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Related Concept Videos

SDS-PAGE01:27

SDS-PAGE

Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed  polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
Two-dimensional Gel Electrophoresis01:22

Two-dimensional Gel Electrophoresis

Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as  cells...
DNA Agarose Gel Electrophoresis02:35

DNA Agarose Gel Electrophoresis

Agarose gel electrophoresis is a laboratory technique commonly used to separate DNA fragments by size. However, it can also be used to isolate and purify DNA fragments using a gel extraction protocol.
Gel extraction follows five major steps: running gel electrophoresis to separate fragments, isolating the individual bands, extracting DNA from those bands, and removing the dye and salts from the extracted mixture to obtain pure DNA.
In cloning experiments, both the insert and vector DNA...

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Related Experiment Video

Updated: May 22, 2026

Preparation of DNA-crosslinked Polyacrylamide Hydrogels
09:06

Preparation of DNA-crosslinked Polyacrylamide Hydrogels

Published on: August 27, 2014

Native polyacrylamide gels.

Claudia Arndt1, Stefanie Koristka, Holger Bartsch

  • 1Carl Gustav Carus University TU Dresden, Dresden, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|May 16, 2012
PubMed
Summary
This summary is machine-generated.

This study introduces a starting protocol for native polyacrylamide gel electrophoresis (PAGE). Native PAGE separates proteins based on charge and size, unlike standard methods using sodium dodecyl sulfate (SDS).

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Last Updated: May 22, 2026

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Published on: February 24, 2011

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Proteins are typically separated using polyacrylamide gel electrophoresis (PAGE) with denaturing agents like sodium dodecyl sulfate (SDS).
  • SDS masks native protein charges, enabling separation primarily by molecular weight.
  • Alternative electrophoresis methods are needed to preserve protein structure and native charge characteristics.

Purpose of the Study:

  • To describe a foundational protocol for performing native polyacrylamide gel electrophoresis (PAGE).
  • To enable protein separation based on intrinsic charge and size, without denaturing agents.

Main Methods:

  • Development of a starting protocol for native PAGE.
  • Electrophoresis of proteins under non-denaturing conditions, omitting detergents like SDS.
  • Analysis of protein mobility influenced by native charge (isoelectric point) and pH.

Main Results:

  • A protocol for native PAGE has been established.
  • Demonstration that protein mobility in native PAGE is primarily governed by intrinsic charge and molecular size.
  • Successful separation of proteins without the use of denaturing detergents.

Conclusions:

  • Native PAGE offers an alternative to SDS-PAGE for protein separation.
  • This method preserves protein native state, allowing analysis of charge-dependent migration.
  • The described protocol serves as a basis for further optimization of native PAGE techniques.