-
-
Overview
-
Product Uses
IC50 & EC50 determinations for anti-tubulin ligands.
Characterization of tubulin binding proteins
Background Information
Tubulin is composed of a heterodimer of two closely related 55 kDa proteins called alpha and beta tubulin. The two proteins are encoded by separate genes, or small gene families, whose sequences are highly conserved throughout the eukaryotic kingdom.
Tubulin polymerizes to form structures called microtubules (MTs). When tubulin polymerizes it initially forms protofilaments, MTs consist of 13 protofilaments and are 25 nm in diameter. Each µm of MT length is composed of 1650 heterodimers. Microtubules are highly ordered structures that have an intrinsic polarity.
Materials
Tubulin protein has been purified from sheep brain by an adaptation of the method of Shelanski et al. Further purification to >99% purity was achieved by cation exchange chromatography. Sheep brain tubulin is supplied in 0.10 ml aliquots at 12 mg/ml in 50 mM potassium MES pH 6.8, 0.25 mM MgCl2, 0.5 mM EGTA, 33% glycerol and 0.1 mM GTP. Tubulin consists of a heterodimer of one alpha and one beta isotype, each tubulin isotype is 55 kDa in size, SDS-PAGE analysis shows tubulin running as a 55 kDa species. Typically, the molar equivalent of tubulin is defined as the heterodimer which has a molecular weight of 110 kDa.
Storage
It is recommended that T234S be stored at -70°C, where it is stable for 6 months. The protein should be rapidly thawed in a room temperature water bath, immediately transferred to ice and aliquoted into “experiment sized” amounts. Snap freeze aliquots in liquid nitrogen and store at -70°C.
Aliquots of T234S MUST be snap frozen in liquid nitrogen prior to storage at -70°C, failure to do this results in significant loss of activity.Please contact us at for specific academic pricing.
-
- Properties
-
Overview