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Mol Biol Cell November 1, 2012; 23 (22): 4393-401.

One-step purification of assembly-competent tubulin from diverse eukaryotic sources.

Widlund PO , Podolski M , Reber S , Alper J , Storch M , Hyman AA , Howard J , Drechsel DN .

We have developed a protocol that allows rapid and efficient purification of native, active tubulin from a variety of species and tissue sources by affinity chromatography. The affinity matrix comprises a bacterially expressed, recombinant protein, the TOG1/2 domains from Saccharomyces cerevisiae Stu2, covalently coupled to a Sepharose support. The resin has a high capacity to specifically bind tubulin from clarified crude cell extracts, and, after washing, highly purified tubulin can be eluted under mild conditions. The eluted tubulin is fully functional and can be efficiently assembled into microtubules. The method eliminates the need to use heterologous systems for the study of microtubule-associated proteins and motor proteins, which has been a major issue in microtubule-related research.

PubMed ID: 22993214
PMC ID: PMC3496613
Article link: Mol Biol Cell

Genes referenced: alb ckap5 dnajb1 herpud1 hsp70 hsp90aa1.1 hspa1l

Article Images: [+] show captions
References [+] :
Akhmanova, Tracking the ends: a dynamic protein network controls the fate of microtubule tips. 2008, Pubmed

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