i am currently at a stage where i have purified my protein via ion exchange and gradient elution. so when i did SDS-PAGE, i found out there were few bands on the elution lane and the bands gradually faded. so the questions are:
1. if there were few bands observed, how do i determine which of the band(s) is my protein of interest?
2. i want to do native SDS-PAGE and localize the proteins straight away on the gel, but how do i concentrate the proteins without having to denature them?
3. is using PEG6000 better than acetone?
4. say if i sucessfully detect my protein band of interest, would silver staining the gel denature my native proteins? (coomasive staining doesn't work for me btw)