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ferrous iron chelating assay kit  (AMS Biotechnology)


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    AMS Biotechnology ferrous iron chelating assay kit
    ( A ) Volcano plot of TPP of YFP-Parkin–expressing HeLa cell lysate treated with 40 μM FB231 compared to equivalent DMSO-treated lysate. Significantly destabilized proteins compared to DMSO, with fold change < −1 and P < 0.05 indicated in blue. Proteins significantly stabilized compared to DMSO, fold-change >1 and P < 0.05 indicated in red. Gene names of significantly altered proteins are labeled. ( B ) Immunoblots of <t>iron-sensitive</t> protein IREB2 in YFP-Parkin–expressing HeLa cells treated with various doses of FB231 or in combination with 10 nM O/A. ( C ) Normalized densitometry analysis of (B), ( N = 3). ( D ) In vitro <t>ferrous</t> ion (Fe 2+ ) chelation <t>assay</t> using colorimetric analysis of ferrozine. EDTA, DFP, and FB231 chelation ability is normalized to the maximum <t>chelating</t> activity observed for EDTA. Points represent means and SD ( N = 3) for individual well measurements, and solid lines represent corresponding fits of the data to a four-parameter Hill equation use to determine the EC 50 . ( E ) mt-Keima–based mitophagy assays for YFP-Parkin HeLa cells treated alone or in combinations of FB231, 10 nM O/A, 25 μM FeSO 4 , and 100 nM O/A for 24 hours ( N = 6). ( F ) mt-Keima–based mitophagy assay of YFP-Parkin/mt-Keima–expressing HeLa cells treated with varying doses of O/A and previously reported mitochondrial toxin DFP for 24 hours. ( G ) Mitophagy induction threshold, the EC 50 of O/A for mitophagy, is calculated for each dose of DFP ( N = 3). All cells were administered with 20 μM Q-VD-OPh to prevent cell death. Data are presented as means ± SD; * P ≤ 0.05, ** P ≤ 0.01, **** P ≤ 0.0001 (one-way ANOVA).
    Ferrous Iron Chelating Assay Kit, supplied by AMS Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/aox-15/pmc12383277-443-5-11?v=AMS+Biotechnology
    Average 96 stars, based on 2 article reviews
    ferrous iron chelating assay kit - by Bioz Stars, 2026-07
    96/100 stars

    Images

    1) Product Images from "Putative PINK1/Parkin activators lower the threshold for mitophagy by sensitizing cells to mitochondrial stress"

    Article Title: Putative PINK1/Parkin activators lower the threshold for mitophagy by sensitizing cells to mitochondrial stress

    Journal: Science Advances

    doi: 10.1126/sciadv.ady0240

    ( A ) Volcano plot of TPP of YFP-Parkin–expressing HeLa cell lysate treated with 40 μM FB231 compared to equivalent DMSO-treated lysate. Significantly destabilized proteins compared to DMSO, with fold change < −1 and P < 0.05 indicated in blue. Proteins significantly stabilized compared to DMSO, fold-change >1 and P < 0.05 indicated in red. Gene names of significantly altered proteins are labeled. ( B ) Immunoblots of iron-sensitive protein IREB2 in YFP-Parkin–expressing HeLa cells treated with various doses of FB231 or in combination with 10 nM O/A. ( C ) Normalized densitometry analysis of (B), ( N = 3). ( D ) In vitro ferrous ion (Fe 2+ ) chelation assay using colorimetric analysis of ferrozine. EDTA, DFP, and FB231 chelation ability is normalized to the maximum chelating activity observed for EDTA. Points represent means and SD ( N = 3) for individual well measurements, and solid lines represent corresponding fits of the data to a four-parameter Hill equation use to determine the EC 50 . ( E ) mt-Keima–based mitophagy assays for YFP-Parkin HeLa cells treated alone or in combinations of FB231, 10 nM O/A, 25 μM FeSO 4 , and 100 nM O/A for 24 hours ( N = 6). ( F ) mt-Keima–based mitophagy assay of YFP-Parkin/mt-Keima–expressing HeLa cells treated with varying doses of O/A and previously reported mitochondrial toxin DFP for 24 hours. ( G ) Mitophagy induction threshold, the EC 50 of O/A for mitophagy, is calculated for each dose of DFP ( N = 3). All cells were administered with 20 μM Q-VD-OPh to prevent cell death. Data are presented as means ± SD; * P ≤ 0.05, ** P ≤ 0.01, **** P ≤ 0.0001 (one-way ANOVA).
    Figure Legend Snippet: ( A ) Volcano plot of TPP of YFP-Parkin–expressing HeLa cell lysate treated with 40 μM FB231 compared to equivalent DMSO-treated lysate. Significantly destabilized proteins compared to DMSO, with fold change < −1 and P < 0.05 indicated in blue. Proteins significantly stabilized compared to DMSO, fold-change >1 and P < 0.05 indicated in red. Gene names of significantly altered proteins are labeled. ( B ) Immunoblots of iron-sensitive protein IREB2 in YFP-Parkin–expressing HeLa cells treated with various doses of FB231 or in combination with 10 nM O/A. ( C ) Normalized densitometry analysis of (B), ( N = 3). ( D ) In vitro ferrous ion (Fe 2+ ) chelation assay using colorimetric analysis of ferrozine. EDTA, DFP, and FB231 chelation ability is normalized to the maximum chelating activity observed for EDTA. Points represent means and SD ( N = 3) for individual well measurements, and solid lines represent corresponding fits of the data to a four-parameter Hill equation use to determine the EC 50 . ( E ) mt-Keima–based mitophagy assays for YFP-Parkin HeLa cells treated alone or in combinations of FB231, 10 nM O/A, 25 μM FeSO 4 , and 100 nM O/A for 24 hours ( N = 6). ( F ) mt-Keima–based mitophagy assay of YFP-Parkin/mt-Keima–expressing HeLa cells treated with varying doses of O/A and previously reported mitochondrial toxin DFP for 24 hours. ( G ) Mitophagy induction threshold, the EC 50 of O/A for mitophagy, is calculated for each dose of DFP ( N = 3). All cells were administered with 20 μM Q-VD-OPh to prevent cell death. Data are presented as means ± SD; * P ≤ 0.05, ** P ≤ 0.01, **** P ≤ 0.0001 (one-way ANOVA).

