I have a sample suspended in 0.34 M NaCl after using ion exchange chromatography. I would like to perform hydrophobic interaction chromatography (HIC). Is it okay that I use greater salt concentration for my equilibration buffer than the salt concentration of my sample (to which it may precipitate)?

Before the run, I've performed a "stability window" test by adding the sample to varying concentrations of ammonium sulfate. I've found out that 0.46 M ammonium sulfate is the maximum amount I can add to it (before it precipitates). With this, I've performed an HIC run using 0.8 M ammonium sulfate (based on the total salt content = 0.46 M NH42SO4 + 0.34 M NaCl). Based on my SDS-PAGE gel, it seemed I wasn't able to purify the protein. I would like to run next the sample in 1 M NH42SO4, would that be fine even if the sample would possibly precipitate in the column?

Thanks.