Figure 2 | Scientific Reports

Figure 2

From: Chemical activation of divergent protein tyrosine phosphatase domains with cyanine-based biarsenicals

Figure 2

actHePTP is strongly activated by AsCy5. (A) PTP activity of actHePTP (200 nM) was measured with pNPP (1.5625 mM, quenched assay) in the absence (DMSO) or presence of the indicated biarsenicals (500 nM) after 120-minute pre-incubations. (B) Dose dependence of actHePTP activation. PTP activity of actHePTP (200 nM) was measured with pNPP (1.5625 mM, quenched assay) in the absence (DMSO) or presence of the indicated concentrations of AsCy5 after 20-min pre-incubations. (C) Time dependence of actHePTP activation. PTP reaction rates of actHePTP (200 nM) were measured with pNPP (2 mM, continuous assay) in the absence (DMSO) or presence of AsCy5 (625 nM) after indicated pre-incubation times. (D) The activity of wt-HePTP and actHePTP (2 µM) was measured with the phosphopeptide TGFLTEpYVATR (200 µM) as a substrate after 20-min of pre-incubation in the absence (DMSO) or presence of AsCy5 (4 µM). (E) The activity of wt-HePTP and actHePTP (2 µM) was measured with the phosphopeptide DADEpYLIPQQG (100 µM) as a substrate after 20-min of pre-incubation in the absence (DMSO) or presence of AsCy5 (4 µM).

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