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3 methyladenine 3 ma  (MedChemExpress)


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    Structured Review

    MedChemExpress 3 methyladenine 3 ma
    NCOA1 is a host factor targeted by compound 10 to regulate lipid metabolic programs (A) Validation of DARTS assay by western blot in Huh-7 cell lysates. Compd. 10 (50 μM) treatment increases the protease resistance of NCOA1 protein. (B and C) CETSA analysis reveals that compd. 10 (50 μM) induced thermal stabilization of NCOA1 is abolished by D276A and R281A mutations. Experiments were performed in HEK293T cells. (D and E) Western blot analysis shows a dose-dependent reduction of NCOA1 protein levels by compd. 10 . Data were analyzed by one-way ANOVA followed by Dunnett’s test (∗∗ p < 0.01). (F and G) CHX chase assay demonstrates accelerated degradation of NCOA1 in the presence of compd. 10 (8 μM). Student’s t test was used for statistical analysis (∗ p < 0.05, ∗∗ p < 0.01). (H and I) CHX chase analysis shows reduced stability of PPARγ protein upon compd. 10 (8 μM) treatment. Student’s t test was used for statistical analysis (∗∗ p < 0.01). (J and K) Western blot analysis shows that autophagy-lysosome inhibitors <t>(3-MA,</t> BafA1), but not the proteasome inhibitor MG132, rescue NCOA1 protein levels reduced by compd. 10 (8 μM), indicating lysosome-dependent degradation. Data were analyzed by two-way ANOVA followed by Šídák’s test (∗∗ p < 0.01, ∗∗∗ p < 0.001). Data are presented as mean ± SD from at least three independent experiments.
    3 Methyladenine 3 Ma, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 99/100, based on 1643 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ma/3-Methyladenine/pmc13475704-34-0-3
    Average 99 stars, based on 1643 article reviews
    3 methyladenine 3 ma - by Bioz Stars, 2026-10
    99/100 stars

    Images

    1) Product Images from "Targeting host lipogenesis with a diarylamide inhibitor disrupts SARS-CoV-2 replication"

    Article Title: Targeting host lipogenesis with a diarylamide inhibitor disrupts SARS-CoV-2 replication

    Journal: iScience

    doi: 10.1016/j.isci.2026.117111

    NCOA1 is a host factor targeted by compound 10 to regulate lipid metabolic programs (A) Validation of DARTS assay by western blot in Huh-7 cell lysates. Compd. 10 (50 μM) treatment increases the protease resistance of NCOA1 protein. (B and C) CETSA analysis reveals that compd. 10 (50 μM) induced thermal stabilization of NCOA1 is abolished by D276A and R281A mutations. Experiments were performed in HEK293T cells. (D and E) Western blot analysis shows a dose-dependent reduction of NCOA1 protein levels by compd. 10 . Data were analyzed by one-way ANOVA followed by Dunnett’s test (∗∗ p < 0.01). (F and G) CHX chase assay demonstrates accelerated degradation of NCOA1 in the presence of compd. 10 (8 μM). Student’s t test was used for statistical analysis (∗ p < 0.05, ∗∗ p < 0.01). (H and I) CHX chase analysis shows reduced stability of PPARγ protein upon compd. 10 (8 μM) treatment. Student’s t test was used for statistical analysis (∗∗ p < 0.01). (J and K) Western blot analysis shows that autophagy-lysosome inhibitors (3-MA, BafA1), but not the proteasome inhibitor MG132, rescue NCOA1 protein levels reduced by compd. 10 (8 μM), indicating lysosome-dependent degradation. Data were analyzed by two-way ANOVA followed by Šídák’s test (∗∗ p < 0.01, ∗∗∗ p < 0.001). Data are presented as mean ± SD from at least three independent experiments.
    Figure Legend Snippet: NCOA1 is a host factor targeted by compound 10 to regulate lipid metabolic programs (A) Validation of DARTS assay by western blot in Huh-7 cell lysates. Compd. 10 (50 μM) treatment increases the protease resistance of NCOA1 protein. (B and C) CETSA analysis reveals that compd. 10 (50 μM) induced thermal stabilization of NCOA1 is abolished by D276A and R281A mutations. Experiments were performed in HEK293T cells. (D and E) Western blot analysis shows a dose-dependent reduction of NCOA1 protein levels by compd. 10 . Data were analyzed by one-way ANOVA followed by Dunnett’s test (∗∗ p < 0.01). (F and G) CHX chase assay demonstrates accelerated degradation of NCOA1 in the presence of compd. 10 (8 μM). Student’s t test was used for statistical analysis (∗ p < 0.05, ∗∗ p < 0.01). (H and I) CHX chase analysis shows reduced stability of PPARγ protein upon compd. 10 (8 μM) treatment. Student’s t test was used for statistical analysis (∗∗ p < 0.01). (J and K) Western blot analysis shows that autophagy-lysosome inhibitors (3-MA, BafA1), but not the proteasome inhibitor MG132, rescue NCOA1 protein levels reduced by compd. 10 (8 μM), indicating lysosome-dependent degradation. Data were analyzed by two-way ANOVA followed by Šídák’s test (∗∗ p < 0.01, ∗∗∗ p < 0.001). Data are presented as mean ± SD from at least three independent experiments.

