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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: 99/100, based on 75 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/adam10+fluorogenic+substrate/Mca-KPLGL-Dpa-AR-NH2+Fluorogenic+Peptide+Substrate/pm34324289-92-4-9
    Average 99 stars, based on 75 article reviews
    adam10 substrate - by Bioz Stars, 2026-09
    99/100 stars

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    Related Articles

    Injection:

    Article Title: Biochemical characterisation and substrate-specific proteolytic diversity of venom metalloproteinases in African puff adders
    Article Snippet: sing C18 ZipTips and manually injected into an ESI-Orbitrap mass spectrometer (see 2.3.6.1 for details). This assay, which kinetically measures the cleavage of a quenched fluorogenic substrate (ES010, R&D Biosystems) by metalloproteases was performed as previously described ( Albulescu et al., 2020 ). Reactions were set up in a 384-well plate (Greiner) and consisted of 15 μL of pure SVMP PI isoform

    Mass Spectrometry:

    Article Title: Biochemical characterisation and substrate-specific proteolytic diversity of venom metalloproteinases in African puff adders
    Article Snippet: sing C18 ZipTips and manually injected into an ESI-Orbitrap mass spectrometer (see 2.3.6.1 for details). This assay, which kinetically measures the cleavage of a quenched fluorogenic substrate (ES010, R&D Biosystems) by metalloproteases was performed as previously described ( Albulescu et al., 2020 ). Reactions were set up in a 384-well plate (Greiner) and consisted of 15 μL of pure SVMP PI isoform

    Incubation:

    Article Title: Biochemical characterisation and substrate-specific proteolytic diversity of venom metalloproteinases in African puff adders
    Article Snippet: sing C18 ZipTips and manually injected into an ESI-Orbitrap mass spectrometer (see 2.3.6.1 for details). This assay, which kinetically measures the cleavage of a quenched fluorogenic substrate (ES010, R&D Biosystems) by metalloproteases was performed as previously described ( Albulescu et al., 2020 ). Reactions were set up in a 384-well plate (Greiner) and consisted of 15 μL of pure SVMP PI isoform

    Concentration Assay:

    Article Title: Biochemical characterisation and substrate-specific proteolytic diversity of venom metalloproteinases in African puff adders
    Article Snippet: sing C18 ZipTips and manually injected into an ESI-Orbitrap mass spectrometer (see 2.3.6.1 for details). This assay, which kinetically measures the cleavage of a quenched fluorogenic substrate (ES010, R&D Biosystems) by metalloproteases was performed as previously described ( Albulescu et al., 2020 ). Reactions were set up in a 384-well plate (Greiner) and consisted of 15 μL of pure SVMP PI isoform

    Proximity Ligation Assay:

    Article Title: Biochemical characterisation and substrate-specific proteolytic diversity of venom metalloproteinases in African puff adders
    Article Snippet: sing C18 ZipTips and manually injected into an ESI-Orbitrap mass spectrometer (see 2.3.6.1 for details). This assay, which kinetically measures the cleavage of a quenched fluorogenic substrate (ES010, R&D Biosystems) by metalloproteases was performed as previously described ( Albulescu et al., 2020 ). Reactions were set up in a 384-well plate (Greiner) and consisted of 15 μL of pure SVMP PI isoform

    In Vitro:

    Article Title: Biochemical characterisation and substrate-specific proteolytic diversity of venom metalloproteinases in African puff adders
    Article Snippet: sing C18 ZipTips and manually injected into an ESI-Orbitrap mass spectrometer (see 2.3.6.1 for details). This assay, which kinetically measures the cleavage of a quenched fluorogenic substrate (ES010, R&D Biosystems) by metalloproteases was performed as previously described ( Albulescu et al., 2020 ). Reactions were set up in a 384-well plate (Greiner) and consisted of 15 μL of pure SVMP PI isoform

    Activity Assay:

    Article Title: Biochemical characterisation and substrate-specific proteolytic diversity of venom metalloproteinases in African puff adders
    Article Snippet: sing C18 ZipTips and manually injected into an ESI-Orbitrap mass spectrometer (see 2.3.6.1 for details). This assay, which kinetically measures the cleavage of a quenched fluorogenic substrate (ES010, R&D Biosystems) by metalloproteases was performed as previously described ( Albulescu et al., 2020 ). Reactions were set up in a 384-well plate (Greiner) and consisted of 15 μL of pure SVMP PI isoform

    Inhibition:

    Article Title: Biochemical characterisation and substrate-specific proteolytic diversity of venom metalloproteinases in African puff adders
    Article Snippet: sing C18 ZipTips and manually injected into an ESI-Orbitrap mass spectrometer (see 2.3.6.1 for details). This assay, which kinetically measures the cleavage of a quenched fluorogenic substrate (ES010, R&D Biosystems) by metalloproteases was performed as previously described ( Albulescu et al., 2020 ). Reactions were set up in a 384-well plate (Greiner) and consisted of 15 μL of pure SVMP PI isoform

    HAT Assay:

    Article Title: Biochemical characterisation and substrate-specific proteolytic diversity of venom metalloproteinases in African puff adders
    Article Snippet: sing C18 ZipTips and manually injected into an ESI-Orbitrap mass spectrometer (see 2.3.6.1 for details). This assay, which kinetically measures the cleavage of a quenched fluorogenic substrate (ES010, R&D Biosystems) by metalloproteases was performed as previously described ( Albulescu et al., 2020 ). Reactions were set up in a 384-well plate (Greiner) and consisted of 15 μL of pure SVMP PI isoform

    Fluorescence:

    Article Title: Biochemical characterisation and substrate-specific proteolytic diversity of venom metalloproteinases in African puff adders
    Article Snippet: sing C18 ZipTips and manually injected into an ESI-Orbitrap mass spectrometer (see 2.3.6.1 for details). This assay, which kinetically measures the cleavage of a quenched fluorogenic substrate (ES010, R&D Biosystems) by metalloproteases was performed as previously described ( Albulescu et al., 2020 ). Reactions were set up in a 384-well plate (Greiner) and consisted of 15 μL of pure SVMP PI isoform



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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) 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