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Related Experiment Video

Updated: Jul 1, 2026

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag

Published on: January 16, 2012

Novel affinity tag system using structurally defined antibody-tag interaction: application to single-step protein

Terukazu Nogi¹, Takeshi Sangawa, Sanae Tabata

¹Laboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.

Protein Science : a Publication of the Protein Society

|September 13, 2008

Summary

Researchers developed a new peptide tag for protein purification. This cost-effective system uses a specific antibody and organic solvents for non-denaturing elution, simplifying the production of important human proteins.

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Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method

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Published on: July 27, 2016

Area of Science:

Biochemistry
Molecular Biology
Protein Engineering

Background:

Mammalian cell expression is crucial for studying biologically important human proteins.
Protein production and purification present significant technical and economic challenges.

Purpose of the Study:

To introduce a novel, cost-effective affinity peptide tagging system for protein purification.
To address the challenges in producing and purifying mammalian-expressed proteins.

Main Methods:

Engineered an 18-residue affinity tag by concatenating a short recognition sequence.
Utilized a low-affinity anti-peptide monoclonal antibody for binding.
Developed a non-denaturing elution method using water-miscible organic solvents.

Main Results:

Achieved ideal solution binding kinetics for the engineered affinity tag.
Demonstrated a low-cost purification method for mammalian-expressed proteins.
Established a structural basis for the antibody-peptide interaction.

Conclusions:

The novel peptide tagging system offers an efficient and economical solution for protein purification.
The system facilitates the structural studies of biologically important human proteins.
Further improvements and modifications of the antibody-peptide interaction are possible.