I hope i chose the right sub for this question.
I have been doing the same protein purification for the past few months, only with the murine for of the protein.
After eluting the protein from my Ni-NTA column (whole process at 4C in the cold room) using a Tris-HCl (pH 8) and imidazole-based buffer in 10ml fractions, i put the fractions on ice and left them in the cold room for the past two days.
Today i wanted to continue and see that the fractions where i predicted the protein to be had big pellets.
Is this reversible? How? I need to dialyse the stuff for the next two days.
What i did right now was dilute the fractions (added 5ml of elution buffer) and left them to shake at room temperature.
Blindspot
Member Since 14 Jan 2013Offline Last Active Jan 15 2013 08:32 AM





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