So, I see a band that is twice the size of my protein. I confirmed that this band contains my protein and since it is twice the size I believe it is a dimer. However, it doesn't make sence that a dimer will form in a denaturing SDS-PAGE?
Is it possible to see a dimer/oligomer in denaturing SDS-PAGE?
1 reply to this topic
Posted 29 March 2011 - 10:02 PM
Hola again I have answered your other question in mol. clonning forum. So to see multimers cys mediated there is a method with a loading buffer withouth reducer and withouth boil samples. SDS covers your multimers and they run as a band of double or cuadruple etc mol. weigh. For that I said to add 1ul of mercapto ethanol to your sample before boil. Tell us if it runs or not to ask more information to solve your problem. Buena suerte