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Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes
Published on: December 20, 2019
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Expression and isolation of recombinant tau
Rebecca L Best1, Peter J Chung2, Sarah J Benbow1
1Neuroscience Research Institute, University of California, Santa Barbara, Santa Barbara, CA, United States; University of California, Santa Barbara, Santa Barbara, CA, United States.
Methods in Cell Biology
|September 9, 2017
Summary
This chapter details methods for purifying tau protein, both untagged and polyhistidine-tagged, using bacterial expression and chromatography. These techniques provide pure tau protein for studying its mechanisms of action.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Chemistry
Background:
- Tau protein is crucial in neuronal function and implicated in neurodegenerative diseases.
- Purified tau protein is essential for biochemical and biophysical studies.
- Existing purification methods may have limitations in yield or purity.
Purpose of the Study:
- To describe robust methods for the purification of tau protein.
- To provide protocols for both untagged and polyhistidine-tagged tau protein.
- To enable further research into the mechanisms of tau action.
Main Methods:
- Utilizing a bacterial expression system for tau protein production.
- Employing heat treatment to denature and precipitate contaminating proteins.
- Implementing column chromatography for the separation and purification of tau protein.
Main Results:
- Successful purification of biochemically pure untagged tau protein.
- Successful purification of biochemically pure polyhistidine-tagged tau protein.
- High yield and purity of tau protein suitable for downstream applications.
Conclusions:
- The described methods provide reliable protocols for tau protein purification.
- These protocols facilitate the study of tau protein's role in biological processes.
- The availability of pure tau protein is critical for advancing tauopathy research.
