Well, If it is an SDS-PAGE gel, then the act of boiling the protein in detergent generally denatures the protein and breaks apart non-covalent interactions.
To assess dimerisation, a non-denaturing technique might be more helpful. Native-PAGE, Size Exlusion Chromatography, Analytical Ultracentrifugation... SEC with a suitable column for your predicted protein size would probably be a first thing to try. If you have SEC with in-line MALLS, even better. HTH, Dave [image: David Briggs on about.me] David Briggs about.me/david_briggs <http://about.me/david_briggs> On 20 October 2014 12:00, arun kumar <arungreenlo...@gmail.com> wrote: > Hello everyone, > > I would like to take a advice from you all. I have protein like 200 KDa > when i lode in a gel it shows band on 200KDa, Is that this protein gets > dimer or anything else is happening. > I would appreciate for some open discussion. > > -- > > * Regards,** Arun * >
