Tubulin (bovine brain, >99% pure, lyophilized)

Product Uses Include

• Positive control for the study of microtubule binding proteins
• Investigation of the the effect of Tau on microtubule dynamics
  
  

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.

Figure 1: Tau protein purity determination. A 10 ug sample of TA01 was separated by electrophoresis in a 12% SDS-PAGE system, and stained with Coomassie Blue.

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.

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