Protein elution question - (Feb/14/2006 )

I preformed an anti-Flag immunoprecipitate today and eluted in sample buffer containing SDS and mercaptoethanol by heating to what I believed to be 95 degrees celsius for 5 min. I didnt realize until after I started running my gel (SDS polyacrylamide) that the temperature of the heating block had been turned down to 80 degrees. I was just wondering what sort of effect this will have on my experiment, should enough of my protein still have been eluted from my beads to detect it via western blot?

normally yes, but only a western will give the true answer