    Techniques Used: Biomarker Discovery, Western Blot

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    NCOA1 is a host factor targeted by compound 10 to regulate lipid metabolic programs (A) Validation of DARTS assay by western blot in Huh-7 cell lysates. Compd. 10 (50 μM) treatment increases the protease resistance of NCOA1 protein. (B and C) CETSA analysis reveals that compd. 10 (50 μM) induced thermal stabilization of NCOA1 is abolished by D276A and R281A mutations. Experiments were performed in HEK293T cells. (D and E) Western blot analysis shows a dose-dependent reduction of NCOA1 protein levels by compd. 10 . Data were analyzed by one-way ANOVA followed by Dunnett’s test (∗∗ p < 0.01). (F and G) CHX chase assay demonstrates accelerated degradation of NCOA1 in the presence of compd. 10 (8 μM). Student’s t test was used for statistical analysis (∗ p < 0.05, ∗∗ p < 0.01). (H and I) CHX chase analysis shows reduced stability of PPARγ protein upon compd. 10 (8 μM) treatment. Student’s t test was used for statistical analysis (∗∗ p < 0.01). (J and K) Western blot analysis shows that autophagy-lysosome inhibitors <t>(3-MA,</t> BafA1), but not the proteasome inhibitor MG132, rescue NCOA1 protein levels reduced by compd. 10 (8 μM), indicating lysosome-dependent degradation. Data were analyzed by two-way ANOVA followed by Šídák’s test (∗∗ p < 0.01, ∗∗∗ p < 0.001). Data are presented as mean ± SD from at least three independent experiments.
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    NCOA1 is a host factor targeted by compound 10 to regulate lipid metabolic programs (A) Validation of DARTS assay by western blot in Huh-7 cell lysates. Compd. 10 (50 μM) treatment increases the protease resistance of NCOA1 protein. (B and C) CETSA analysis reveals that compd. 10 (50 μM) induced thermal stabilization of NCOA1 is abolished by D276A and R281A mutations. Experiments were performed in HEK293T cells. (D and E) Western blot analysis shows a dose-dependent reduction of NCOA1 protein levels by compd. 10 . Data were analyzed by one-way ANOVA followed by Dunnett’s test (∗∗ p < 0.01). (F and G) CHX chase assay demonstrates accelerated degradation of NCOA1 in the presence of compd. 10 (8 μM). Student’s t test was used for statistical analysis (∗ p < 0.05, ∗∗ p < 0.01). (H and I) CHX chase analysis shows reduced stability of PPARγ protein upon compd. 10 (8 μM) treatment. Student’s t test was used for statistical analysis (∗∗ p < 0.01). (J and K) Western blot analysis shows that autophagy-lysosome inhibitors <t>(3-MA,</t> BafA1), but not the proteasome inhibitor MG132, rescue NCOA1 protein levels reduced by compd. 10 (8 μM), indicating lysosome-dependent degradation. Data were analyzed by two-way ANOVA followed by Šídák’s test (∗∗ p < 0.01, ∗∗∗ p < 0.001). Data are presented as mean ± SD from at least three independent experiments.
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    NCOA1 is a host factor targeted by compound 10 to regulate lipid metabolic programs (A) Validation of DARTS assay by western blot in Huh-7 cell lysates. Compd. 10 (50 μM) treatment increases the protease resistance of NCOA1 protein. (B and C) CETSA analysis reveals that compd. 10 (50 μM) induced thermal stabilization of NCOA1 is abolished by D276A and R281A mutations. Experiments were performed in HEK293T cells. (D and E) Western blot analysis shows a dose-dependent reduction of NCOA1 protein levels by compd. 10 . Data were analyzed by one-way ANOVA followed by Dunnett’s test (∗∗ p < 0.01). (F and G) CHX chase assay demonstrates accelerated degradation of NCOA1 in the presence of compd. 10 (8 μM). Student’s t test was used for statistical analysis (∗ p < 0.05, ∗∗ p < 0.01). (H and I) CHX chase analysis shows reduced stability of PPARγ protein upon compd. 10 (8 μM) treatment. Student’s t test was used for statistical analysis (∗∗ p < 0.01). (J and K) Western blot analysis shows that autophagy-lysosome inhibitors <t>(3-MA,</t> BafA1), but not the proteasome inhibitor MG132, rescue NCOA1 protein levels reduced by compd. 10 (8 μM), indicating lysosome-dependent degradation. Data were analyzed by two-way ANOVA followed by Šídák’s test (∗∗ p < 0.01, ∗∗∗ p < 0.001). Data are presented as mean ± SD from at least three independent experiments.
