Tubulin protein: Hela cancer cell

Product Uses Include:
Screening for anti-tumor drugs
Assessing the effects of modulators of microtubule dynamics on tubulin isolated from actively growing cells
A new substrate for motor proteins

Material
HeLa Cell tubulin is isolated from the human cervical cancer derived HeLa S3 cell line, a model system to study many aspects of tumor cell growth. Hela Cell tubulin may be used in all situations where previously bovine brain tubulin has been employed, for example drug screening, motility assays and biochemical studies including microtubule dynamics. The advantage of using this novel tubulin is that it is derived from an actively dividing cell line which often, in contrast to brain derived tubulins, more accurately portrays the situation that many researchers are trying to reconstruct in vitro.
The specificity of ligands for for a particular tubulin variant can be determined by performing comparative studies with both cancer cell and neuronal tubulins. Cytoskeleton, Inc. has advanced this concept by developing the Tubulin Ligand Index (TLI) system (patent pending). In this system, IC50 values for inhibitory compounds or EC50 values for stabilizing compounds are determined in in polymerization assays using cancer cell and neuronal tubulins. The IC50 or EC50 values for each tubulin variant are analyzed as a ratio (neuronal/cancer cell) and allow for determinations of the relative specificity for each tested compound. TLI values greater than 1.0 indicate that the particular compound is more active on cancer cell tubulin. Conversely, TLI values less than 1.0 suggest that a compound is more specific for neuronal tubulin. Table 1 summarizes data from a study comparing the specificity of several tubulin ligands using the TLI system.
HeLa cell tubulin is also available as a biotinylated conjugate for scintillation proximity assay (SPA) applications (Cat. # H003). For another human cancer cell derived tubulin, see our MCF-7 tubulin (Cat. # H005) Purity H001 contains >90% pure HeLa cell tubulin. Purity is determined by scanning densitometry of proteins on SDS-PAGE gels.

Please contact us at for specific academic pricing.