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Tagging and Fusion Proteins

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

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Related Experiment Video

Updated: Apr 9, 2026

One-step Purification of Twin-Strep-tagged Proteins and Their Complexes on Strep-Tactin Resin Cross-linked With Bissulfosuccinimidyl Suberate BS3

One-step Purification of Twin-Strep-tagged Proteins and Their Complexes on Strep-Tactin Resin Cross-linked With Bissulfosuccinimidyl Suberate BS3

Published on: April 20, 2014

Strep-Tagged Protein Purification.

Barbara Maertens¹, Anne Spriestersbach¹, Jan Kubicek¹

¹QIAGEN GmbH, Research and Development, Qiagenstrasse 1, 40724 Hilden, Germany.

Methods in Enzymology

|June 23, 2015

Summary

This summary is machine-generated.

This study provides updated protocols for purifying Strep-tagged proteins from various expression systems like E. coli and mammalian cells. It details methods for lysis, affinity purification using Strep-Tactin resins, and batch binding for efficient recombinant protein recovery.

Keywords:

Baculovirus-infected insect cells E. coli lysates Microscale purification Strep-Tactin magnetic beads Strep-tag system Strep-tagged protein purification Transfected mammalian cells

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Last Updated: Apr 9, 2026

One-step Purification of Twin-Strep-tagged Proteins and Their Complexes on Strep-Tactin Resin Cross-linked With Bissulfosuccinimidyl Suberate BS3

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High-throughput Purification of Affinity-tagged Recombinant Proteins

High-throughput Purification of Affinity-tagged Recombinant Proteins

Published on: August 26, 2012

Area of Science:

Biochemistry
Molecular Biology
Protein Chemistry

Background:

Recombinant protein purification is crucial for biological research and biotechnology.
The Strep-tag system offers a convenient method for protein purification.
Existing protocols require updates to accommodate new expression systems and techniques.

Purpose of the Study:

To provide updated and comprehensive protocols for Strep-tagged protein purification.
To detail methods applicable to diverse expression systems including E. coli, insect, and mammalian cells.
To offer guidance on selecting appropriate purification strategies based on protein abundance.

Main Methods:

Development and description of lysis protocols for different cell types.
Affinity purification using Strep-Tactin agarose-based matrices and magnetic beads.
Batch binding, washing, and elution techniques for gravity flow purification.

Main Results:

Validated protocols for Strep-tagged protein purification from E. coli, insect, and mammalian cells.
Demonstrated high binding capacity of Strep-Tactin resins (up to 9 mg/mL).
Outlined suitability of magnetic beads for low-abundance protein purification.

Conclusions:

The described protocols serve as an updated resource for Strep-tagged protein purification.
The methods are versatile and adaptable to various expression systems and protein quantities.
These updated protocols enhance the efficiency and accessibility of recombinant protein purification.