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adam10 substrate  (R&D Systems)


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    Structured Review

    R&D Systems adam10 substrate
    Adam10 Substrate, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 78 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/fluorogenic+adam10+substrate/Mca-KPLGL-Dpa-AR-NH2+Fluorogenic+Peptide+Substrate/pm34324289-92-4-9
    Average 95 stars, based on 78 article reviews
    adam10 substrate - by Bioz Stars, 2026-10
    95/100 stars

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    Related Articles

    Fluorescence:

    Article Title: Repurposed small molecule toxin inhibitors neutralise a diversity of venoms from the Neotropical viperid snake genus Bothrops
    Article Snippet: C for 25 min (to keep conditions identical to the drug inhibition assays described below). Plates were then allowed to acclimatise to room temperature for 5 min, before 75 µL of fluorescent substrate (Bio Techne, Cat. no. ES010) at a final 7.5 µM reaction concentration in SVMP assay buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl) was added to each well. Immediately following addition of substrate, the

    Inhibition:

    Article Title: Repurposed small molecule toxin inhibitors neutralise a diversity of venoms from the Neotropical viperid snake genus Bothrops
    Article Snippet: C for 25 min (to keep conditions identical to the drug inhibition assays described below). Plates were then allowed to acclimatise to room temperature for 5 min, before 75 µL of fluorescent substrate (Bio Techne, Cat. no. ES010) at a final 7.5 µM reaction concentration in SVMP assay buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl) was added to each well. Immediately following addition of substrate, the

    Incubation:

    Article Title: Repurposed small molecule toxin inhibitors neutralise a diversity of venoms from the Neotropical viperid snake genus Bothrops
    Article Snippet: C for 25 min (to keep conditions identical to the drug inhibition assays described below). Plates were then allowed to acclimatise to room temperature for 5 min, before 75 µL of fluorescent substrate (Bio Techne, Cat. no. ES010) at a final 7.5 µM reaction concentration in SVMP assay buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl) was added to each well. Immediately following addition of substrate, the

    Concentration Assay:

    Article Title: Repurposed small molecule toxin inhibitors neutralise a diversity of venoms from the Neotropical viperid snake genus Bothrops
    Article Snippet: C for 25 min (to keep conditions identical to the drug inhibition assays described below). Plates were then allowed to acclimatise to room temperature for 5 min, before 75 µL of fluorescent substrate (Bio Techne, Cat. no. ES010) at a final 7.5 µM reaction concentration in SVMP assay buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl) was added to each well. Immediately following addition of substrate, the

    Injection:

    Article Title: Repurposed small molecule toxin inhibitors neutralise a diversity of venoms from the Neotropical viperid snake genus Bothrops
    Article Snippet: C for 25 min (to keep conditions identical to the drug inhibition assays described below). Plates were then allowed to acclimatise to room temperature for 5 min, before 75 µL of fluorescent substrate (Bio Techne, Cat. no. ES010) at a final 7.5 µM reaction concentration in SVMP assay buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl) was added to each well. Immediately following addition of substrate, the

    Mass Spectrometry:

    Article Title: Repurposed small molecule toxin inhibitors neutralise a diversity of venoms from the Neotropical viperid snake genus Bothrops
    Article Snippet: C for 25 min (to keep conditions identical to the drug inhibition assays described below). Plates were then allowed to acclimatise to room temperature for 5 min, before 75 µL of fluorescent substrate (Bio Techne, Cat. no. ES010) at a final 7.5 µM reaction concentration in SVMP assay buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl) was added to each well. Immediately following addition of substrate, the

    Proximity Ligation Assay:

    Article Title: Repurposed small molecule toxin inhibitors neutralise a diversity of venoms from the Neotropical viperid snake genus Bothrops
    Article Snippet: C for 25 min (to keep conditions identical to the drug inhibition assays described below). Plates were then allowed to acclimatise to room temperature for 5 min, before 75 µL of fluorescent substrate (Bio Techne, Cat. no. ES010) at a final 7.5 µM reaction concentration in SVMP assay buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl) was added to each well. Immediately following addition of substrate, the

    In Vitro:

    Article Title: Repurposed small molecule toxin inhibitors neutralise a diversity of venoms from the Neotropical viperid snake genus Bothrops
    Article Snippet: C for 25 min (to keep conditions identical to the drug inhibition assays described below). Plates were then allowed to acclimatise to room temperature for 5 min, before 75 µL of fluorescent substrate (Bio Techne, Cat. no. ES010) at a final 7.5 µM reaction concentration in SVMP assay buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl) was added to each well. Immediately following addition of substrate, the

    Activity Assay:

    Article Title: Repurposed small molecule toxin inhibitors neutralise a diversity of venoms from the Neotropical viperid snake genus Bothrops
    Article Snippet: C for 25 min (to keep conditions identical to the drug inhibition assays described below). Plates were then allowed to acclimatise to room temperature for 5 min, before 75 µL of fluorescent substrate (Bio Techne, Cat. no. ES010) at a final 7.5 µM reaction concentration in SVMP assay buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl) was added to each well. Immediately following addition of substrate, the

    HAT Assay:

