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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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Updated: Jul 19, 2026

A Guided Materials Screening Approach for Developing Quantitative Sol-gel Derived Protein Microarrays

A Guided Materials Screening Approach for Developing Quantitative Sol-gel Derived Protein Microarrays

Published on: August 26, 2013

Protein array staining methods for undefined protein content, manufacturing quality control, and performance

Daniel S Schabacker¹, Ivana Stefanovska, Igor Gavin

¹Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439, USA. dschabacker@anl.gov

Analytical Biochemistry

|October 13, 2006

Summary

New methods assess protein microarray quality using on-chip staining. This quality control ensures reliable data for host-pathogen interaction studies, even without prior knowledge of cell composition.

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A Guided Materials Screening Approach for Developing Quantitative Sol-gel Derived Protein Microarrays

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V3 Stain-free Workflow for a Practical, Convenient, and Reliable Total Protein Loading Control in Western Blotting

V3 Stain-free Workflow for a Practical, Convenient, and Reliable Total Protein Loading Control in Western Blotting

Published on: December 30, 2013

Area of Science:

Proteomics
Biotechnology
Array Technology

Background:

Assessing protein microarray quality is crucial for reliable interaction assays.
Variability in slide-to-slide protein content complicates data interpretation.
Standardized methods are needed for quality control of protein arrays.

Purpose of the Study:

To develop on-chip staining methods for assessing protein microarray quality.
To quantify immobilized protein content and evaluate transfer efficiency.
To establish a basis for whole-proteome array development.

Main Methods:

Utilized two-dimensional liquid-phase fractionation (PF2D) for protein separation.
Developed total- and posttranslational modification-specific on-chip staining.
Employed Deep Purple protein stain and a portable microarray imager.
Used bovine serum albumin standard curves for quantification.

Main Results:

Achieved a linear dynamic range of at least 3 logs for protein stains.
Determined a lower limit of detection of 8 pg protein per gel element.
Successfully isolated and immobilized transmembrane proteins from Yersinia pestis.
Demonstrated quantification of total protein immobilized per gel element.

Conclusions:

Developed robust quality assurance/quality control methods for protein microarrays.
PF2D technology combined with gel element arrays enables whole-proteome analysis.
These methods support host-pathogen interaction studies independent of prior genomic or proteomic knowledge.