Kinesin heavy chain motor domain protein: GST tagged: Homo sapiens recombinant

Kinesin heavy chain motor domain protein: GST tagged: Homo sapiens recombinant

Product uses

  • Measurement of microtubule-activated ATPase activity
  • Identification/characterization of proteins or small molecules that affect motor ATPase activity
  • Identification/characterization of proteins or small molecules that affect kinesin motility
  • Identification/characterization of proteins or small molecules that affect motor/microtubule interactions

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.


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.

Biological Activity
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.


Figure 2. Microtubule activated kinesin ATPase assay (Cat. # BK060) using kinesin heavy chain motor domain protein (Cat. # KR01) and pre-formed microtubules (Cat. # MT001). Each condition (microtubules (MT) alone, kinesin alone and microtubules + kinesin) was performed in triplicates.

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AuthorTitleJournalYearArticle Link
Perdomo, Doranda et al. TbKINX1B: a novel BILBO1 partner and an essential protein in bloodstream form Trypanosoma brucei Parasite2022Article Link
Lin, Jong Wei et al.Dexamethasone accelerates muscle regeneration by modulating kinesin-1-mediated focal adhesion signalsCell Death Discovery2021ISSN 2058-7716
Labrière, Christophe et al.New MKLP-2 inhibitors in the paprotrain series: Design, synthesis and biological evaluationsBioorganic and Medicinal Chemistry2016ISSN 1464-3391
Kadakkuzha, Beena M. et al.High-throughput screening for small molecule modulators of motor protein kinesinAssay and Drug Development Technologies2014ISSN 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 lineDARU, Journal of Pharmaceutical Sciences2013ISSN 1560-8115
Soppina, Virupakshi et al.Luminal Localization of α-tubulin K40 Acetylation by Cryo-EM Analysis of Fab-Labeled MicrotubulesPLoS ONE2012ISSN 1932-6203
Gutiérrez-Medina, Braulio et al.Visualizing individual microtubules by bright field microscopyAmerican Journal of Physics2010ISSN 0002--9505
Del Duca, Stefano et al.Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubulesand actin filamentsBiochemical Journal2009ISSN 1470-8728
Funk, C. Joel et al.Development of high-throughput screens for discovery of kinesin adenosine triphosphatase modulatorsAnalytical Biochemistry2004ISSN 0003-2697
Wada, Yuuko et al.Evidence for a Novel Affinity Mechanism of Motor-assisted Transport Along MicrotubulesMolecular Biology of the Cell2000ISSN 1059-1524
Endow, Sharyn A. et al.Determinants of Kinesin Motor PolarityScience1998ISSN 0036-8075

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