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. Author manuscript; available in PMC: 2020 Nov 1.
Published in final edited form as: Cell Signal. 2019 Jul 25;63:109366. doi: 10.1016/j.cellsig.2019.109366

Figure 2. The affinity of MELK1−326,T167E for arrestin-31−393 in the presence of ATP.

Figure 2.

A binding curve for bovine arrestin-31−393 with human MELK1−326,T167E in the presence of 1 mM ATP and 2 mM MgCl2 is shown with the average Kd value (n=3). Microscale thermophoresis was performed at a constant concentration of Tris-NTA-labeled His-MELK1−326,T167E (50 nM) with a serial dilution of arrestin-31−393 (0–40 μM). The binding isotherm was calculated using preset T-jump in the software PALMIST [59, 60], and the graph was created in the program GUSSI.