Tau protein (TA01)

Material
Tau protein is isolated from MAP-rich bovine brain tubulin by ion exchange chromatography over a phosphocellulose matrix. The protein is supplied lyophilized. When reconstituted to 1 mg/ml (protein concentration determined by Precision Red Advanced Protein Assay, Cat. # ADV02), the protein will be in in 50 mM PIPES, 1 mM EDTA and 16 mM NaCl.

Purity
Purity is determined by scanning densitometry of proteins on SDS-PAGE gels. Samples are approximately 90% Tau proteins. Approximatley 1% contamination by high molecular weight MAPs and 9% other MAPs and non-MAP proteins.

Biological Activity
Biological activity of is determined by the ability of Tau protein to enhance the polymerization rate (Vmax) of purified bovine brain tubulin (Cat. # TL238) in vitro. Stringent quality control ensures that the Tau protein will stimulate tubulin polymerization approximately 20-fold when compared to tubulin polymerization without Tau fraction.

Figure 2: Tubulin polymerization in the presence and absence of Tau protein. Tubulin polymerization reactions were carried out as in BK006 with 3 mg/ml of pure bovine brain tubulin (Cat. # TL238) being polymerized in the presence and absence of 1 mg/ml Tau protein.

Examples of publications where this product was used:
Roger, B., Al-Bassam, J., Dehmelt, L., Milligan, R. A. and Halpain, S. (2004). MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain. Curr. Biol. 14, 363-371.

Rouzier, R., Rajan, R., Wagner, P., Hess, K. R., Gold, D. L., Stec, J., Ayers, M., Ross, J. S., Zhang, P., Buchholz, T. A. et al. (2005). Microtubule-associated protein tau: A marker of paclitaxel sensitivity in breast cancer. Proc. Natl. Acad. Sci. U. S. A. 102, 8315-8320.