Question

What is the difference between SDS-PAGE gel and Native gel and what do you use to visualize migrated proteins?

Answer 1

Difference:

SDS PAGE	NATIVE PAGE
Type of polyacrylamide gel used is Denaturing gel	Type of polyacrylamide gel used is Non-Denaturing gel
The gel is made with addition of anionic detergent called Sodium Dodecyl sulfate (SDS)	SDS or no other detergent is added to the gel.
Separation in based mainly of molecular weight or mass of the molecules.	Separation is based mainly on charge / mass ratio, related to shape, size and charge of the molecules.
Wide pH range may be used.	Neutral pH is maintained
Net negative charges are imparted to the protein samples. The SDS binding is proportional to the relative molecular mass of the protein sample.	No charge is imparted to the protein sample by the gel, the charge of the sample itself determines its separation.
SDS denatures the protein samples into monomeric units.	The protein folding, and 3-dimensional structures of proteins are retained, protein recovered in original state
The proteins with lower molecular weight travels fasted in SDS page and are found closer to the anode compared to samples of higher molecular weight.	Mobility depends on charge, size and 3-D protein structure, like the charge of side chains of amino acids, et charge, folding, bonds.
Used for: Distinguishing and isolating protein from a sample mixture. Purification and protein assessment. As preliminary stage for Western-Blotting.	Used for: Separation of acidic proteins like in samples of recombinant erythropoietin, Bovine serum albumin (BSA). Separation and distinguishing proteins in their native forms. Observation of migrated proteins.

Native gels are used to visualize migrated proteins.