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Updated: Apr 3, 2026

An Optimized Protocol for Electrophoretic Mobility Shift Assay Using Infrared Fluorescent Dye-labeled Oligonucleotides

An Optimized Protocol for Electrophoretic Mobility Shift Assay Using Infrared Fluorescent Dye-labeled Oligonucleotides

Published on: November 29, 2016

Electrophoretic Mobility Shift Assay Using Radiolabeled DNA Probes.

Dominic Poulin-Laprade¹, Vincent Burrus²

¹Département de Biologie, Faculté des Sciences, Université de Sherbrooke, Sherbrooke, QC, Canada, J1K 2R1.

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

|September 26, 2015

Summary

This summary is machine-generated.

Electrophoretic mobility shift assays (EMSA) detect biological molecule interactions. This method uses radiolabeled DNA probes and gel electrophoresis to visualize protein-DNA complexes, enabling diverse molecular binding studies.

Keywords:

DNA probe labeling EMSA Electrophoretic mobility shift assay Gel retardation Gel shift Native polyacrylamide gel Phosphorus-32 Protein–DNA interactions

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Screening for Functional Non-coding Genetic Variants Using Electrophoretic Mobility Shift Assay EMSA and DNA-affinity Precipitation Assay DAPA

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Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Electrophoretic mobility shift assays (EMSA) are established techniques for investigating molecular interactions.
Understanding protein-DNA interactions is crucial in molecular biology and genetics.

Purpose of the Study:

To present a protocol for performing Electrophoretic Mobility Shift Assays (EMSA).
To highlight the versatility and applications of EMSA in studying biological molecule interactions.

Main Methods:

Incubation of a purified protein with a 5'-end radiolabeled DNA probe.
Separation of protein-DNA complexes using polyacrylamide gel electrophoresis.
Detection of bound complexes via phosphorimaging.

Main Results:

Successful visualization of protein-DNA complexes.
Demonstration of EMSA's capability to analyze binding interactions.

Conclusions:

EMSA is a powerful tool for studying protein-DNA interactions.
The technique supports diverse applications including thermodynamic analysis, conformational studies, and binding stoichiometry determination.