2D Gel Electrophoresis| Principle & Limitations | 2 Dimensional Gel Electrophoresis | 2DGE | PENS#89

2D Gel Electrophoresis| Principle & Limitations | 2 Dimensional Gel Electrophoresis | 2DGE | PENS#89
#2dgel #2DGE #proteomics

The primary technique for proteomics research is two-dimensional gel electrophoresis, or 2D-PAGE. It uses two different features of proteins to distinguish the complicated mixture of samples. Proteins are distinguished in the first dimension by their pI value, and in the second dimension by their relative molecular weight. Although it was first reported by O'Farrell in 1975, the introduction of immobilised pH gradient strips improved its application and adoption since they provided consistent findings and were easy to handle. Proteins were first visualised using 32P or 35S labelling. SYBRO Ruby, a more delicate approach, has now taken its place. Advances were made in various stages of the 2D-PAGE technology, which can separate up to 10,000 proteins in a single run.

The Lectures are given Dr. Nagendra Singh aiming to spread basic understanding and awareness of biological molecules and reactions. Dr. Nagendra Singh finished his Doctoral and Post Doctoral studies from "All India Institute of Medical Sciences" (AIIMS) New Delhi. Dr. Singh has a vast experience of research and Teaching in the fields of Structure & Molecular Biology and Biochemistry, which also include Biomolecules, Proteomics, Protein Engineering and Drug Design.

[IBTSaiyadaIqraKamil]

Thank you sir. You made it crystal clear.💫

[AditiSarkar-yh]

Thank you so much for this insightful and detailed video on 2DGE. May I ask you two questions? 1. What is the chemistry behind the formation of the pH gradient in the IPG strips? 2. As SDS completely disrupt the polymeric configuration of a protein, doesn't it affect further downstream analysis like MS methods? It will be helpful if you please answer this.