Speeding up SDS–PAGE: Theory and experiment

In order to accelerate Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE), here we propose an optimized version of the technique enabled by experimental tuning reinforced by theoretical description. In the resulting system, the gel buffer was diluted twofold and supplemented with g...

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Bibliographic Details
Published in:	Electrophoresis Vol. 44; no. 15-16; pp. 1155 - 1164
Main Authors:	Koshkina, Maria K., Shelomov, Mikhail D., Pometun, Anastasia A., Savin, Svyatoslav S., Tishkov, Vladimir I., Atroshenko, Denis L.
Format:	Journal Article
Language:	English
Published:	Germany Wiley Subscription Services, Inc 01-08-2023
Subjects:	Electrophoresis Glycine Laemmli electrophoresis Polyacrylamide protein electrophoresis acceleration SDS–PAGE Sodium dodecyl sulfate Laemmli electrophoresis SDS-PAGE protein electrophoresis acceleration
Online Access:	Get full text
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Summary:	In order to accelerate Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE), here we propose an optimized version of the technique enabled by experimental tuning reinforced by theoretical description. In the resulting system, the gel buffer was diluted twofold and supplemented with glycine at a low concentration, whereas a higher voltage was applied. This approach reduced runtime from 90 to 18 min. It is important to emphasize that, despite the high voltage applied to the gel, the resolution of the bands did not decrease compared to the original Laemmli method. The proposed acceleration approach can be used in other variants of SDS–PAGE.
Bibliography:	See the article online to view Figures 1, 2, 4 and 5 in color. Maria K. Koshkina and Denis L. Atroshenko contributed equally to this manuscript. Color online ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0173-0835 1522-2683
DOI:	10.1002/elps.202300011