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Targeted purification of SnAvi-tagged proteins
Ursula Schäffer1, Ralf Baumeister, Ekkehard Schulze
1Institute for Biology 3, University of Freiburg, Schänzlestr. 4, 79104, Freiburg, Germany, ursula_schaeffer@hotmail.com.
Methods in Molecular Biology (Clifton, N.J.)
|June 20, 2014
Summary
We introduce the SnAvi-tag, a versatile Tandem Affinity Purification (TAP) tag. This modular tag enhances protein complex identification by reducing contaminants and enabling in vivo visualization and cell-specific activation studies.
Area of Science:
- Molecular Biology
- Biochemistry
- Proteomics
Background:
- Tandem affinity purification (TAP) is crucial for identifying protein complex members.
- TAP-tags enable sequential enrichment steps, minimizing contaminants.
- A need exists for versatile TAP tags applicable across different expression systems.
Purpose of the Study:
- To describe the application and utility of the SnAvi-tag, a novel TAP tag.
- To highlight the SnAvi-tag's modular composition and multifunctional capabilities.
- To demonstrate its use in various expression systems for protein complex analysis.
Main Methods:
- Application of the SnAvi-tag in different expression systems.
- Utilizing the modular composition for sequential protein enrichment.
- Employing the tag for in vivo visualization of tagged proteins.
Main Results:
- The SnAvi-tag effectively reduces contaminants during protein complex purification.
- The tag facilitates in vivo visualization of tagged proteins.
- Demonstrated cell type-specific activation of tagged proteins is possible.
Conclusions:
- The SnAvi-tag is a powerful and multifunctional tool for protein complex identification.
- Its modular design offers advantages in reducing contaminants and enabling advanced applications.
- The SnAvi-tag is suitable for diverse research settings, including visualization and activation studies.

