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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 1, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)

Published on: August 31, 2018

A robust and sensitive method for detecting subtle structural differences in bovine serum albumin.

Teruo Akuta¹, Tomomi Sato¹, Masataka Nakagawa¹

¹Research and Development Division, Kyokuto Pharmaceutical Industrial Co., Ltd, Takahagi, Japan.

|March 3, 2026

Summary

Fatty acid content causes bovine serum albumin (BSA) lot variability. Subtle structural differences in BSA were detected using circular dichroism and fluorescence spectroscopy, especially under heat stress, improving protein quality assessment.

Keywords:

Agarose native gel electrophoresis Bovine serum albumin (BSA)Intrinsic fluorescence Tryptophan microenvironment circular dichroism (CD) spectroscopy fatty acid binding lot-to-lot variability

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Last Updated: Jul 1, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)

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Published on: August 31, 2018

Proteome-wide Quantification of Labeling Homogeneity at the Single Molecule Level

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Published on: April 19, 2019

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering (SEC-MALS)

Published on: June 20, 2019

Area of Science:

Biochemistry
Protein Chemistry

Background:

Bovine serum albumin (BSA) exhibits lot-to-lot variability.
Fatty acid content is a contributing factor to this variability.
Assessing structural consistency across BSA lots is crucial for reliable experimental outcomes.

Purpose of the Study:

To compare the structural properties of two BSA lots with differing fatty acid content.
To identify sensitive methods for detecting subtle conformational differences in BSA.
To establish a practical approach for evaluating BSA lot consistency.

Main Methods:

Comparative analysis of fatty acid-bound and fatty acid-free BSA lots.
Utilized conventional techniques: UV absorbance spectroscopy, SDS-PAGE, gel filtration chromatography, and agarose native gel electrophoresis.
Employed advanced methods: Circular dichroism (CD) spectroscopy and intrinsic fluorescence measurements, particularly under heat stress conditions (73-76°C).

Main Results:

Conventional methods showed no significant structural differences between BSA lots.
CD spectroscopy and fluorescence measurements revealed subtle but significant conformational variations, especially around tryptophan residues.
Distinct behaviors under heat stress, including different aggregation propensities, were observed between the two BSA lots.

Conclusions:

Subtle conformational differences in BSA lots, influenced by fatty acid content, can be detected using CD and fluorescence spectroscopy.
Combining these spectroscopic techniques with native electrophoresis under heat stress offers a sensitive method for assessing BSA quality and consistency.
This approach provides a valuable tool for ensuring reliable protein preparations in research and diagnostics.