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sod2  (Proteintech)


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    Structured Review

    Proteintech sod2
    Sod2, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 2079 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/anti+sod2+antibodies/LC3+Antibody/pm41906653-153-55-65
    Average 96 stars, based on 2079 article reviews
    sod2 - by Bioz Stars, 2026-10
    96/100 stars

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    Related Articles

    Incubation:

    Article Title: Intraperitoneal Triamcinolone Reduces Postoperative Adhesions, Possibly through Alteration of Mitochondrial Function
    Article Snippet: Unless specified otherwise, primary antibodies were used at a concentration of 1:500 and secondary antibodies at a concentration of 1:5000.Unless specified otherwise, primary antibodies were used at a concentration of 1:500 and secondary antibodies at a concentration of 1:5000.. We obtained anti-HIF1α and anti-SOD2 antibodies (Proteintech, Chicago, IL, USA), anti-NOX2 (GeneTex, Irvine, CA, USA), and anti-Actin and anti-Tubulin antibodies (Cell Signaling Technology, Danvers, MA, USA) from the indicated sources.

    Article Title: Small mitochondrial-targeted RNAs modulate endogenous mitochondrial protein expression in vivo
    Article Snippet: ATP6 antisera is used 1:2000.ATP6 antisera is used 1:2000.. Anti-COXII antibodies (Proteintech, Chicago IL, USA) and anti-SOD2 antibodies (LSBio, Seattle WA, USA) were used at 1:2500 and 1:2000, respectively.. Anti-ATP-alpha (a5-c antibody, Developmental Studies Hybridoma Bank, University of Iowa, USA) was used as a loading control.Anti-ATP-alpha (a5-c antibody, Developmental Studies Hybridoma Bank, University of Iowa, USA) was used as a loading control.

    Article Title: Small mitochondrial-targeted RNAs modulate endogenous mitochondrial protein expression in vivo
    Article Snippet: antisera is used 1:2000. .. Anti-COXII antibodies (Proteintech, Chicago IL, USA) and anti-SOD2 antibodies (LSBio, Seattle WA, USA) were used at 1:2500 and 1:2000, respectively. .. Anti-ATP-alpha (a5-c antibody

    Glo Assay:

    Article Title: Intraperitoneal Triamcinolone Reduces Postoperative Adhesions, Possibly through Alteration of Mitochondrial Function
    Article Snippet: Unless specified otherwise, primary antibodies were used at a concentration of 1:500 and secondary antibodies at a concentration of 1:5000.Unless specified otherwise, primary antibodies were used at a concentration of 1:500 and secondary antibodies at a concentration of 1:5000.. We obtained anti-HIF1α and anti-SOD2 antibodies (Proteintech, Chicago, IL, USA), anti-NOX2 (GeneTex, Irvine, CA, USA), and anti-Actin and anti-Tubulin antibodies (Cell Signaling Technology, Danvers, MA, USA) from the indicated sources.

    Article Title: Small mitochondrial-targeted RNAs modulate endogenous mitochondrial protein expression in vivo
    Article Snippet: ATP6 antisera is used 1:2000.ATP6 antisera is used 1:2000.. Anti-COXII antibodies (Proteintech, Chicago IL, USA) and anti-SOD2 antibodies (LSBio, Seattle WA, USA) were used at 1:2500 and 1:2000, respectively.. Anti-ATP-alpha (a5-c antibody, Developmental Studies Hybridoma Bank, University of Iowa, USA) was used as a loading control.Anti-ATP-alpha (a5-c antibody, Developmental Studies Hybridoma Bank, University of Iowa, USA) was used as a loading control.

    Article Title: Small mitochondrial-targeted RNAs modulate endogenous mitochondrial protein expression in vivo
    Article Snippet: antisera is used 1:2000. .. Anti-COXII antibodies (Proteintech, Chicago IL, USA) and anti-SOD2 antibodies (LSBio, Seattle WA, USA) were used at 1:2500 and 1:2000, respectively. .. Anti-ATP-alpha (a5-c antibody

    Standard Deviation:

    Article Title: Intraperitoneal Triamcinolone Reduces Postoperative Adhesions, Possibly through Alteration of Mitochondrial Function
    Article Snippet: Unless specified otherwise, primary antibodies were used at a concentration of 1:500 and secondary antibodies at a concentration of 1:5000.Unless specified otherwise, primary antibodies were used at a concentration of 1:500 and secondary antibodies at a concentration of 1:5000.. We obtained anti-HIF1α and anti-SOD2 antibodies (Proteintech, Chicago, IL, USA), anti-NOX2 (GeneTex, Irvine, CA, USA), and anti-Actin and anti-Tubulin antibodies (Cell Signaling Technology, Danvers, MA, USA) from the indicated sources.

