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Published September 26, 2019 | Version v1
Dataset Open

Purification of HTT N-HEAT_81-1643

Creators

  • 1. Structural Genomics Consortium, UofT

Description

The purification of huntingtin (HTT) fragments is a useful approach to learn more about the function of HTT in the cell. By obtaining soluble and monomeric samples of HTT domains namely the C-HEAT, N-HEAT and bridge domains, specific protein-protein interactions can be studied. Furthermore, domains of HTT in soluble monomeric form could enable crystallization studies.  

The first expression and purification of these fragments can be found on these posts https://zenodo.org/record/2600051#.XKU89aeZPOQ and https://zenodo.org/record/2628060#.XULMtnspDb0 (performed by Dr. Rachel Harding). The latest post shows the purification of construct the HTT N-HEAT_81-1643 domain which elutes from Superdex 200 10/300 GL column in the void volume. The results here presented are a follow up of that purification.

Notes

Dr. Harding is the recipient of the Huntington's Disease Society of America Berman Topper Career Development Fellowship which funds and supports this research, in addition to generous funding from the CHDI Foundation and the Huntington Society of Canada. The SGC is a registered charity (number 1097737) that receives funds from AbbVie, Bayer Pharma AG, Boehringer Ingelheim, Canada Foundation for Innovation, Eshelman Institute for Innovation, Genome Canada through Ontario Genomics Institute [OGI-055], Innovative Medicines Initiative (EU/EFPIA) [ULTRA-DD grant no. 115766], Janssen, Merck KGaA, Darmstadt, Germany, MSD, Novartis Pharma AG, Ontario Ministry of Research, Innovation and Science (MRIS), Pfizer, São Paulo Research Foundation-FAPESP, Takeda, and Wellcome.

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20190603 N-termHTT (81-1643).pdf

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