hi everyone,

is there any method to eliminate the protein dimers from the recombinant protein sample. our is not a formulated sample we are still in trial stage the sample we get after solubilization refolding purification is analysed by SDS pAGE. it does not contain preservative or surfactant. We obtain some high molecular weight bands some of which we suspect to be dimers as they bind the specific antibody. is there any reagent that can be added to our sample to get rid / eliminate protein dimers.
kindly guide me on this

You can always add DTT or beta-mercaptoethanol to your sample to reduce dimerization before loading the sample onto a protein gel. Look in the protein chemistry forum for details. There are mulitple examples and concentrations discussed


Rb

exec said:

hi everyone, is there any method to eliminate the protein dimers from the recombinant protein sample. our is not a formulated sample we are still in trial stage the sample we get after solubilization refolding purification is analysed by SDS pAGE. it does not contain preservative or surfactant. We obtain some high molecular weight bands some of which we suspect to be dimers as they bind the specific antibody. is there any reagent that can be added to our sample to get rid / eliminate protein dimers. kindly guide me on this