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

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

Item no.	TL238-A
Manufacturer	Cytoskeleton
Amount	4 x 250 ug
Quantity options	4 x 250 ug 1 x 1 mg 5 x 1 mg 10 x 1 mg 1 x 10 mg
Category	Peptides & Proteins Recombinant Proteins Cell Biology Cytoskeleton Mikrotubules
Type	Proteins
Specific against	Cattle (Bovine)
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.
Citations	Hsieh et al., 2012. DDA3 Stabilizes Microtubules and Suppresses Neurite Formation. J. Cell Sci. doi: 10.1242/Ÿ??jcs.099150. Rocha et al., 2012. Cell cycle arrest through inhibition of tubulin polymerization by withaphysalin F, a bioactive compound isolated from Acnistus arborescens. Invest. New Drugs. v 30, pp 959-966. Hawkins et al., 2012. Perturbations in Microtubule Mechanics from Tubulin Preparation. Cell. Mol. Bioengineer. v 5, pp 227-238. Zhang et al., 2011. Growth-Arrest-Specific Protein 2 Inhibits Cell Division in Xenopus Embryos. PLoS ONE. 6:e24698. Feizabadi et al., 2011. Measuring the persistence length of MCF7 cell microtubules in vitro. Biotech. J. v 6, pp 882-887. Skiniotis et al., 2004. Modulation of kinesin binding by the C-termini of tubulin. EMBO J. v 23, pp 989-999. Thompson et al., 2004. Dynamin 2 binds g-tubulin and participates in centrosome cohesion. Nat. Cell Biol. v 6, pp 335-342. Moores et al., 2004. Mechanism of microtubule stabilization by doublecortin. Mol. Cell. v 14, pp 833-839. Fan et al., 2004. Polarity proteins control ciliogenesis via kinesin motor interactions. Curr. Biol. v 14, pp 1451-1461. Zhang et al., 2003. HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J. v 22, pp 1168-1179.?iu Haggarty et al., 2003. Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc. Natl. Acad. Sci. U.S.A. v 100, pp 4389-4394. Kar et al., 2003. Repeat motifs of tau bind to the insides of microtubules in the absence of taxol. EMBO J. v 22, pp 70-77. Ovechkina et al., 2002. K-loop insertion restores microtubule depolymerizing activity of a "neckless" MCAK mutant. J. Cell Biol. v 159, pp 557-562. Groisman et al., 2000. CPEB, maskin, and cyclin B1 mRNA at the mitotic apparatus: implications for local translational control of cell division. Cell. v 103, pp 435-447. Larsson et al., 1999. Mutations of oncoprotein 18/stathmin identify tubulin-directed regulatory activities distinct from tubulin association. Mol. Cell. Biol. v 19, pp 2242-2250. Nogales et al., 1998. Structure of the &alpha,&beta, tubulin dimer by electron crystallography. Nature. v 391, pp 199-203.
ECLASS 10.1	32160409
ECLASS 11.0	32160409
UNSPSC	12352202
Alias	Frozen pure tubulin is used for high fidelity work where T240's excipients would otherwise interfer with the experiment, tubulin, tubulin protein, porcine tubulin, porcine brain tubulin.
Similar products	tubulin, tubulin protein, porcine tubulin, Frozen pure tubulin is used for high fidelity work where T240's excipients would otherwise interfer with the experiment, porcine brain tubulin.
Available
Shipping Temperature	AT
Storage Conditions	On Arrival: 4°C
Delivery Time	1-2 Weeks
Product Uses	ositive 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.
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-foldWhen compared to tubulin polymerization without Tau fraction.
Figure 1 Legend	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.
Figure 2 Legend	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.

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

TL238-A.pdf

TL238-A-datasheet.pdf

TL238-A-safety-datasheet.pdf