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Western Blotting

Western Blotting

Western blotting is an analytical technique for protein identification. It has various applications in immunology and medicine, including detecting diseases like bovine spongiform encephalopathy, mad cow disease, and human and feline immunodeficiency virus from biological samples.
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.

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Related Experiment Video

Updated: Jul 2, 2026

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Assays for total protein.

Rex Lovrien¹, Daumantas Matulis

¹University of Minnesota, St. Paul, Minnesota, USA.

Current Protocols in Microbiology

|September 5, 2008

Summary

This summary is machine-generated.

This study details protein quantification methods, including copper-based assays like Biuret, Hartree-Lowry, and bicinchoninic acid (BCA), alongside amino acid, UV spectrophotometry, Bradford, and dry weight measurements for accurate protein analysis.

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High Throughput, Absolute Determination of the Content of a Selected Protein at Tissue Levels Using Quantitative Dot Blot Analysis (QDB)

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Published on: August 21, 2018

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Last Updated: Jul 2, 2026

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

High Throughput, Absolute Determination of the Content of a Selected Protein at Tissue Levels Using Quantitative Dot Blot Analysis (QDB)

High Throughput, Absolute Determination of the Content of a Selected Protein at Tissue Levels Using Quantitative Dot Blot Analysis (QDB)

Published on: August 21, 2018

Area of Science:

Biochemistry
Analytical Chemistry

Background:

Accurate protein quantitation is crucial for various biological and chemical analyses.
Multiple methods exist, each with advantages and limitations regarding sensitivity, specificity, and applicability.

Purpose of the Study:

To describe and compare several protein quantification assays.
To provide protocols for sample preparation and contaminant removal.

Main Methods:

Copper-based assays: Biuret, Hartree-Lowry (Lowry variation), Bicinchoninic Acid (BCA).
Amino acid quantitation via acid hydrolysis and ninhydrin detection.
Ultraviolet (UV) spectrophotometry for total protein and contaminant detection.
Coomassie dye-binding (Bradford) assay.
Dry weight measurement for pure protein.
Support protocols: heat sealing for hydrolysis, dialysis in polyacrylamide gel wells, and Trichloroacetic acid (TCA) precipitation.

Main Results:

The Biuret, Hartree-Lowry, and BCA assays are presented for total protein measurement.
Amino acid content can be quantified using acid hydrolysis and ninhydrin.
UV spectrophotometry aids in assessing protein concentration and identifying contaminants.
The Bradford assay offers simplicity and sensitivity but can yield variable results.
Dry weight measurement is suitable for pure protein samples.
Dialysis and TCA precipitation are effective for removing low-molecular-weight contaminants.

Conclusions:

A comprehensive overview of diverse protein quantification techniques is provided.
The selection of an appropriate method depends on the specific experimental requirements and sample characteristics.
Effective sample preparation techniques are essential for reliable protein quantitation.