How SDS Page and Native Page are Used in Protein Studies (2025)

This research project will explore the principles and applications of SDS PAGE (Sodium Dodecyl Sulfate Poly Acrylamide Gel Electrophoresis) and NATIVE page (Polyacrylamide Gel Electrophoresis under non-denaturing conditions). SDS and Native Page are two important lab techniques for protein analysis. SDS- PAGE denatures proteins by surrounding them with uniform negative charges thereby enabling separation solely based on differences in molecular weights. In contrast, Native PAGE maintains proteins in their natural folded state, enabling separation based on a variety of combinations of sizes, shapes, and charges. Detection in SDS PAGE thus reveals individuals’ subunits of protein complexes, while Native PAGE provides information about proteins without overall breaking down to its individual subunits. This study highlights differences in sample preparation, gel composition, electrophoresis behavior and detection outcomes. It offers important insights into the purity of proteins, their identification, and interactions with other proteins, and shows how each method can be used to address specific biological questions and prepare protein complexes, such as NOA4-ferritin for structural studies.