-06T06:00:14Z-
dc.date.available2022-06-06T06:00:14Z-
dc.date.created2022-06-06-
dc.date.created2022-06-06-
dc.date.issued2021-12-
dc.identifier.citationSTAR Protocols, v.2, no.4-
dc.identifier.issn2666-1667-
dc.identifier.urihttp://hdl.handle.net/10203/296828-
dc.description.abstractHuntington'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).-
dc.languageEnglish-
dc.publisherCell Press-
dc.titlePurification of full-length recombinant human huntingtin proteins with allelic series of polyglutamine lengths-
dc.typeArticle-
dc.identifier.scopusid2-s2.0-85122837099-
dc.type.rimsART-
dc.citation.volume2-
dc.citation.issue4-
dc.citation.publicationnameSTAR Protocols-
dc.identifier.doi10.1016/j.xpro.2021.100886-
dc.contributor.localauthorSong, Ji-Joon-
dc.contributor.nonIdAuthorHyun, Kyung-gi-
dc.contributor.nonIdAuthorLloret, Alejandro-
dc.contributor.nonIdAuthorSeong, Ihn Sik-
dc.description.isOpenAccessN-
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