4.1 Article

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

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STAR PROTOCOLS
Volume 2, Issue 4, Pages -

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ELSEVIER
DOI: 10.1016/j.xpro.2021.100886

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Funding

  1. National Research Foundation of Korea [NRF-2016K1A1A2912057]

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This study presents a protocol for generating and purifying full-length recombinant human HTT proteins, which is crucial for investigating the biochemical function of HTT proteins and the molecular mechanism underlying Huntington's disease pathology.
Huntington's disease (HD) is an autosomal dominant neurodegenerative disor-der caused by the polyglutamine (polyQ) expansion in huntingtin (HTT) protein. The challenge of obtaining full-length HTT proteins with high purity limits the un-derstanding 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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