Fig 1: Comparison of mRNA and protein levels in HepG2 cells, 0 μM isoscopoletin group was used as a control (n = 3).(A-D) mRNA levels. (A) GPD2. (B) GPI. (C) Hsp90α. (D) PGK2. (E-H) Protein levels. (E) GPD2. (F) GPI. (G) Hsp90α. (H) PGK2. (Data were mean ± SD, *P < 0.05, **P < 0.01, ***P < 0.001).
Fig 2: SD-test capillary sharp and SD-test capillary scan (n = 3).(A) Hsp90α (0.945 μM). (B) GPI (0.5 μM). (C) GPD2 (0.02 μM). (D) PGK2 (5.3 μM).
Fig 3: The results of molecular docking.(A) Isoscopoletin-Hsp90AA1 (5njx). (B) Isoscopoletin-GPI (7w72). (C) Isoscopoletin-GPD2 (1x0v). (D) Isoscopoletin-PGK2 (2paa).
Fig 4: The effect of anti-GPD2 antibody between isoscopoletin and GPD2 (0.5 μM), which was analyzed by NT.115 (n = 3).(A) SD-test capillary sharp. (B) SD-test capillary scan. (C) MST time traces of isoscopoletin at 16 different concentrations (ranging from 0.000168 mM to 5.5 mM). (D) Failed, dependence of the MST signal on the isoscopoletin concentration (measured 30s after turning on heating).
Fig 5: The binding of isoscopoletin with glycolysis-proteins detected by NT.115 analysis (n = 3).MST time traces of isoscopoletin at 16 different concentrations, dependence of the MST signal on the isoscopoletin concentration (measured 30s after turning on heating). (A) Hsp90α (0.945 μM) with isoscopoletin (ranging from 0.000168 to 5.5 mM). (B) GPI (0.5 μM) with isoscopoletin (ranging from 0.000168 to 5.5 mM). (C) GPD2 (0.02 μM) with isoscopoletin (ranging from 0.000336 to 11 mM). (D) PGK2 (5.3 μM) with isoscopoletin (ranging from 0.0000839 to 2.75 mM).
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