    Article Title: Small mitochondrial-targeted RNAs modulate endogenous mitochondrial protein expression in vivo
    Article Snippet: ATP6 antisera is used 1:2000.ATP6 antisera is used 1:2000.. Anti-COXII antibodies (Proteintech, Chicago IL, USA) and anti-SOD2 antibodies (LSBio, Seattle WA, USA) were used at 1:2500 and 1:2000, respectively.. Anti-ATP-alpha (a5-c antibody, Developmental Studies Hybridoma Bank, University of Iowa, USA) was used as a loading control.Anti-ATP-alpha (a5-c antibody, Developmental Studies Hybridoma Bank, University of Iowa, USA) was used as a loading control.

    Article Title: Small mitochondrial-targeted RNAs modulate endogenous mitochondrial protein expression in vivo
    Article Snippet: antisera is used 1:2000. .. Anti-COXII antibodies (Proteintech, Chicago IL, USA) and anti-SOD2 antibodies (LSBio, Seattle WA, USA) were used at 1:2500 and 1:2000, respectively. .. Anti-ATP-alpha (a5-c antibody

    SDS Page:

    Article Title: Intraperitoneal Triamcinolone Reduces Postoperative Adhesions, Possibly through Alteration of Mitochondrial Function
    Article Snippet: Unless specified otherwise, primary antibodies were used at a concentration of 1:500 and secondary antibodies at a concentration of 1:5000.Unless specified otherwise, primary antibodies were used at a concentration of 1:500 and secondary antibodies at a concentration of 1:5000.. We obtained anti-HIF1α and anti-SOD2 antibodies (Proteintech, Chicago, IL, USA), anti-NOX2 (GeneTex, Irvine, CA, USA), and anti-Actin and anti-Tubulin antibodies (Cell Signaling Technology, Danvers, MA, USA) from the indicated sources.

    Article Title: Small mitochondrial-targeted RNAs modulate endogenous mitochondrial protein expression in vivo
    Article Snippet: ATP6 antisera is used 1:2000.ATP6 antisera is used 1:2000.. Anti-COXII antibodies (Proteintech, Chicago IL, USA) and anti-SOD2 antibodies (LSBio, Seattle WA, USA) were used at 1:2500 and 1:2000, respectively.. Anti-ATP-alpha (a5-c antibody, Developmental Studies Hybridoma Bank, University of Iowa, USA) was used as a loading control.Anti-ATP-alpha (a5-c antibody, Developmental Studies Hybridoma Bank, University of Iowa, USA) was used as a loading control.

    Article Title: Small mitochondrial-targeted RNAs modulate endogenous mitochondrial protein expression in vivo
    Article Snippet: antisera is used 1:2000. .. Anti-COXII antibodies (Proteintech, Chicago IL, USA) and anti-SOD2 antibodies (LSBio, Seattle WA, USA) were used at 1:2500 and 1:2000, respectively. .. Anti-ATP-alpha (a5-c antibody

    Control:

    Article Title: Intraperitoneal Triamcinolone Reduces Postoperative Adhesions, Possibly through Alteration of Mitochondrial Function
    Article Snippet: Unless specified otherwise, primary antibodies were used at a concentration of 1:500 and secondary antibodies at a concentration of 1:5000.Unless specified otherwise, primary antibodies were used at a concentration of 1:500 and secondary antibodies at a concentration of 1:5000.. We obtained anti-HIF1α and anti-SOD2 antibodies (Proteintech, Chicago, IL, USA), anti-NOX2 (GeneTex, Irvine, CA, USA), and anti-Actin and anti-Tubulin antibodies (Cell Signaling Technology, Danvers, MA, USA) from the indicated sources.

    Article Title: Small mitochondrial-targeted RNAs modulate endogenous mitochondrial protein expression in vivo
    Article Snippet: ATP6 antisera is used 1:2000.ATP6 antisera is used 1:2000.. Anti-COXII antibodies (Proteintech, Chicago IL, USA) and anti-SOD2 antibodies (LSBio, Seattle WA, USA) were used at 1:2500 and 1:2000, respectively.. Anti-ATP-alpha (a5-c antibody, Developmental Studies Hybridoma Bank, University of Iowa, USA) was used as a loading control.Anti-ATP-alpha (a5-c antibody, Developmental Studies Hybridoma Bank, University of Iowa, USA) was used as a loading control.

