Hi folks! Recently, I have been doing some work to further characterise the huntingtin protein samples I am generating in the lab. My huntingtin protein is made in insect cells and these cells process proteins they make differently to human cells. In particular, I am keen to see whether a chemical modification called phosphorylation is present on the insect cell huntingtin and where this modification is found on huntingtin as we know phosphorylations can play an important role in the function of huntingtin protein. So far, I have run 2 experiments and I can see phosphorylations (woop!) and they seem to be located at the same positions as huntingtin from human cells – great news! This means that the huntingtin protein is likely being phosphorylated in a physiologically relevant manner.

I have also been honing in on optimizing the way I make HMGB1, a huntingtin interacting protein, in the lab and have success. You can read all about that on Zenodo. Now to probe the interaction….

HMGB1 purification