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phosphosens csox-based sensor assay assayquant aqt0135  (AssayQuant Technologies Inc)
90
AssayQuant Technologies Inc phosphosens csox-based sensor assay assayquant aqt0135
(A) Inhibition of STK3 by 6 using the <t>PhosphoSens</t> CSox-based sensor assay (AssayQuant <t>AQT0135),</t> with fluorescence intensity as a readout (excitation/emission 360/485 nm). (B) The initial reaction velocity in (A) was plotted against the log compound concentration, and IC50 values were calculated using log [inhibitor] vs response four-parameter variable slope equation in Prism 8 software. (C) Fluorescent Thermal melt curves for STK3 and STK4 in the presence of 6, 11, and 32 (20 μM) showing protein thermal shifts (DTm) >8°C compared with DMSO. (D) Binding affinities and thermodynamic signatures from isothermal titration calorimetry (ITC) for compounds 6 and 32. (E) Representative ITC binding data for the interactions between 6 and STK3 and STK4. The normalized heat of binding with the single-site binding fits (red line) is shown, and the raw isotherms of titration heat are displayed as inserts.
Phosphosens Csox Based Sensor Assay Assayquant Aqt0135, supplied by AssayQuant Technologies Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/four-parameter+sigmoidal+concentration-response+curve+graphpad+prism8/phosphosens+csox+based+sensor+assay+assayquant+aqt0135/pmc10149138-152-13-17
Average 90 stars, based on 1 article reviews
phosphosens csox-based sensor assay assayquant aqt0135 - by Bioz Stars, 2026-09
90/100 stars
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mpxv a35 protein  (Sino Biological)
93
Sino Biological mpxv a35 protein
(A) Inhibition of STK3 by 6 using the <t>PhosphoSens</t> CSox-based sensor assay (AssayQuant <t>AQT0135),</t> with fluorescence intensity as a readout (excitation/emission 360/485 nm). (B) The initial reaction velocity in (A) was plotted against the log compound concentration, and IC50 values were calculated using log [inhibitor] vs response four-parameter variable slope equation in Prism 8 software. (C) Fluorescent Thermal melt curves for STK3 and STK4 in the presence of 6, 11, and 32 (20 μM) showing protein thermal shifts (DTm) >8°C compared with DMSO. (D) Binding affinities and thermodynamic signatures from isothermal titration calorimetry (ITC) for compounds 6 and 32. (E) Representative ITC binding data for the interactions between 6 and STK3 and STK4. The normalized heat of binding with the single-site binding fits (red line) is shown, and the raw isotherms of titration heat are displayed as inserts.
Mpxv A35 Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/four-parameter+sigmoidal+concentration-response+curve+graphpad+prism8/Monkeypox+Virus+(MPXV)+Protein+A35/pmc10213010__41421_2023_556_MOESM1_ESM-14-35-38
Average 93 stars, based on 1 article reviews
mpxv a35 protein - by Bioz Stars, 2026-09
93/100 stars
  Buy from Supplier

Image Search Results


(A) Inhibition of STK3 by 6 using the PhosphoSens CSox-based sensor assay (AssayQuant AQT0135), with fluorescence intensity as a readout (excitation/emission 360/485 nm). (B) The initial reaction velocity in (A) was plotted against the log compound concentration, and IC50 values were calculated using log [inhibitor] vs response four-parameter variable slope equation in Prism 8 software. (C) Fluorescent Thermal melt curves for STK3 and STK4 in the presence of 6, 11, and 32 (20 μM) showing protein thermal shifts (DTm) >8°C compared with DMSO. (D) Binding affinities and thermodynamic signatures from isothermal titration calorimetry (ITC) for compounds 6 and 32. (E) Representative ITC binding data for the interactions between 6 and STK3 and STK4. The normalized heat of binding with the single-site binding fits (red line) is shown, and the raw isotherms of titration heat are displayed as inserts.

Journal: Journal of medicinal chemistry

Article Title: Inhibitors of the Hippo Pathway Kinases STK3/MST2 and STK4/MST1 Have Utility for the Treatment of Acute Myeloid Leukemia

doi: 10.1021/acs.jmedchem.1c00804

Figure Lengend Snippet: (A) Inhibition of STK3 by 6 using the PhosphoSens CSox-based sensor assay (AssayQuant AQT0135), with fluorescence intensity as a readout (excitation/emission 360/485 nm). (B) The initial reaction velocity in (A) was plotted against the log compound concentration, and IC50 values were calculated using log [inhibitor] vs response four-parameter variable slope equation in Prism 8 software. (C) Fluorescent Thermal melt curves for STK3 and STK4 in the presence of 6, 11, and 32 (20 μM) showing protein thermal shifts (DTm) >8°C compared with DMSO. (D) Binding affinities and thermodynamic signatures from isothermal titration calorimetry (ITC) for compounds 6 and 32. (E) Representative ITC binding data for the interactions between 6 and STK3 and STK4. The normalized heat of binding with the single-site binding fits (red line) is shown, and the raw isotherms of titration heat are displayed as inserts.

Article Snippet: Biochemical characterization of STK3/4 inhibitors. (A) Inhibition of STK3 by 6 using the PhosphoSens CSox-based sensor assay (AssayQuant AQT0135), with fluorescence intensity as a readout (excitation/emission 360/485 nm). (B) The initial reaction velocity in (A) was plotted against the log compound concentration, and IC 50 values were calculated using log [inhibitor] vs response four-parameter variable slope equation in Prism 8 software. (C) Fluorescent Thermal melt curves for STK3 and STK4 in the presence of 6, 11 , and 32 (20 μM) showing protein thermal shifts (DT m ) >8°C compared with DMSO. (D) Binding affinities and thermodynamic signatures from isothermal titration calorimetry (ITC) for compounds 6 and 32 . (E) Representative ITC binding data for the interactions between 6 and STK3 and STK4.

Techniques: Inhibition, Fluorescence, Concentration Assay, Software, Binding Assay, Isothermal Titration Calorimetry, Titration