Is it to denature the proteins? I know that DTT reduces disulfide bonds. Please explain to me why this step is so essential.
If disulfide bonds are not reduced, the residual structure of the protein may cause it to run at an incorrect molecular weight.
DTT is a redox reagent that reduces disulfides to their corresponding thiols.
To answer this question, you should also understand the differene between native and SDS-PAGE.
https://www.researchgate.net/post/Can_anyone_detail_the_differences_between_Native_PAGE_and_SDS-PAGE
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