    Article Title: Repurposed small molecule toxin inhibitors neutralise a diversity of venoms from the Neotropical viperid snake genus Bothrops
    Article Snippet: C for 25 min (to keep conditions identical to the drug inhibition assays described below). Plates were then allowed to acclimatise to room temperature for 5 min, before 75 µL of fluorescent substrate (Bio Techne, Cat. no. ES010) at a final 7.5 µM reaction concentration in SVMP assay buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl) was added to each well. Immediately following addition of substrate, the



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    a) Alexa Fluor 647-labeled AhlyH35A (7.5nM) was incubated with A549 cells in the presence of increasing concentrations of Peptide 88 or a control bicyclic peptide. Cell-associated fluorescence was quantified by flow cytometry and shown as histogram overlays. Negative control (cells only) shown in black; positive control (AhlyH35A without peptide) shown in red. b) Quantification of median fluorescence intensity plotted against peptide concentration. Data are normalized to the negative and positive controls. c) <t>ADAM10</t> protease activation by Ahly (6µM) was measured using a whole-cell FRET peptide cleavage assay in the presence of Peptide 88 or a control bicyclic peptide (900µM). Mean of two biological replicates; error bars indicate standard deviation. Data were analysed using one-way ANOVA with Dunnett’s test: ns = not significant; ** = P < 0.01.
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    a) Alexa Fluor 647-labeled AhlyH35A (7.5nM) was incubated with A549 cells in the presence of increasing concentrations of Peptide 88 or a control bicyclic peptide. Cell-associated fluorescence was quantified by flow cytometry and shown as histogram overlays. Negative control (cells only) shown in black; positive control (AhlyH35A without peptide) shown in red. b) Quantification of median fluorescence intensity plotted against peptide concentration. Data are normalized to the negative and positive controls. c) <t>ADAM10</t> protease activation by Ahly (6µM) was measured using a whole-cell FRET peptide cleavage assay in the presence of Peptide 88 or a control bicyclic peptide (900µM). Mean of two biological replicates; error bars indicate standard deviation. Data were analysed using one-way ANOVA with Dunnett’s test: ns = not significant; ** = P < 0.01.
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    R&D Systems fluorogenic adam10/17 substrate peptide (tace substrate iii
    a) Alexa Fluor 647-labeled AhlyH35A (7.5nM) was incubated with A549 cells in the presence of increasing concentrations of Peptide 88 or a control bicyclic peptide. Cell-associated fluorescence was quantified by flow cytometry and shown as histogram overlays. Negative control (cells only) shown in black; positive control (AhlyH35A without peptide) shown in red. b) Quantification of median fluorescence intensity plotted against peptide concentration. Data are normalized to the negative and positive controls. c) <t>ADAM10</t> protease activation by Ahly (6µM) was measured using a whole-cell FRET peptide cleavage assay in the presence of Peptide 88 or a control bicyclic peptide (900µM). Mean of two biological replicates; error bars indicate standard deviation. Data were analysed using one-way ANOVA with Dunnett’s test: ns = not significant; ** = P < 0.01.
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    a) Alexa Fluor 647-labeled AhlyH35A (7.5nM) was incubated with A549 cells in the presence of increasing concentrations of Peptide 88 or a control bicyclic peptide. Cell-associated fluorescence was quantified by flow cytometry and shown as histogram overlays. Negative control (cells only) shown in black; positive control (AhlyH35A without peptide) shown in red. b) Quantification of median fluorescence intensity plotted against peptide concentration. Data are normalized to the negative and positive controls. c) ADAM10 protease activation by Ahly (6µM) was measured using a whole-cell FRET peptide cleavage assay in the presence of Peptide 88 or a control bicyclic peptide (900µM). Mean of two biological replicates; error bars indicate standard deviation. Data were analysed using one-way ANOVA with Dunnett’s test: ns = not significant; ** = P < 0.01.

    Journal: bioRxiv

    Article Title: Discovery, characterisation and optimisation of bicyclic peptide inhibitors that disarm Staphylococcus aureus α-hemolysin

    doi: 10.64898/2026.03.09.710508

    Figure Lengend Snippet: a) Alexa Fluor 647-labeled AhlyH35A (7.5nM) was incubated with A549 cells in the presence of increasing concentrations of Peptide 88 or a control bicyclic peptide. Cell-associated fluorescence was quantified by flow cytometry and shown as histogram overlays. Negative control (cells only) shown in black; positive control (AhlyH35A without peptide) shown in red. b) Quantification of median fluorescence intensity plotted against peptide concentration. Data are normalized to the negative and positive controls. c) ADAM10 protease activation by Ahly (6µM) was measured using a whole-cell FRET peptide cleavage assay in the presence of Peptide 88 or a control bicyclic peptide (900µM). Mean of two biological replicates; error bars indicate standard deviation. Data were analysed using one-way ANOVA with Dunnett’s test: ns = not significant; ** = P < 0.01.

    Article Snippet: Following incubation, cells were washed once with 25mM Tris buffer, pH 8.0 and a fluorogenic ADAM10 substrate peptide (Mca-PLAQAV-Dpa-RSSSR-NH 2 ; R&D Systems) was added at a final concentration of 10μM.

    Techniques: Labeling, Incubation, Control, Fluorescence, Flow Cytometry, Negative Control, Positive Control, Concentration Assay, Activation Assay, Cleavage Assay, Standard Deviation