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When a protein is complexed with the powerful cationic detergent sodium dodecyl sulfate (SDS) and separated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, its migration distance can be used to calculate its apparent molecular weight (MW) standard curve.
When a protein is complexed with the powerful cationic detergent sodium dodecyl sulfate (SDS) and separated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, its migration distance can be used to calculate its apparent molecular weight (MW) (SDS-PAGE). Due to its simplicity, this approach, which was developed in 1969, is still widely used today. Even though it has been noted that many proteins exhibit some variation in MW when measured on SDS-PAGE, particularly when their peptide chains are posttranslationally modified, this adaptable technique is still utilized frequently in modern biochemical works today. In this protocol, a straightforward technique to calculate MW by running SDS-PAGE of benchmark proteins is described by an example where proteins extracted from mouse retina were
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