KHC Motor Domain (Hm.sap.)

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There are approximately 50 human kinesins that are currently divided into at least 14 classes. Kinesins are involved in almost all aspects of intracellular transport and their well documented role in cell division suggests that they may be excellent targets for anti-mitotic drug discovery. All kinesin proteins contain a conserved motor domain that contains a microtubule binding site and the ATP binding / hydrolysis site. The motor domain of various kinesins have been shown to have widely differing sensitivities to ATP analogs and inhibitory compounds such as monastrol, such results lead the way to the identification of therapeutically useful kinesin specific inhibitors. Cytoskeleton, Inc. has made available a selection of recombinant human kinesin motor domain proteins from 8 of the 14 reported kinesin classes. The proteins are extensively quality controlled for purity (> 85%) and biological activity (microtubule activated ATPase activity must be at least comparable to published data). The protein domains are useful as targets for anti-mitotic drug discovery and as reagents for comparative studies of kinesin class specific motor activities.

Figure 1. Purity of kinesin motor domain proteins. BimC (BM01), CENP-E (CP01) and Eg5 (EG01) were run on SDS-PAGE gels and stained with coomassie blue.