Microtubule associated protein rich fraction: bovine brain

Product Uses Include

• Positive control for the study of microtubule binding proteins
• Investigation of the the effect of MAPs on microtubule dynamics
• Substrate for many protein kinases
  
  

Material
A microtubule associated protein (MAP) fraction has been isolated from bovine brain by temperature induced tubulin polymerization followed by ionic exchange chromatography over a phosphocellulose matrix and salt elution (1, 2). The MAP fraction protein is supplied as a white lyophilized powder

Purity
Protein purity is determined by scanning densitometry of Coomassie Blue stained protein on a 12% polyacrylamide gel. MAP2 constitutes 70% of the total protein (see Figure 1).

	Figure 1: Microtubule associated protein fraction purity determination. A 10 µg sample of MAPF was separated by electrophoresis in a 12% SDS-PAGE system, and stained with Coomassie Blue.

Biological Activity
The biological activity of the MAP fraction is determined by the ability of 0.1 mg/ml MAP fraction to enhance the polymerization rate (Vmax) of purified bovine brain tubulin (Cat. # TL238) in vitro. Stringent quality control ensures that the MAP fraction protein will stimulate tubulin polymerization at least five fold when compared to tubulin polymerization without MAP fraction.

	Figure 2: Tubulin polymerization in the presence and absence of microtubule associated protein fraction. Tubulin polymerization reactions were carried out as in BK006 with 5% glycerol containing 2 mg/ml of pure bovine brain tubulin (Cat. # TL238) being polymerized in the presence and absence of 0.1 mg/ml MAP fraction protein.

References

1. Vallee, R. B. 1982. J. Cell Biol. 92, 435-442
2. Kuznetsov S. A., et al. 1981. FEBS Lett. 135, 241-244

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Product Description

MSDS

Datasheet

Cat #

Microtubule associated protein rich fraction: bovine brain MAPF

Cho, H. P., Liu, Y., Gomez, M., Dunlap, J., Tyers, M. and Wang, Y. (2005). The dual-specificity phosphatase CDC14B bundles and stabilizes microtubules. Mol. Cell. Biol. 25, 4541-4551.

Satish, L., Blair, H. C., Glading, A. and Wells, A. (2005). Interferon-inducible protein 9 (CXCL11)-induced cell motility in keratinocytes requires calcium flux-dependent activation of μ-calpain. Mol. Cell. Biol. 25, 1922-1941.

Teckchandani, A. M., Birukova, A. A., Tar, K., Verin, A. D. and Tsygankov, A. Y. (2005). The multidomain protooncogenic protein c-Cbl binds to tubulin and stabilizes microtubules. Exp. Cell Res. 306, 114-127.

Mamoune, A., Luo, J. H., Lauffenburger, D. A. and Wells, A. (2003). Calpain-2 as a target for limiting prostate cancer invasion. Cancer Res. 63, 4632-4640.

Nielsen, F. C., Nielsen, J., Kristensen, M. A., Koch, G. and Christiansen, J. (2002). Cytoplasmic trafficking of IGF-II mRNA-binding protein by conserved KH domains. J. Cell Sci. 115, 2087-2097.

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