Alvarez, Claudia
Harding, Rachel
Ackloo, Suzanne
Hutchinson, Ashley
Seitova, Alma
Arrowsmith, Cheryl
2019-08-02
<p>The purification of HTT fragments is a useful approach to learn more about the function of huntingtin in the cell. By obtaining soluble and monomeric samples of HTT domains namely the HTT 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. </p>
<p>Expression and purification of these fragments can be found on these posts <a href="https://zenodo.org/record/2600051#.XKU89aeZPOQ">https://zenodo.org/record/2600051#.XKU89aeZPOQ</a> and <a href="https://zenodo.org/record/2628060#.XULMtnspDb0">https://zenodo.org/record/2628060#.XULMtnspDb0</a> (performed by Dr. Rachel Harding). The latest post shows the successful purification of a monomeric and mono disperse sample of the HTT C-HEAT domain. The results here presented are a follow up of those experiments and aim to further characterize the HTT C-HEAT domain as well as explore strategies to improve buffer conditions for crystallization purposes.</p>
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, Innovation and Science (MRIS), Pfizer, São Paulo Research Foundation-FAPESP, Takeda, and Wellcome.
https://doi.org/10.5281/zenodo.3358864
oai:zenodo.org:3358864
Zenodo
https://zenodo.org/communities/sgc-opennotebook
https://zenodo.org/communities/openlabnotebooks
https://doi.org/10.5281/zenodo.3358863
info:eu-repo/semantics/openAccess
Creative Commons Attribution 4.0 International
https://creativecommons.org/licenses/by/4.0/legalcode
HTT
Huntingtin
Purification
HTT domain
C-HEAT
Purification of the HTT C-HEAT domain (2088-3144)
info:eu-repo/semantics/other