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pronase e  (MedChemExpress)


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    Structured Review

    MedChemExpress pronase e
    DMNQ binds to the SH2 domain of STAT3 and inhibits its phosphorylation A Venn diagram of DMNQ targets screened from the SuperPred database and gastric cancer therapeutic targets (GC 0349530). B Molecular docking results between DMNQ and its potential target STAT3 were obtained via MOE and PyMOL. C Western blot (WB) analysis of tSTAT3 and pSTAT3 levels in gastric cancer cells treated with DMNQ. D Molecular dynamics simulation of the DMNQ-STAT3 complex were performed via Yasara software. E After 48 h of DMNQ treatment, a CETSA assay was conducted; the protein stability of STAT3 was examined via WB at 40–80 °C. F The STAT3 protein was mutated (S611A/E612A/S613A), followed by 48 h of DMNQ treatment. A CETSA assay was then performed, and the protein stability of STAT3 was examined via WB at 40–80 °C. G Cell lysates were incubated with DMNQ at different concentrations and digested with pronase E, and the reaction was terminated by adding the corresponding enzyme inhibitor. The protein level of STAT3 was detected by WB. H After 48 h of DMNQ treatment, the level of pSTAT3 in gastric cancer cells was detected by immunofluorescence. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
    Pronase E, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 24 article reviews
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    Images

    1) Product Images from "DMNQ induces ferroptosis and augments the efficacy of anti-PD-L1 immunotherapy in gastric cancer via the STAT3/SLC1A4 axis to mediate cysteine metabolism reprogramming"

    Article Title: DMNQ induces ferroptosis and augments the efficacy of anti-PD-L1 immunotherapy in gastric cancer via the STAT3/SLC1A4 axis to mediate cysteine metabolism reprogramming

    Journal: Redox Biology

    doi: 10.1016/j.redox.2026.104055

    DMNQ binds to the SH2 domain of STAT3 and inhibits its phosphorylation A Venn diagram of DMNQ targets screened from the SuperPred database and gastric cancer therapeutic targets (GC 0349530). B Molecular docking results between DMNQ and its potential target STAT3 were obtained via MOE and PyMOL. C Western blot (WB) analysis of tSTAT3 and pSTAT3 levels in gastric cancer cells treated with DMNQ. D Molecular dynamics simulation of the DMNQ-STAT3 complex were performed via Yasara software. E After 48 h of DMNQ treatment, a CETSA assay was conducted; the protein stability of STAT3 was examined via WB at 40–80 °C. F The STAT3 protein was mutated (S611A/E612A/S613A), followed by 48 h of DMNQ treatment. A CETSA assay was then performed, and the protein stability of STAT3 was examined via WB at 40–80 °C. G Cell lysates were incubated with DMNQ at different concentrations and digested with pronase E, and the reaction was terminated by adding the corresponding enzyme inhibitor. The protein level of STAT3 was detected by WB. H After 48 h of DMNQ treatment, the level of pSTAT3 in gastric cancer cells was detected by immunofluorescence. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
    Figure Legend Snippet: DMNQ binds to the SH2 domain of STAT3 and inhibits its phosphorylation A Venn diagram of DMNQ targets screened from the SuperPred database and gastric cancer therapeutic targets (GC 0349530). B Molecular docking results between DMNQ and its potential target STAT3 were obtained via MOE and PyMOL. C Western blot (WB) analysis of tSTAT3 and pSTAT3 levels in gastric cancer cells treated with DMNQ. D Molecular dynamics simulation of the DMNQ-STAT3 complex were performed via Yasara software. E After 48 h of DMNQ treatment, a CETSA assay was conducted; the protein stability of STAT3 was examined via WB at 40–80 °C. F The STAT3 protein was mutated (S611A/E612A/S613A), followed by 48 h of DMNQ treatment. A CETSA assay was then performed, and the protein stability of STAT3 was examined via WB at 40–80 °C. G Cell lysates were incubated with DMNQ at different concentrations and digested with pronase E, and the reaction was terminated by adding the corresponding enzyme inhibitor. The protein level of STAT3 was detected by WB. H After 48 h of DMNQ treatment, the level of pSTAT3 in gastric cancer cells was detected by immunofluorescence. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

    Techniques Used: Phospho-proteomics, Biomarker Discovery, Western Blot, Software, Incubation, Immunofluorescence



