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adam10  (BPS Bioscience)


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    Structured Review

    BPS Bioscience adam10
    Adam10, supplied by BPS Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/fluorogenic+adam10/ADAM10+Fluorogenic+Assay+Kit/pm41337883-160-0-18
    Average 94 stars, based on 3 article reviews
    adam10 - by Bioz Stars, 2026-10
    94/100 stars

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    Related Articles

    Activity Assay:

    Article Title: Reduced efficacy of an anti-toxin vaccine from senescence-driven attenuation of toxin virulence
    Article Snippet: Primer (Integrated DNA Technologies) sequences of ADAM10 and housekeeping genes are as follows: For mouse ADAM10 Forward ADAM10: 5’-TCATGGTGAAACGCATAAGAATCA-3’ Reverse ADAM10: 5’-CCAGACCAAGTACGCCATCA-3’ Ms 18s Forward: 5’-GCCGCTAGAGGTGAAATTCTT-3’ Ms 18s Reverse: 5’-CGTCTTCGAACCTCCGACT-3’ For human ADAM10 ADAM10_F Sequence: 5’-CTGGCCAACCTATTTGTGGAA-3’ ADAM10_R Sequence: 5’-GACCTTGACTTGGACTGCACTG-3’ GAPDH_ F Sequence: 5’-GAAGGGCTCATGACCACAGTCCAT-3’ GAPDH_R Sequence: 5’-TCATTGTCGTACCAGGAAATGAGCTT-3’ .. ADAM10 enzymatic activity was measured using the ADAM10 Fluorogenic Assay Kit (BPS Biosciences). .. Neutrophil lysates were prepared by lysing cells in RIPA lysis buffer (Millipore Sigma) with cOmplete protease inhibitor cocktail (Sigma) on ice for 20 minutes, followed by a high-speed centrifugation at 14,500×g for 10 minutes at 4°C.

    Comparison:

    Article Title: DeFrND: detergent-free reconstitution into native nanodiscs with designer membrane scaffold peptides
    Article Snippet: The orientation of ADAM10 in reconstituted vesicles was assayed by Trypsin digestion in the absence or presence of Triton X-100 (1%) for 1 h on ice, followed by SDS-PAGE and western blot using the anti-ADAM10 antibody (1/1000 dilution) from Abcam (ab124695). .. Activities of ADAM10 in DeFrNDs or vesicles formed by detergent-mediated reconstitution were determined using an ADAM10 assay kit (BPS Bioscience) in comparison with crude membranes. ..



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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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    Average 94 stars, based on 1 article reviews
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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