Figure 1 Schematic protocol of PEG-PCMal
Figure 2 Structure of PEG-PCMal
Figure 3 Gel shift assay mechanism by PEG-PCMal depend on protein redox state
1. L. Makmura, M. Hamann, A. Areopagita, S. Furuta, A. Munoz and J. Momand. , “Development of a sensitive assay to detect reversibly oxidized protein cysteine sulfhydryl groups”, Antioxid Redox Signal., 2001, 3, (6), 1105.2. HH Wu, J.A. Thomas and J. Momand, “p53 protein oxidation in cultured cells in response to pyrrolidine dithiocarbamate: a novel method for relating the amount of p53 oxidation in vivo to the regulation of p53-responsive genes”, Biochem J., 2000, 351, 87.3. JR. Burgoyne, O. Oviosu and P. Eaton., “The PEG-switch assay: A fast semi-quantitative method to determine protein reversible cysteine oxidation”, J Pharmacol Toxicol Methods., 2013, 68, (3), 297.4. L. JTetsch, C. Koller, A. Donhofer and K. Jung, “Detection and function of an intramolecular disulfide bond in the pH-responsive CadC of Escherichia coli”, BMC Microbiol., 2011, doi: 10.1186/1471-2180-11-74.
Analysis of the redox states of TRX (Thioredoxin) in HeLa cells
Figure 4 Visualization of the redox state of the TRX in HeLa cells
Analysis of the redox states of protein (ATP synthase γ subunit) in Arabidopsis thaliana
Figure 5 Visualization of the redox state of the photoresponsive protein in Arabidopsis thaliana
Technical advisorDr. Toru Hisabori (Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology)Dr. Keisuke Yoshida (Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology)Dr. Satoshi Hara (School of Life Science and Technology, Tokyo Institute of Technology)