S-Trityl-L-cysteine
Chemical Name: S-(Triphenylmethyl)-L-cysteine
Biological Activity
S-Trityl-L-cysteine is a potent, cell-permeable, selective inhibitor of mitotic kinesin Eg5, a protein required for establishing and maintaining a bipolar spindle. Inhibits basal ATPase activity (IC50 = 1 mM) and microtubule-activated ATPase activity of Eg5 (IC50 = 140 nM). Induces mitotic arrest in HeLa cells with an IC50 of 700 nM. Displays antitumor activity.Technical Data
The technical data provided above is for guidance only.
For batch specific data refer to the Certificate of Analysis.
Tocris products are intended for laboratory research use only, unless stated otherwise.
Background References
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In vitro screening for inhibitors of the human mitotic kinesin Eg5 with antimitotic and antitumour activities.
DeBonis et al.
Mol.Cancer Ther., 2004;3:1079 -
Identification of the protein binding region of S-trityl-L-cysteine, a new potent inhibitor of mitotic kinesin Eg5.
Brier et al.
Biochemistry, 2004;43:13072
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Citations for S-Trityl-L-cysteine
The citations listed below are publications that use Tocris products. Selected citations for S-Trityl-L-cysteine include:
6 Citations: Showing 1 - 6
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A Ploidy Increase Promotes Sensitivity of Glioma Stem Cells to Aurora Kinases Inhibition.
Authors: Cilibrasi Et al.
J Oncol 2019;2019:9014045
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Dissecting the role of the tubulin code in mitosis.
Authors: Ferreira Et al.
Methods Cell Biol 2018;144:33
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Inner centromere localization of the CPC maintains centromere cohesion and allows mitoticcheckpoint silencing.
Authors: Hengeveld
Nat Commun 2017;8:15542
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Baculoviral delivery of CRISPR/Cas9 facilitates efficient genome editing in human cells.
Authors: Hindriksen Et al.
PLoS One 2017;12:e0179514
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Nuclear translocation of Cyclin B1 marks the restriction point for terminal cell cycle exit in G2 phase.
Authors: Müllers Et al.
PLoS Genet 2014;13:2733
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PP2A/B55 and Fcp1 regulate Greatwall and Ensa dephosphorylation during mitotic exit.
Authors: Hégarat Et al.
J Pharmacol Exp Ther 2014;10:e1004004
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