Kinesin heavy chain motor domain protein (KIF5A): 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

The conserved motor domain of human Kinesin Heavy Chain (KIF5A) has been produced in a bacterial expression system. The recombinant protein contains a GST-tag at the amino terminus and has a combined calculated molecular weight of approximately 70 kDa. The protein has been determined to be biologically active in a microtubule-activated ATPase assay. The protein is supplied as a white lyophilized powder.

Protein purity is determined by scanning densitometry of Coomassie Blue stained protein on an SDS gradient gel. Figure 1 shows 10 µg of KR01 protein that was determined to be 88% pure. The major contaminant at approximately 30 kDa is GST protein. The microtubule-activated ATPase activity of the Kinesin Heavy Chain is not inhibited by this contaminant.


Figure 1. Kinesin Heavy Chain Motor Protein Purity Determination. A 10 µg sample of recombinant Kinesin Heavy Chain Motor Domain protein was separated on a 420% SDS gel along with Mark12 molecular weight markers (Invitrogen) and stained with Coomassie Blue. The fusion protein has an approximate molecular weight of 65 kDa. Protein quantitation was determined using the Precision Red™ Protein Assay reagent. (Cat. # ADV02)

Biological Activity - Microtubule Activated ATPase Assay
Kinesin Heavy Chain ATPase activity was measured by monitoring real time free phosphate generation using the Kinesin ELIPA Assay Biochem Kit (Cat. # BK060). The assay is based upon an absorbance shift (330 nm—360 nm) that occurs when 2-amino-6mercapto-7-methylpurine ribonucleoside (MESG) is catalytically converted to 2-amino-6-mercapto-7-methylpurine in the presence of inorganic phosphate (Pi). One molecule of Pi will yield one molecule of 2-amino-6-mercapto-7-methylpurine in an essentially irreversible reaction. Hence, the absorbance at 360 nm is directly proportional to the amount of Pi generated in the kinesin ATPase reaction.


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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