Related Experiment Video
Updated: Feb 9, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
Published on: January 2, 2015
Preparation of Tau Oligomers After the Protein Extraction from Bacteria and Brain Cortices
Elentina K Argyrousi1,2,3, Agnieszka Staniszewski1,2, Russell E Nicholls1,2
1Department of Pathology and Cell Biology, Columbia University, New York, NY, USA.
Abstract:
Oligomerization of soluble tau protein is attracting the attention of an increasingly larger number of scientists involved in research on Alzheimer's disease and other tauopathies. A variety of methods have been developed for the purification of proteins from biological tissues and bacterial cells. Various types of high performance liquid chromatography (HPLC) and affinity tags represent the most common techniques for isolating proteins. Here, we describe a procedure for extracting recombinant tau protein from bacterial cells, utilizing a 6×His affinity tag, or endogenous tau from brain cortices using acid extraction followed by fast protein liquid chromatography (FPLC). Additionally, we introduce a method for oligomerization based on reduction and oxidation of cysteine residues. Our preparation assures high yield of tau protein, while preserving its physiological function.
Related Concept Videos
Cytoskeletal Proteins in Bacteria
Kendall's Tau Test
A τ value of +1 indicates...
Protein-protein Interfaces
The Roles of Bacteria and Fungi in Plant Nutrition
The Tree of Life - Bacteria, Archaea, Eukaryotes
Other Unique Bacteria

