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mmp fluorogenic peptide substrate  (R&D Systems)


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    R&D Systems mmp fluorogenic peptide substrate
    Figure 1 | Fluid flow stimulates motility and matrix metalloprotease activity. (a) Cylindrical PDMS fluidics channels coated in collagen support a monolayer of cells. Flow of media through the culture chamber exposes cells to WSS of 0.05 dyne cm 2. Scale bar on bright field photomicrograph of PC3 cells within the scaffold represents 400 mm. (b) Filopodia formation in response to WSS is extensive. Scale bar in left panel, 10 mm, scale bar in right panel, 5 mm. (c) Transcription of MMP2 and MMP9 is stimulated by WSS (n ¼ 3 independent experiments; Kruskal–Wallis one-way ANOVA, Po0.001). (d) Total <t>MMP</t> activity measured by fluorogenic peptide substrate digestion assays was increased by exposure to 6 h WSS (n ¼ 3 independent experiments; unpaired t-test, **Po0.0001). (e) Spatial tracking of PC3 and DU145 cancer cell movement during 6 h of time-lapse imaging, where each cell lies at the origin (0,0) at t ¼ 0 h. Plots depict motility of individual cells in one representative experiment. (f) Quantification of migration speed reveals increased cellular velocities of individual cells under WSS. (n ¼ 7 independent experiments, two-tailed t-test, **P ¼ 4.22E 18 for PC3 cells; n ¼ 3 independent experiments, two-tailed t-test, **P ¼ 1.56E 9 for DU145 cells). (g) Time segmented migration speed of cells after WSS initiation (Kruskal–Wallis one-way ANOVA, *Po0.05, **Po0.01). Error bars represent±s.e.m.
    Mmp Fluorogenic Peptide Substrate, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 81 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/fluorogenic+substrate/pm28098159-293-1-6?v=R%26D+Systems
    Average 93 stars, based on 81 article reviews
    mmp fluorogenic peptide substrate - by Bioz Stars, 2026-07
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    Images

    1) Product Images from "Fluid shear stress activates YAP1 to promote cancer cell motility."

    Article Title: Fluid shear stress activates YAP1 to promote cancer cell motility.

    Journal: Nature communications

    doi: 10.1038/ncomms14122

    Figure 1 | Fluid flow stimulates motility and matrix metalloprotease activity. (a) Cylindrical PDMS fluidics channels coated in collagen support a monolayer of cells. Flow of media through the culture chamber exposes cells to WSS of 0.05 dyne cm 2. Scale bar on bright field photomicrograph of PC3 cells within the scaffold represents 400 mm. (b) Filopodia formation in response to WSS is extensive. Scale bar in left panel, 10 mm, scale bar in right panel, 5 mm. (c) Transcription of MMP2 and MMP9 is stimulated by WSS (n ¼ 3 independent experiments; Kruskal–Wallis one-way ANOVA, Po0.001). (d) Total MMP activity measured by fluorogenic peptide substrate digestion assays was increased by exposure to 6 h WSS (n ¼ 3 independent experiments; unpaired t-test, **Po0.0001). (e) Spatial tracking of PC3 and DU145 cancer cell movement during 6 h of time-lapse imaging, where each cell lies at the origin (0,0) at t ¼ 0 h. Plots depict motility of individual cells in one representative experiment. (f) Quantification of migration speed reveals increased cellular velocities of individual cells under WSS. (n ¼ 7 independent experiments, two-tailed t-test, **P ¼ 4.22E 18 for PC3 cells; n ¼ 3 independent experiments, two-tailed t-test, **P ¼ 1.56E 9 for DU145 cells). (g) Time segmented migration speed of cells after WSS initiation (Kruskal–Wallis one-way ANOVA, *Po0.05, **Po0.01). Error bars represent±s.e.m.
    Figure Legend Snippet: Figure 1 | Fluid flow stimulates motility and matrix metalloprotease activity. (a) Cylindrical PDMS fluidics channels coated in collagen support a monolayer of cells. Flow of media through the culture chamber exposes cells to WSS of 0.05 dyne cm 2. Scale bar on bright field photomicrograph of PC3 cells within the scaffold represents 400 mm. (b) Filopodia formation in response to WSS is extensive. Scale bar in left panel, 10 mm, scale bar in right panel, 5 mm. (c) Transcription of MMP2 and MMP9 is stimulated by WSS (n ¼ 3 independent experiments; Kruskal–Wallis one-way ANOVA, Po0.001). (d) Total MMP activity measured by fluorogenic peptide substrate digestion assays was increased by exposure to 6 h WSS (n ¼ 3 independent experiments; unpaired t-test, **Po0.0001). (e) Spatial tracking of PC3 and DU145 cancer cell movement during 6 h of time-lapse imaging, where each cell lies at the origin (0,0) at t ¼ 0 h. Plots depict motility of individual cells in one representative experiment. (f) Quantification of migration speed reveals increased cellular velocities of individual cells under WSS. (n ¼ 7 independent experiments, two-tailed t-test, **P ¼ 4.22E 18 for PC3 cells; n ¼ 3 independent experiments, two-tailed t-test, **P ¼ 1.56E 9 for DU145 cells). (g) Time segmented migration speed of cells after WSS initiation (Kruskal–Wallis one-way ANOVA, *Po0.05, **Po0.01). Error bars represent±s.e.m.

