I am performing western blots on some old brain tissue and I did a BCA and I basically would need to add 200ul of each protein sample to achieve the right concentration which obviously too much for gel electrophoresis. I think the person who isolated this tissue a few years ago added too much lysis buffer because the sample is clear and usually it is at least a little cloudy. I am trying to figure out the best way to concentrate these protein samples and I am not sure if the lysis buffer will play a role. It looks like the simplest method is TCA or acetone precipitation... Does anyone have any input?

Thanks!