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.
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