    Techniques Used: Expressing, Labeling, Western Blot, In Vitro, Activity Assay, Mitophagy Assay



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    ( A ) Volcano plot of TPP of YFP-Parkin–expressing HeLa cell lysate treated with 40 μM FB231 compared to equivalent DMSO-treated lysate. Significantly destabilized proteins compared to DMSO, with fold change < −1 and P < 0.05 indicated in blue. Proteins significantly stabilized compared to DMSO, fold-change >1 and P < 0.05 indicated in red. Gene names of significantly altered proteins are labeled. ( B ) Immunoblots of <t>iron-sensitive</t> protein IREB2 in YFP-Parkin–expressing HeLa cells treated with various doses of FB231 or in combination with 10 nM O/A. ( C ) Normalized densitometry analysis of (B), ( N = 3). ( D ) In vitro <t>ferrous</t> ion (Fe 2+ ) chelation <t>assay</t> using colorimetric analysis of ferrozine. EDTA, DFP, and FB231 chelation ability is normalized to the maximum <t>chelating</t> activity observed for EDTA. Points represent means and SD ( N = 3) for individual well measurements, and solid lines represent corresponding fits of the data to a four-parameter Hill equation use to determine the EC 50 . ( E ) mt-Keima–based mitophagy assays for YFP-Parkin HeLa cells treated alone or in combinations of FB231, 10 nM O/A, 25 μM FeSO 4 , and 100 nM O/A for 24 hours ( N = 6). ( F ) mt-Keima–based mitophagy assay of YFP-Parkin/mt-Keima–expressing HeLa cells treated with varying doses of O/A and previously reported mitochondrial toxin DFP for 24 hours. ( G ) Mitophagy induction threshold, the EC 50 of O/A for mitophagy, is calculated for each dose of DFP ( N = 3). All cells were administered with 20 μM Q-VD-OPh to prevent cell death. Data are presented as means ± SD; * P ≤ 0.05, ** P ≤ 0.01, **** P ≤ 0.0001 (one-way ANOVA).
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    ( A ) Volcano plot of TPP of YFP-Parkin–expressing HeLa cell lysate treated with 40 μM FB231 compared to equivalent DMSO-treated lysate. Significantly destabilized proteins compared to DMSO, with fold change < −1 and P < 0.05 indicated in blue. Proteins significantly stabilized compared to DMSO, fold-change >1 and P < 0.05 indicated in red. Gene names of significantly altered proteins are labeled. ( B ) Immunoblots of <t>iron-sensitive</t> protein IREB2 in YFP-Parkin–expressing HeLa cells treated with various doses of FB231 or in combination with 10 nM O/A. ( C ) Normalized densitometry analysis of (B), ( N = 3). ( D ) In vitro <t>ferrous</t> ion (Fe 2+ ) chelation <t>assay</t> using colorimetric analysis of ferrozine. EDTA, DFP, and FB231 chelation ability is normalized to the maximum <t>chelating</t> activity observed for EDTA. Points represent means and SD ( N = 3) for individual well measurements, and solid lines represent corresponding fits of the data to a four-parameter Hill equation use to determine the EC 50 . ( E ) mt-Keima–based mitophagy assays for YFP-Parkin HeLa cells treated alone or in combinations of FB231, 10 nM O/A, 25 μM FeSO 4 , and 100 nM O/A for 24 hours ( N = 6). ( F ) mt-Keima–based mitophagy assay of YFP-Parkin/mt-Keima–expressing HeLa cells treated with varying doses of O/A and previously reported mitochondrial toxin DFP for 24 hours. ( G ) Mitophagy induction threshold, the EC 50 of O/A for mitophagy, is calculated for each dose of DFP ( N = 3). All cells were administered with 20 μM Q-VD-OPh to prevent cell death. Data are presented as means ± SD; * P ≤ 0.05, ** P ≤ 0.01, **** P ≤ 0.0001 (one-way ANOVA).
