There is a great need for a robust method that combines the electrophoretic resolution of proteins with retention of their functional behavior.
In traditional SDS-PAGE the proteins are well separated but are denatured such that the structure and function are no longer adequately maintained for carrying out further functional assays.
A new method of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) in which proteins can be well separated during electrophoresis as well as maintain their native 3-dimensional conformations and functional activity. This native SDS-PAGE method will allow for important new experiments to be conducted in the proteomic field and a better understanding of proteins such as isolation from the gel of native proteins for further analysis, direct in-gel assay of enzymatic activity, direct in-gel survey of binding activity of proteins with small molecules (e.g. drugs, toxic agents) and macromolecules (e.g. protein binding partners including antibodies, cognate DNA binding sites), and isolation of protein for subsequent mass spectral identification.
Our easy to implement Native SDS-PAGE method has retained the enzymatic activity of a number of enzymes tested and has also maintained protein complexes in a bound state.
Issued U.S. Patent, Native protein electrophoresis and methods of use, US9709526B2