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Related Experiment Video

Updated: Mar 15, 2026

Analysis of Mitochondrial Respiratory Chain Complexes in Cultured Human Cells using Blue Native Polyacrylamide Gel Electrophoresis and Immunoblotting

Analysis of Mitochondrial Respiratory Chain Complexes in Cultured Human Cells using Blue Native Polyacrylamide Gel Electrophoresis and Immunoblotting

Published on: February 12, 2019

Protein electrophoretic migration data from custom and commercial gradient gels.

Andrew J Miller¹, Brandon Roman¹, Eric M Norstrom¹

¹Department of Biological Sciences, DePaul University, 2325 N. Clifton Ave, Chicago, IL 60614, USA.

|September 14, 2016

Summary

This study compares protein migration rates in hand-poured versus commercial acrylamide gradient gels. Results offer insights into electrophoretic mobility variations for different protein masses and gel types.

Keywords:

Electrophoresis Gradient Molecular weight Polyacrylamide Protein biochemistry

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Last Updated: Mar 15, 2026

Analysis of Mitochondrial Respiratory Chain Complexes in Cultured Human Cells using Blue Native Polyacrylamide Gel Electrophoresis and Immunoblotting

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Published on: February 12, 2019

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Fast and Sensitive Colloidal Coomassie G-250 Staining for Proteins in Polyacrylamide Gels

Fast and Sensitive Colloidal Coomassie G-250 Staining for Proteins in Polyacrylamide Gels

Published on: August 3, 2009

Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Gradient gel electrophoresis is a powerful technique for protein separation.
Customizable gradient gels offer potential advantages in resolution and flexibility.
Understanding protein migration behavior is crucial for accurate analysis.

Purpose of the Study:

To present data on the electrophoretic migration rates of proteins in acrylamide gradient gels.
To compare migration patterns between hand-poured and commercially acquired gels.
To analyze the influence of polypeptide mass on migration speed.

Main Methods:

Electrophoretic migration of nine polypeptides of varying molecular masses was measured.
Proteins were analyzed in both hand-poured and commercially prepared acrylamide gradient gels.
Migration distances were recorded within individual lanes and across multiple gels.

Main Results:

Data quantifies the rate of electrophoretic migration for specific polypeptides.
Variations in migration rates were observed between hand-poured and commercial gels.
Analysis revealed differences in migration patterns within single and multiple gel experiments.

Conclusions:

The presented data provides a valuable resource for researchers using gradient gel electrophoresis.
Findings contribute to the understanding of protein separation dynamics in customizable gel systems.
This work supports the optimization of gel electrophoresis protocols for protein analysis.