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    ( A ) Volcano plot of TPP of YFP-Parkin–expressing HeLa cell lysate treated with 40 μM FB231 compared to equivalent DMSO-treated lysate. Significantly destabilized proteins compared to DMSO, with fold change < −1 and P < 0.05 indicated in blue. Proteins significantly stabilized compared to DMSO, fold-change >1 and P < 0.05 indicated in red. Gene names of significantly altered proteins are labeled. ( B ) Immunoblots of <t>iron-sensitive</t> protein IREB2 in YFP-Parkin–expressing HeLa cells treated with various doses of FB231 or in combination with 10 nM O/A. ( C ) Normalized densitometry analysis of (B), ( N = 3). ( D ) In vitro <t>ferrous</t> ion (Fe 2+ ) chelation <t>assay</t> using colorimetric analysis of ferrozine. EDTA, DFP, and FB231 chelation ability is normalized to the maximum <t>chelating</t> activity observed for EDTA. Points represent means and SD ( N = 3) for individual well measurements, and solid lines represent corresponding fits of the data to a four-parameter Hill equation use to determine the EC 50 . ( E ) mt-Keima–based mitophagy assays for YFP-Parkin HeLa cells treated alone or in combinations of FB231, 10 nM O/A, 25 μM FeSO 4 , and 100 nM O/A for 24 hours ( N = 6). ( F ) mt-Keima–based mitophagy assay of YFP-Parkin/mt-Keima–expressing HeLa cells treated with varying doses of O/A and previously reported mitochondrial toxin DFP for 24 hours. ( G ) Mitophagy induction threshold, the EC 50 of O/A for mitophagy, is calculated for each dose of DFP ( N = 3). All cells were administered with 20 μM Q-VD-OPh to prevent cell death. Data are presented as means ± SD; * P ≤ 0.05, ** P ≤ 0.01, **** P ≤ 0.0001 (one-way ANOVA).
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    ( A ) Volcano plot of TPP of YFP-Parkin–expressing HeLa cell lysate treated with 40 μM FB231 compared to equivalent DMSO-treated lysate. Significantly destabilized proteins compared to DMSO, with fold change < −1 and P < 0.05 indicated in blue. Proteins significantly stabilized compared to DMSO, fold-change >1 and P < 0.05 indicated in red. Gene names of significantly altered proteins are labeled. ( B ) Immunoblots of <t>iron-sensitive</t> protein IREB2 in YFP-Parkin–expressing HeLa cells treated with various doses of FB231 or in combination with 10 nM O/A. ( C ) Normalized densitometry analysis of (B), ( N = 3). ( D ) In vitro <t>ferrous</t> ion (Fe 2+ ) chelation <t>assay</t> using colorimetric analysis of ferrozine. EDTA, DFP, and FB231 chelation ability is normalized to the maximum <t>chelating</t> activity observed for EDTA. Points represent means and SD ( N = 3) for individual well measurements, and solid lines represent corresponding fits of the data to a four-parameter Hill equation use to determine the EC 50 . ( E ) mt-Keima–based mitophagy assays for YFP-Parkin HeLa cells treated alone or in combinations of FB231, 10 nM O/A, 25 μM FeSO 4 , and 100 nM O/A for 24 hours ( N = 6). ( F ) mt-Keima–based mitophagy assay of YFP-Parkin/mt-Keima–expressing HeLa cells treated with varying doses of O/A and previously reported mitochondrial toxin DFP for 24 hours. ( G ) Mitophagy induction threshold, the EC 50 of O/A for mitophagy, is calculated for each dose of DFP ( N = 3). All cells were administered with 20 μM Q-VD-OPh to prevent cell death. Data are presented as means ± SD; * P ≤ 0.05, ** P ≤ 0.01, **** P ≤ 0.0001 (one-way ANOVA).
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    Image Search Results