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    NCOA1 is a host factor targeted by compound 10 to regulate lipid metabolic programs (A) Validation of DARTS assay by western blot in Huh-7 cell lysates. Compd. 10 (50 μM) treatment increases the protease resistance of NCOA1 protein. (B and C) CETSA analysis reveals that compd. 10 (50 μM) induced thermal stabilization of NCOA1 is abolished by D276A and R281A mutations. Experiments were performed in HEK293T cells. (D and E) Western blot analysis shows a dose-dependent reduction of NCOA1 protein levels by compd. 10 . Data were analyzed by one-way ANOVA followed by Dunnett’s test (∗∗ p < 0.01). (F and G) CHX chase assay demonstrates accelerated degradation of NCOA1 in the presence of compd. 10 (8 μM). Student’s t test was used for statistical analysis (∗ p < 0.05, ∗∗ p < 0.01). (H and I) CHX chase analysis shows reduced stability of PPARγ protein upon compd. 10 (8 μM) treatment. Student’s t test was used for statistical analysis (∗∗ p < 0.01). (J and K) Western blot analysis shows that autophagy-lysosome inhibitors <t>(3-MA,</t> BafA1), but not the proteasome inhibitor MG132, rescue NCOA1 protein levels reduced by compd. 10 (8 μM), indicating lysosome-dependent degradation. Data were analyzed by two-way ANOVA followed by Šídák’s test (∗∗ p < 0.01, ∗∗∗ p < 0.001). Data are presented as mean ± SD from at least three independent experiments.
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    NCOA1 is a host factor targeted by compound 10 to regulate lipid metabolic programs (A) Validation of DARTS assay by western blot in Huh-7 cell lysates. Compd. 10 (50 μM) treatment increases the protease resistance of NCOA1 protein. (B and C) CETSA analysis reveals that compd. 10 (50 μM) induced thermal stabilization of NCOA1 is abolished by D276A and R281A mutations. Experiments were performed in HEK293T cells. (D and E) Western blot analysis shows a dose-dependent reduction of NCOA1 protein levels by compd. 10 . Data were analyzed by one-way ANOVA followed by Dunnett’s test (∗∗ p < 0.01). (F and G) CHX chase assay demonstrates accelerated degradation of NCOA1 in the presence of compd. 10 (8 μM). Student’s t test was used for statistical analysis (∗ p < 0.05, ∗∗ p < 0.01). (H and I) CHX chase analysis shows reduced stability of PPARγ protein upon compd. 10 (8 μM) treatment. Student’s t test was used for statistical analysis (∗∗ p < 0.01). (J and K) Western blot analysis shows that autophagy-lysosome inhibitors <t>(3-MA,</t> BafA1), but not the proteasome inhibitor MG132, rescue NCOA1 protein levels reduced by compd. 10 (8 μM), indicating lysosome-dependent degradation. Data were analyzed by two-way ANOVA followed by Šídák’s test (∗∗ p < 0.01, ∗∗∗ p < 0.001). Data are presented as mean ± SD from at least three independent experiments.
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    NCOA1 is a host factor targeted by compound 10 to regulate lipid metabolic programs (A) Validation of DARTS assay by western blot in Huh-7 cell lysates. Compd. 10 (50 μM) treatment increases the protease resistance of NCOA1 protein. (B and C) CETSA analysis reveals that compd. 10 (50 μM) induced thermal stabilization of NCOA1 is abolished by D276A and R281A mutations. Experiments were performed in HEK293T cells. (D and E) Western blot analysis shows a dose-dependent reduction of NCOA1 protein levels by compd. 10 . Data were analyzed by one-way ANOVA followed by Dunnett’s test (∗∗ p < 0.01). (F and G) CHX chase assay demonstrates accelerated degradation of NCOA1 in the presence of compd. 10 (8 μM). Student’s t test was used for statistical analysis (∗ p < 0.05, ∗∗ p < 0.01). (H and I) CHX chase analysis shows reduced stability of PPARγ protein upon compd. 10 (8 μM) treatment. Student’s t test was used for statistical analysis (∗∗ p < 0.01). (J and K) Western blot analysis shows that autophagy-lysosome inhibitors (3-MA, BafA1), but not the proteasome inhibitor MG132, rescue NCOA1 protein levels reduced by compd. 10 (8 μM), indicating lysosome-dependent degradation. Data were analyzed by two-way ANOVA followed by Šídák’s test (∗∗ p < 0.01, ∗∗∗ p < 0.001). Data are presented as mean ± SD from at least three independent experiments.

