What Are the Differences Between SDS and Non-SDS Systems in Protein Gel Electrophoresis?
When performing protein gel electrophoresis, the inclusion or exclusion of SDS (sodium dodecyl sulfate) leads to distinct differences in the following aspects:
Sample Preparation
1. With SDS
Adding SDS during sample preparation imparts a uniform negative charge to protein molecules and linearizes them by disrupting their secondary and tertiary structures.
2. Without SDS
Omitting SDS means proteins retain their native charges and conformations during sample preparation.
Gel Preparation
1. With SDS
Polyacrylamide gels are prepared with SDS, which binds to proteins, conferring a negative charge and facilitating their migration toward the anode under an electric field.
2. Without SDS
Gels are prepared without SDS, so protein migration is influenced by their intrinsic charges and structures.
Electrophoresis Process
1. With SDS
In SDS-containing systems, proteins acquire a negative charge and migrate toward the anode. The consistent SDS-to-protein binding ratio ensures that migration speed inversely correlates with molecular weight. This method is known as SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis).
2. Without SDS
In the absence of SDS, protein migration depends on their native charges and structures. This approach, called native gel electrophoresis, is typically used to study proteins' natural conformations and charge properties.
The presence or absence of SDS in electrophoresis systems significantly affects sample preparation, gel composition, and the electrophoresis process. SDS systems standardize protein charge and shape, enabling separation based on molecular weight, while non-SDS systems preserve native protein characteristics, making them suitable for studying natural structures and charge properties.
MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.
Related Services
How to order?