    ( A ) Volcano plot of TPP of YFP-Parkin–expressing HeLa cell lysate treated with 40 μM FB231 compared to equivalent DMSO-treated lysate. Significantly destabilized proteins compared to DMSO, with fold change < −1 and P < 0.05 indicated in blue. Proteins significantly stabilized compared to DMSO, fold-change >1 and P < 0.05 indicated in red. Gene names of significantly altered proteins are labeled. ( B ) Immunoblots of iron-sensitive protein IREB2 in YFP-Parkin–expressing HeLa cells treated with various doses of FB231 or in combination with 10 nM O/A. ( C ) Normalized densitometry analysis of (B), ( N = 3). ( D ) In vitro ferrous ion (Fe 2+ ) chelation assay using colorimetric analysis of ferrozine. EDTA, DFP, and FB231 chelation ability is normalized to the maximum chelating activity observed for EDTA. Points represent means and SD ( N = 3) for individual well measurements, and solid lines represent corresponding fits of the data to a four-parameter Hill equation use to determine the EC 50 . ( E ) mt-Keima–based mitophagy assays for YFP-Parkin HeLa cells treated alone or in combinations of FB231, 10 nM O/A, 25 μM FeSO 4 , and 100 nM O/A for 24 hours ( N = 6). ( F ) mt-Keima–based mitophagy assay of YFP-Parkin/mt-Keima–expressing HeLa cells treated with varying doses of O/A and previously reported mitochondrial toxin DFP for 24 hours. ( G ) Mitophagy induction threshold, the EC 50 of O/A for mitophagy, is calculated for each dose of DFP ( N = 3). All cells were administered with 20 μM Q-VD-OPh to prevent cell death. Data are presented as means ± SD; * P ≤ 0.05, ** P ≤ 0.01, **** P ≤ 0.0001 (one-way ANOVA).

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    doi: 10.1126/sciadv.ady0240

    Figure Lengend Snippet: ( A ) Volcano plot of TPP of YFP-Parkin–expressing HeLa cell lysate treated with 40 μM FB231 compared to equivalent DMSO-treated lysate. Significantly destabilized proteins compared to DMSO, with fold change < −1 and P < 0.05 indicated in blue. Proteins significantly stabilized compared to DMSO, fold-change >1 and P < 0.05 indicated in red. Gene names of significantly altered proteins are labeled. ( B ) Immunoblots of iron-sensitive protein IREB2 in YFP-Parkin–expressing HeLa cells treated with various doses of FB231 or in combination with 10 nM O/A. ( C ) Normalized densitometry analysis of (B), ( N = 3). ( D ) In vitro ferrous ion (Fe 2+ ) chelation assay using colorimetric analysis of ferrozine. EDTA, DFP, and FB231 chelation ability is normalized to the maximum chelating activity observed for EDTA. Points represent means and SD ( N = 3) for individual well measurements, and solid lines represent corresponding fits of the data to a four-parameter Hill equation use to determine the EC 50 . ( E ) mt-Keima–based mitophagy assays for YFP-Parkin HeLa cells treated alone or in combinations of FB231, 10 nM O/A, 25 μM FeSO 4 , and 100 nM O/A for 24 hours ( N = 6). ( F ) mt-Keima–based mitophagy assay of YFP-Parkin/mt-Keima–expressing HeLa cells treated with varying doses of O/A and previously reported mitochondrial toxin DFP for 24 hours. ( G ) Mitophagy induction threshold, the EC 50 of O/A for mitophagy, is calculated for each dose of DFP ( N = 3). All cells were administered with 20 μM Q-VD-OPh to prevent cell death. Data are presented as means ± SD; * P ≤ 0.05, ** P ≤ 0.01, **** P ≤ 0.0001 (one-way ANOVA).

    Article Snippet: Ferrous iron chelating assays using ferrous iron chelating assay kit (#AOX-15, AMSbio) according to manufacturer’s protocol.

    Techniques: Expressing, Labeling, Western Blot, In Vitro, Activity Assay, Mitophagy Assay