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SDS-PAGE

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...

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Related Experiment Video

Updated: May 22, 2026

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Tricine-SDS-PAGE.

Syed R Haider¹, Helen J Reid, Barry L Sharp

¹Loughborough University, Loughborough, UK.

Methods in Molecular Biology (Clifton, N.J.)

|May 16, 2012

Summary

This summary is machine-generated.

We simplified Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for separating small proteins. This improved method allows for easier protein recovery from gels for quantitative analysis using advanced detectors.

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Area of Science:

Biochemistry
Proteomics
Analytical Chemistry

Background:

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) is a standard technique for separating low-molecular-mass proteins.
The conventional tricine-SDS-PAGE system can be complex and hinder the recovery of separated proteins for subsequent quantitative analysis.

Purpose of the Study:

To develop a simplified tricine-SDS-PAGE system for efficient separation of low-molecular-mass proteins.
To enhance the compatibility of the separation method with downstream quantitative detection techniques.

Main Methods:

A simplified tricine-SDS-PAGE protocol was developed.
Low-percentage polyacrylamide gels were utilized for improved protein resolution.
The system was optimized for compatibility with UV and inductively coupled plasma mass spectrometry (ICP-MS).

Main Results:

The simplified system effectively separates low-molecular-mass proteins.
The modified gels demonstrate high compatibility with UV and ICP-MS detection.
Protein recovery from the gels for quantitative analysis is facilitated.

Conclusions:

The developed simplified tricine-SDS-PAGE offers an efficient and accessible method for analyzing small proteins.
This technique improves the utility of gel electrophoresis for quantitative proteomics and biochemical studies.
The enhanced compatibility with modern detectors broadens the application of this method in various analytical workflows.