SDS PAGE and Native PAGE

Why is SDS not used in Native PAGE?

Native PAGE is employed to examine the composition and native structure of proteins. Therefore, SDS is not used due to its disruptive effect on the 3D structure of the proteins.

What are the Different Types of Native PAGE?

There are 3 types of native PAGE: Blue native PAGE (BN PAGE), Clear native PAGE (CN PAGE) and Preparative native continuous PAGE (PNC PAGE).

Why is APS and TEMED used in PAGE?

In the preparation of a polyacrylamide gel, Ammonium Persulfate (APS) and Tetramethylenediamine (TEMED) both are used for polymerization of acrylamide and bisacrylamide monomers.

What does Native Mean in Gel Electrophoresis?

In gel electrophoresis, “native” means that inside the polyacrylamide gel, the proteins are allowed to retain their three-dimensional shape or native conformation.

What do you Mean by Denaturing Gel?

A denaturing gel is a type of gel used in electrophoresis where the proteins lose their native, three-dimensional structure due to the presence of denaturing agents such SDS.

What is the Difference Between Native PAGE and Denaturing PAGE?

Native PAGE separates proteins based on their native structure, while denaturing PAGE separates proteins based on their molecular weight after denaturation.

What is the Difference Between Western and SDS-PAGE?

Western blotting is a technique used to detect specific proteins in a sample, while SDS-PAGE separates proteins based on their molecular weight.

What is the Difference Between SDS-PAGE and Electrophoresis?

SDS-PAGE is a type of electrophoresis technique specifically designed to separate proteins based on their molecular weight using SDS detergent, whereas electrophoresis is a broader term comprising of various techniques to separate molecules based on their charge and size using an electric field.

What is the Purpose of SDS in SDS-PAGE?

SDS in SDS-PAGE serves to denature proteins, bind to them, and confer a negative charge proportional to the protein’s mass, enabling separation based on size during electrophoresis.

Why is Beta Mercaptoethanol used in SDS-PAGE?

Beta-mercaptoethanol is used in SDS-PAGE to reduce disulfide bonds in proteins, thereby denaturing them and allowing for more accurate separation based on molecular weight during electrophoresis.

Why is Glycerol used in SDS-PAGE?

Glycerol in SDS-PAGE increases sample density, helping loading into gel wells for accurate protein separation by molecular weight.

The difference between SDS-PAGE and native PAGE lies in how proteins are separated in the polyacrylamide gel. In SDS-PAGE, the migration rate of the protein is determined by its molecular weight only, whereas in native PAGE, the migration rate depends on both the size and overall charge of the protein. In this article, we will study the process of SDS PAGE and Native PAGE as well as the similarities and differences between SDS-PAGE and native PAGE.