Currently have punched mouse brain samples of different regions that are of too low protein concentration for Western Blot. Has anyone used the polyacrylamide gel electrophoresis method to detect multiple proteins? Or read it anywhere and can link the literature? Thanks!
Here are some references, hope it can help you.
See 2.6 table 2
Article Comparison of Extraction Methods for the Comprehensive Analy...
Better lysis method may help you get higher conc. of protein.
Besides, you can take a look at this
https://www.nature.com/articles/nn.4160
Maybe you can consider design your experiment see if you can culture the tissue for having a higher amount of sample for western blot or other experiment .
When you say "too low [protein] for western blot", do you mean you've actually tested this, or are you just assuming you need to load 20-40ug per lane, and you don't have that much?
Because western blotting can be incredibly sensitive: you may be able to see useful signal even with much lower protein loads.
Edit: if you have access to a capillary electrophoresis system, these can work with substantially lower protein loads while retaining or surpassing sensitivity of traditional western blotting.
You might want to look at isoelectric focussing which has the advantage that large volumes of sample are loaded into the whole gel mixture but all proteins then move to their isoelectric point and are greatly concentrated at that point by the end of the run
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