SDS-PAGE (sodium dodecyl sulfate–polyacrylamide gel electrophoresis) is a discontinuous electrophoretic system developed by Ulrich K. Laemmli which is commonly used as a method to separate proteins with molecular masses between 5 and 250 kDa.[1][2] The combined use of sodium dodecyl sulfate (SDS, also known as sodium lauryl sulfate) and polyacrylamide gel eliminates the influence of structure and charge, and proteins are separated by differences in their size. At least up to 2012, the publication describing it was the most frequently cited paper by a single author, and the second most cited overall.[3]
- ^ Laemmli, U. K. (1970). "Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4". Nature. 227 (5259): 680–685. Bibcode:1970Natur.227..680L. doi:10.1038/227680a0. ISSN 0028-0836. PMID 5432063. S2CID 3105149.
- ^ "Interview with Ulrich Lämmli". Neue Zürcher Zeitung (in German). No. 11. 2005. Retrieved March 4, 2012.
- ^ Neue Züricher Zeitung: Interview with Ulrich Lämmli (in German). NZZ Folio, No. 11, 2005. Accessed March 4, 2012.