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Updated: May 3, 2026
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Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
Published on: January 16, 2012
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Overview of affinity tags for protein purification
Michelle E Kimple1, Allison L Brill1, Renee L Pasker1
1University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin.
Current Protocols in Protein Science
|February 11, 2014
Summary
Affinity tags help researchers identify specific proteins in complex biological samples. This review covers their history, common types, selection criteria, and emerging technologies for protein research.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Science
Background:
- Recombinant protein expression requires methods to distinguish target proteins from cellular backgrounds.
- Protein-protein interactions are crucial for cellular functions and require specific detection techniques.
Purpose of the Study:
- To provide a historical overview of affinity tag development.
- To review currently used affinity tags and selection strategies.
- To introduce novel affinity tag technologies.
Main Methods:
- Literature review of historical and current affinity tag applications.
- Analysis of commonly used affinity tags and their properties.
- Discussion of selection criteria for different experimental needs.
- Exploration of emerging affinity tag technologies.
Main Results:
- Affinity tags are essential for recombinant protein purification and interaction studies.
- Various tags (e.g., His-tag, GST-tag) are widely employed with established protocols.
- Newer technologies offer enhanced specificity and utility for future research.
Conclusions:
- Affinity tags significantly advance protein research by enabling specific detection and purification.
- Choosing the right tag is critical for experimental success.
- Emerging technologies promise further innovation in protein analysis.
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