    Techniques Used: Activity Assay, Imaging, Migration, Two Tailed Test



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    (A). RT-PCR analysis of SEP 53BP1 mRNA expression in the transduced cell lines. The starting material was total cell RNA (quantities are indicated above the panel). (B). A SEP 53BP1 immunoblot prepared from THP-1 transduced cells. A size marker is provided by the SEP 53BP1 synthetic peptide. (C). Immunoblots performed on HeLa, THP1 and macrophages (phorbol 12-myristate 13-acetate (PA) differentiated THP-1 cells) for specific proteasome (β5), immunoproteasome (β5i) and shared markers (20S. 19S. α4). (D). Assays were performed on cell extracts from HeLa and THP-1 cells using the immunoproteasome substrate Ac-Ala-Asn-Trp-AMC (AdipoGen) plus or minus the specific immunoproteasome inhibitor ONX 0914 (AdipoGen). Each time point was monitored in triplicate and plotted graphically as the mean plus the SD. (E). An immunoblot monitoring immunoproteasome induction in HeLa cells lines treated with interferon gamma (IFNγ) or bacterial lipopolysaccharide (LPS) as determined by the expression of β5i (also called LMP7). (F). Immunoproteasome assays performed on the indicated cell lines. (C). This is the same data as presented in panel (B) excluding the THP-1 cell line.

    Journal: bioRxiv

    Article Title: The microprotein SEP 53BP1 : its bizarre mode of translational expression and intracellular behaviour

    doi: 10.64898/2026.05.04.722586

    Figure Lengend Snippet: (A). RT-PCR analysis of SEP 53BP1 mRNA expression in the transduced cell lines. The starting material was total cell RNA (quantities are indicated above the panel). (B). A SEP 53BP1 immunoblot prepared from THP-1 transduced cells. A size marker is provided by the SEP 53BP1 synthetic peptide. (C). Immunoblots performed on HeLa, THP1 and macrophages (phorbol 12-myristate 13-acetate (PA) differentiated THP-1 cells) for specific proteasome (β5), immunoproteasome (β5i) and shared markers (20S. 19S. α4). (D). Assays were performed on cell extracts from HeLa and THP-1 cells using the immunoproteasome substrate Ac-Ala-Asn-Trp-AMC (AdipoGen) plus or minus the specific immunoproteasome inhibitor ONX 0914 (AdipoGen). Each time point was monitored in triplicate and plotted graphically as the mean plus the SD. (E). An immunoblot monitoring immunoproteasome induction in HeLa cells lines treated with interferon gamma (IFNγ) or bacterial lipopolysaccharide (LPS) as determined by the expression of β5i (also called LMP7). (F). Immunoproteasome assays performed on the indicated cell lines. (C). This is the same data as presented in panel (B) excluding the THP-1 cell line.

    Article Snippet: The immunoproteasome assay was performed in identical buffer conditions but with the fluorogenic peptidyl substrate Ac-Ala-Asn-Trp-AMC (final concentration 10 μM) (AdipoGen) and the specific inhibitor ONX 0914 (10 μM) (AdipoGen) ( , , ).

    Techniques: Reverse Transcription Polymerase Chain Reaction, Expressing, Western Blot, Marker

    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.

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    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