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.
Protein purity is determined by scanning densitometry of Coomassie Blue stained protein on a 12% polyacrylamide gel. All kinesin motor domains are >85% pure. See figure 1 for example purities.
Kinesn motor activity is driven by ATP hydrolysis. All motor domain proteins therefore are tested with regards to their microtubule activated ATPase activity. Stringent quality controls that all Cytoskeleton, Inc's purified kinesin motor domains have ATPase activities comparable to published data.
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|Perdomo, Doranda et al.||TbKINX1B: a novel BILBO1 partner and an essential protein in bloodstream form Trypanosoma brucei||Parasite||2022||Article Link|
|Lin, Jong Wei et al.||Dexamethasone accelerates muscle regeneration by modulating kinesin-1-mediated focal adhesion signals||Cell Death Discovery||2021||ISSN 2058-7716|
|Labrière, Christophe et al.||New MKLP-2 inhibitors in the paprotrain series: Design, synthesis and biological evaluations||Bioorganic and Medicinal Chemistry||2016||ISSN 1464-3391|
|Kadakkuzha, Beena M. et al.||High-throughput screening for small molecule modulators of motor protein kinesin||Assay and Drug Development Technologies||2014||ISSN 1557-8127|
|Abnous, Khalil et al.||Synthesis and molecular modeling of six novel monastrol analogues: Evaluation of cytotoxicity and kinesin inhibitory activity against HeLa cell line||DARU, Journal of Pharmaceutical Sciences||2013||ISSN 1560-8115|
|Soppina, Virupakshi et al.||Luminal Localization of α-tubulin K40 Acetylation by Cryo-EM Analysis of Fab-Labeled Microtubules||PLoS ONE||2012||ISSN 1932-6203|
|Gutiérrez-Medina, Braulio et al.||Visualizing individual microtubules by bright field microscopy||American Journal of Physics||2010||ISSN 0002--9505|
|Del Duca, Stefano et al.||Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubulesand actin filaments||Biochemical Journal||2009||ISSN 1470-8728|
|Funk, C. Joel et al.||Development of high-throughput screens for discovery of kinesin adenosine triphosphatase modulators||Analytical Biochemistry||2004||ISSN 0003-2697|
|Wada, Yuuko et al.||Evidence for a Novel Affinity Mechanism of Motor-assisted Transport Along Microtubules||Molecular Biology of the Cell||2000||ISSN 1059-1524|
|Endow, Sharyn A. et al.||Determinants of Kinesin Motor Polarity||Science||1998||ISSN 0036-8075|
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