Purification of HTT N-HEAT_81-1643

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.亨廷顿蛋白（huntingtin，HTT）片段的纯化，是深入解析HTT在细胞内功能的有效途径。通过获取HTT结构域（包括C-HEAT、N-HEAT及桥接结构域）的可溶性单体样品，可开展特异性蛋白质-蛋白质相互作用的相关研究。此外，可溶性单体形式的HTT结构域，还可用于结晶学研究。上述片段的首次表达与纯化方法，可参阅以下两篇帖子：https://zenodo.org/record/2600051#.XKU89aeZPOQ 与 https://zenodo.org/record/2628060#.XULMtnspDb0（该工作由Rachel Harding博士完成）。最新发布的帖子展示了HTT N-HEAT_81-1643结构域构建体的纯化流程，该结构域在Superdex 200 10/300 GL凝胶过滤层析柱上的洗脱峰位于外水体积处。本文展示的实验结果，正是该纯化工作的后续研究成果。