Protein Purification techniques (SDS and Native PAGE)

Protein purification is a critical step in biochemistry and molecular biology, enabling the isolation and characterization of specific proteins for various applications. Two widely used techniques for protein analysis are SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) and Native PAGE.

SDS-PAGE separates proteins based on their molecular weight, utilizing SDS to denature proteins and impart a uniform negative charge, allowing for effective migration through a polyacrylamide gel under an electric field. This technique is particularly useful for analyzing the purity and size of proteins.

In contrast, Native PAGE maintains the proteins' native conformation and interactions, enabling the separation of proteins based on size, shape, and charge while preserving their biological activity. This method is beneficial for studying protein complexes and functional properties.

Together, these techniques provide complementary insights into protein structure and function, facilitating advancements in research and therapeutic development.