• Positive control for in vitro microtubule polymerization studies
• Substrate for protein kinases
• Control protein for neuronal plaque and Alzheimer’s research

Tau protein is a microtubule-associated protein critical for stabilizing neuronal structure and supporting axonal transport in the central nervous system. Abnormal tau aggregation is a hallmark of neurodegenerative disorders, including Alzheimer’s disease and other tauopathies.

Native Tau proteins have been isolated from MAP-rich bovine brain tubulin by ion exchange chromatography;

• Molecular weight: ~37-50 kDa (Tau proteoforms)
• Formulation: supplied as a lyophilized powder
• Composition: when resuspended to 1 mg/ml, the buffer composition is: 40 mM PIPES pH 7.5, 0.8 mM EDTA, 0.8 mM EGTA, 5% mannitol, 1% dextran and 10 mM NaCl

Protein purity is assessed by scanning densitometry of Coomassie Blue stained protein on a 4-20% polyacrylamide gel.

• Tau proteoforms (37-70 kDa) ≥90%
• Map 1 & 2 ≤1%
• Other MAPs and non-MAP proteins ≤9%

The biological activity of Tau protein is assessed by its ability to enhance the in vitro polymerization of tubulin T240. This is measured by monitoring the increase in absorbance at 340 nm. At a concentration of 100 µg/ml, Tau produces approximately a 10-fold increase in the tubulin polymerization rate (Vmax). See datasheet for details.