What is Native PAGE?
Native PAGE electrophoresis is another polyacrylamide gel electrophoresis technique, used in molecular biology to study the composition, native structure and function of the proteins. This technique separates the protein molecules based on the size and overall charge of the protein. It was developed by Ornstein and Davis. Since SDS is not used as a denaturing agent in the gel, the protein molecules retain their folded state and functionality. The buffers used in SDS PAGE do not contain any denaturing and reducing agents.
There are mainly two types of native PAGE:
- Blue Native PAGE (BN-PAGE): Here Coomassie brilliant blue dye is used during protein separation.
- Clear Native PAGE (CN-PAGE): Here proteins are separated based on their complex charge in a gradient gel without using any dye.
Differences between SDS PAGE and Native PAGE
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.
Table of Content
- Differences Between SDS PAGE and Native PAGE
- What is SDS PAGE?
- What is Native PAGE?
- Similarities between SDS PAGE and Native PAGE
- Conclusion – Differences Between SDS PAGE and Native PAGE
- FAQs on SDS PAGE and Native PAGE