Purification of HTT N-HEAT_81-1643

<p>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.&nbsp;&nbsp;</p> <p>The first 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 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.</p>