What is the Difference Between SDS Page and Native Page?

The main difference between SDS-PAGE and Native PAGE lies in the type of gel used and the factors that determine protein migration. Here are the key differences:

• Gel Type: SDS-PAGE uses a denaturing gel, while Native PAGE uses a non-denaturing gel.
• Migration Factors: In Native PAGE, protein migration depends on both the mass and structure, whereas in SDS-PAGE, migration is determined only by the protein's mass.
• Denaturation: Protein samples are prepared in a non-denaturing and non-reducing buffer in Native PAGE, while SDS-PAGE involves adding an excessive amount of SDS to coat proteins in a negative charge, covering all the intrinsic charges.
• Protein Stability and Recovery: In SDS-PAGE, proteins are not stable, and recovery is not possible as they are denatured. In contrast, proteins are stable in Native PAGE, and recovery is possible.

In summary, SDS-PAGE separates proteins based on their mass, using a denaturing gel, while Native PAGE separates proteins based on their size, charge, and shape, using a non-denaturing gel.

Comparative Table: SDS Page vs Native Page

Here is a table comparing the differences between SDS-PAGE and Native PAGE:

In summary, SDS-PAGE is a technique used to separate proteins based on their mass, using a denaturing gel and sodium dodecyl sulfate to impart a negative charge on protein samples. In contrast, Native PAGE is a technique that uses non-denatured gels to separate proteins based on their size, charge, and sometimes shape. Proteins remain stable in Native PAGE and can be recovered after separation.