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Updated: Mar 12, 2026

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Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
Published on: January 16, 2012
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MAP Tag: A Novel Tagging System for Protein Purification and Detection
Yuki Fujii1, Mika K Kaneko1, Yukinari Kato1
1Department of Regional Innovation, Tohoku University Graduate School of Medicine , Miyagi, Japan .
Monoclonal Antibodies in Immunodiagnosis and Immunotherapy
|November 2, 2016
Summary
A new MAP tag system, using a specific antibody and tag, enables high-quality protein purification. This novel system is also effective for protein detection methods like western blotting and flow cytometry.
Area of Science:
- Biochemistry
- Molecular Biology
- Biophysics
Background:
- Protein purification is crucial in life sciences but faces challenges with existing tag systems.
- Affinity tags offer high specificity but have limitations requiring new solutions.
Purpose of the Study:
- To develop a novel affinity tag system for efficient protein purification and detection.
- To address limitations of current affinity tag systems in protein research.
Main Methods:
- Development of the MAP tag system using a rat anti-mouse podoplanin monoclonal antibody (PMab-1) and a specific MAP tag.
- Demonstration of high affinity and specificity of PMab-1 for the MAP tag.
- Validation of the MAP tag system's utility through purification of nuclear, soluble, and membrane proteins.
Main Results:
- The MAP tag system demonstrated high affinity and specificity for target proteins.
- Successful purification of diverse protein types (nuclear, soluble, membrane) was achieved.
- The system proved effective for protein detection via western blot and flow cytometry.
Conclusions:
- The MAP tag system offers a powerful new tool for high-purity protein purification.
- This system enhances protein detection capabilities in various biological analyses.
- The MAP tag system provides a versatile solution for protein research needs.