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    DMNQ binds to the SH2 domain of STAT3 and inhibits its phosphorylation A Venn diagram of DMNQ targets screened from the SuperPred database and gastric cancer therapeutic targets (GC 0349530). B Molecular docking results between DMNQ and its potential target STAT3 were obtained via MOE and PyMOL. C Western blot (WB) analysis of tSTAT3 and pSTAT3 levels in gastric cancer cells treated with DMNQ. D Molecular dynamics simulation of the DMNQ-STAT3 complex were performed via Yasara software. E After 48 h of DMNQ treatment, a CETSA assay was conducted; the protein stability of STAT3 was examined via WB at 40–80 °C. F The STAT3 protein was mutated (S611A/E612A/S613A), followed by 48 h of DMNQ treatment. A CETSA assay was then performed, and the protein stability of STAT3 was examined via WB at 40–80 °C. G Cell lysates were incubated with DMNQ at different concentrations and digested with pronase E, and the reaction was terminated by adding the corresponding enzyme inhibitor. The protein level of STAT3 was detected by WB. H After 48 h of DMNQ treatment, the level of pSTAT3 in gastric cancer cells was detected by immunofluorescence. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
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    DMNQ binds to the SH2 domain of STAT3 and inhibits its phosphorylation A Venn diagram of DMNQ targets screened from the SuperPred database and gastric cancer therapeutic targets (GC 0349530). B Molecular docking results between DMNQ and its potential target STAT3 were obtained via MOE and PyMOL. C Western blot (WB) analysis of tSTAT3 and pSTAT3 levels in gastric cancer cells treated with DMNQ. D Molecular dynamics simulation of the DMNQ-STAT3 complex were performed via Yasara software. E After 48 h of DMNQ treatment, a CETSA assay was conducted; the protein stability of STAT3 was examined via WB at 40–80 °C. F The STAT3 protein was mutated (S611A/E612A/S613A), followed by 48 h of DMNQ treatment. A CETSA assay was then performed, and the protein stability of STAT3 was examined via WB at 40–80 °C. G Cell lysates were incubated with DMNQ at different concentrations and digested with pronase E, and the reaction was terminated by adding the corresponding enzyme inhibitor. The protein level of STAT3 was detected by WB. H After 48 h of DMNQ treatment, the level of pSTAT3 in gastric cancer cells was detected by immunofluorescence. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
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    DMNQ binds to the SH2 domain of STAT3 and inhibits its phosphorylation A Venn diagram of DMNQ targets screened from the SuperPred database and gastric cancer therapeutic targets (GC 0349530). B Molecular docking results between DMNQ and its potential target STAT3 were obtained via MOE and PyMOL. C Western blot (WB) analysis of tSTAT3 and pSTAT3 levels in gastric cancer cells treated with DMNQ. D Molecular dynamics simulation of the DMNQ-STAT3 complex were performed via Yasara software. E After 48 h of DMNQ treatment, a CETSA assay was conducted; the protein stability of STAT3 was examined via WB at 40–80 °C. F The STAT3 protein was mutated (S611A/E612A/S613A), followed by 48 h of DMNQ treatment. A CETSA assay was then performed, and the protein stability of STAT3 was examined via WB at 40–80 °C. G Cell lysates were incubated with DMNQ at different concentrations and digested with pronase E, and the reaction was terminated by adding the corresponding enzyme inhibitor. The protein level of STAT3 was detected by WB. H After 48 h of DMNQ treatment, the level of pSTAT3 in gastric cancer cells was detected by immunofluorescence. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
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    Image Search Results


    DMNQ binds to the SH2 domain of STAT3 and inhibits its phosphorylation A Venn diagram of DMNQ targets screened from the SuperPred database and gastric cancer therapeutic targets (GC 0349530). B Molecular docking results between DMNQ and its potential target STAT3 were obtained via MOE and PyMOL. C Western blot (WB) analysis of tSTAT3 and pSTAT3 levels in gastric cancer cells treated with DMNQ. D Molecular dynamics simulation of the DMNQ-STAT3 complex were performed via Yasara software. E After 48 h of DMNQ treatment, a CETSA assay was conducted; the protein stability of STAT3 was examined via WB at 40–80 °C. F The STAT3 protein was mutated (S611A/E612A/S613A), followed by 48 h of DMNQ treatment. A CETSA assay was then performed, and the protein stability of STAT3 was examined via WB at 40–80 °C. G Cell lysates were incubated with DMNQ at different concentrations and digested with pronase E, and the reaction was terminated by adding the corresponding enzyme inhibitor. The protein level of STAT3 was detected by WB. H After 48 h of DMNQ treatment, the level of pSTAT3 in gastric cancer cells was detected by immunofluorescence. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

    Journal: Redox Biology

    Article Title: DMNQ induces ferroptosis and augments the efficacy of anti-PD-L1 immunotherapy in gastric cancer via the STAT3/SLC1A4 axis to mediate cysteine metabolism reprogramming

    doi: 10.1016/j.redox.2026.104055

    Figure Lengend Snippet: DMNQ binds to the SH2 domain of STAT3 and inhibits its phosphorylation A Venn diagram of DMNQ targets screened from the SuperPred database and gastric cancer therapeutic targets (GC 0349530). B Molecular docking results between DMNQ and its potential target STAT3 were obtained via MOE and PyMOL. C Western blot (WB) analysis of tSTAT3 and pSTAT3 levels in gastric cancer cells treated with DMNQ. D Molecular dynamics simulation of the DMNQ-STAT3 complex were performed via Yasara software. E After 48 h of DMNQ treatment, a CETSA assay was conducted; the protein stability of STAT3 was examined via WB at 40–80 °C. F The STAT3 protein was mutated (S611A/E612A/S613A), followed by 48 h of DMNQ treatment. A CETSA assay was then performed, and the protein stability of STAT3 was examined via WB at 40–80 °C. G Cell lysates were incubated with DMNQ at different concentrations and digested with pronase E, and the reaction was terminated by adding the corresponding enzyme inhibitor. The protein level of STAT3 was detected by WB. H After 48 h of DMNQ treatment, the level of pSTAT3 in gastric cancer cells was detected by immunofluorescence. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

    Article Snippet: The cell lysates were then aliquoted into separate tubes and incubated with various concentrations of DMNQ (MKN-45: 0, 20, 40, 60, 80 μM; MFC: 0, 6, 12, 18, 24 μM) at 37 °C for 1 h. Following DMNQ treatment, the samples were hydrolyzed with pronase E (MKN-45: 20 μg/mL; MFC: 10 μg/mL, MCE; Shanghai, China) at 37 °C for 20 min.

    Techniques: Phospho-proteomics, Biomarker Discovery, Western Blot, Software, Incubation, Immunofluorescence