    Journal: iScience

    Article Title: Targeting host lipogenesis with a diarylamide inhibitor disrupts SARS-CoV-2 replication

    doi: 10.1016/j.isci.2026.117111

    Figure Lengend Snippet: NCOA1 is a host factor targeted by compound 10 to regulate lipid metabolic programs (A) Validation of DARTS assay by western blot in Huh-7 cell lysates. Compd. 10 (50 μM) treatment increases the protease resistance of NCOA1 protein. (B and C) CETSA analysis reveals that compd. 10 (50 μM) induced thermal stabilization of NCOA1 is abolished by D276A and R281A mutations. Experiments were performed in HEK293T cells. (D and E) Western blot analysis shows a dose-dependent reduction of NCOA1 protein levels by compd. 10 . Data were analyzed by one-way ANOVA followed by Dunnett’s test (∗∗ p < 0.01). (F and G) CHX chase assay demonstrates accelerated degradation of NCOA1 in the presence of compd. 10 (8 μM). Student’s t test was used for statistical analysis (∗ p < 0.05, ∗∗ p < 0.01). (H and I) CHX chase analysis shows reduced stability of PPARγ protein upon compd. 10 (8 μM) treatment. Student’s t test was used for statistical analysis (∗∗ p < 0.01). (J and K) Western blot analysis shows that autophagy-lysosome inhibitors (3-MA, BafA1), but not the proteasome inhibitor MG132, rescue NCOA1 protein levels reduced by compd. 10 (8 μM), indicating lysosome-dependent degradation. Data were analyzed by two-way ANOVA followed by Šídák’s test (∗∗ p < 0.01, ∗∗∗ p < 0.001). Data are presented as mean ± SD from at least three independent experiments.

    Article Snippet: 3-methyladenine (3-MA) , MCE , Cat# HY-19312.

    Techniques: Biomarker Discovery, Western Blot