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Fluorescence-based Monitoring of PAD4 Activity via a Pro-fluorescence Substrate Analog
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Fluorescence-based Monitoring of PAD4 Activity via a Pro-fluorescence Substrate Analog

Article DOI: 10.3791/52114-v • 08:37 min • November 5th, 2014
November 5th, 2014 •
1, 1, 1
1Department of Chemistry, Lehigh University

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PAD4 is an enzyme responsible for the conversion of peptidyl-arginine to peptidyl-citrulline. Dysregulation of PAD4 has been implicated in a number of human diseases. A facile and high-throughput compatible fluorescence based PAD4 assay is described.

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Fluorescence-based Monitoring PAD4 Activity Pro-fluorescence Substrate Analog Post-translational Modifications Protein Functional States Covalent Variations Histone Tails Peptidyl-arginine Deiminase 4 (PAD4) Citrulline Residue Assays Operational Feasibility Sensitivity Non-covalent PAD4 Inhibitors Fluorescence-based Assay Protease Trypsin High-throughput Screening Conditions Signal-to-noise Ratio Crude Cell Lysates
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