    Article Title: Small mitochondrial-targeted RNAs modulate endogenous mitochondrial protein expression in vivo
    Article Snippet: antisera is used 1:2000. .. Anti-COXII antibodies (Proteintech, Chicago IL, USA) and anti-SOD2 antibodies (LSBio, Seattle WA, USA) were used at 1:2500 and 1:2000, respectively. .. Anti-ATP-alpha (a5-c antibody



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    <t>SOD2</t> knockdown rescues GUTK-induced apoptosis and ΔΨm loss in reactivating quiescent PCa cells (A and B) Immunoblot analysis of SOD2 protein levels in quiescent LNCaP (A) and DU145 (B) cells treated with 20 μM GUTK for 12–48 h during cell cycle re-entry. β-actin and GAPDH served as loading controls. Quantification of relative protein levels is shown in the right panel. (C and D) Validation of SOD2 knockdown by immunoblot analysis in LNCaP (C) and DU145 (D) cells transfected with shSOD2. β-actin or GAPDH served as loading controls. Quantification of protein levels is shown in the right panel. (E and F) LNCaP shSOD2 and DU145 shSOD2 cells were treated with or without DOX to induce SOD2 knockdown. Apoptosis was assessed by Annexin V-APC/PI staining and flow cytometry in LNCaP shSOD2 (E) and DU145 shSOD2 (F) cells treated with DMSO or 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of apoptotic cell percentage is shown in the right panel. (G and H) ΔΨm assessment by JC-1 staining and flow cytometry in quiescent LNCaP shSOD2 (G) and DU145 shSOD2 (H) cells treated with either DMSO or 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of cells with low ΔΨm is shown in the right panel. Cont: proliferating control cells; Qsct: quiescent cells. ΔΨm: mitochondrial membrane potential. Data are presented as mean ± SD from three independent experiments. ∗ p < 0.05 and ∗∗∗ p < 0.001 versus indicated group.
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    <t>SOD2</t> knockdown rescues GUTK-induced apoptosis and ΔΨm loss in reactivating quiescent PCa cells (A and B) Immunoblot analysis of SOD2 protein levels in quiescent LNCaP (A) and DU145 (B) cells treated with 20 μM GUTK for 12–48 h during cell cycle re-entry. β-actin and GAPDH served as loading controls. Quantification of relative protein levels is shown in the right panel. (C and D) Validation of SOD2 knockdown by immunoblot analysis in LNCaP (C) and DU145 (D) cells transfected with shSOD2. β-actin or GAPDH served as loading controls. Quantification of protein levels is shown in the right panel. (E and F) LNCaP shSOD2 and DU145 shSOD2 cells were treated with or without DOX to induce SOD2 knockdown. Apoptosis was assessed by Annexin V-APC/PI staining and flow cytometry in LNCaP shSOD2 (E) and DU145 shSOD2 (F) cells treated with DMSO or 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of apoptotic cell percentage is shown in the right panel. (G and H) ΔΨm assessment by JC-1 staining and flow cytometry in quiescent LNCaP shSOD2 (G) and DU145 shSOD2 (H) cells treated with either DMSO or 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of cells with low ΔΨm is shown in the right panel. Cont: proliferating control cells; Qsct: quiescent cells. ΔΨm: mitochondrial membrane potential. Data are presented as mean ± SD from three independent experiments. ∗ p < 0.05 and ∗∗∗ p < 0.001 versus indicated group.
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    sod2  (Santa Cruz Biotechnology)
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    <t>SOD2</t> knockdown rescues GUTK-induced apoptosis and ΔΨm loss in reactivating quiescent PCa cells (A and B) Immunoblot analysis of SOD2 protein levels in quiescent LNCaP (A) and DU145 (B) cells treated with 20 μM GUTK for 12–48 h during cell cycle re-entry. β-actin and GAPDH served as loading controls. Quantification of relative protein levels is shown in the right panel. (C and D) Validation of SOD2 knockdown by immunoblot analysis in LNCaP (C) and DU145 (D) cells transfected with shSOD2. β-actin or GAPDH served as loading controls. Quantification of protein levels is shown in the right panel. (E and F) LNCaP shSOD2 and DU145 shSOD2 cells were treated with or without DOX to induce SOD2 knockdown. Apoptosis was assessed by Annexin V-APC/PI staining and flow cytometry in LNCaP shSOD2 (E) and DU145 shSOD2 (F) cells treated with DMSO or 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of apoptotic cell percentage is shown in the right panel. (G and H) ΔΨm assessment by JC-1 staining and flow cytometry in quiescent LNCaP shSOD2 (G) and DU145 shSOD2 (H) cells treated with either DMSO or 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of cells with low ΔΨm is shown in the right panel. Cont: proliferating control cells; Qsct: quiescent cells. ΔΨm: mitochondrial membrane potential. Data are presented as mean ± SD from three independent experiments. ∗ p < 0.05 and ∗∗∗ p < 0.001 versus indicated group.
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    Image Search Results


    SOD2 knockdown rescues GUTK-induced apoptosis and ΔΨm loss in reactivating quiescent PCa cells (A and B) Immunoblot analysis of SOD2 protein levels in quiescent LNCaP (A) and DU145 (B) cells treated with 20 μM GUTK for 12–48 h during cell cycle re-entry. β-actin and GAPDH served as loading controls. Quantification of relative protein levels is shown in the right panel. (C and D) Validation of SOD2 knockdown by immunoblot analysis in LNCaP (C) and DU145 (D) cells transfected with shSOD2. β-actin or GAPDH served as loading controls. Quantification of protein levels is shown in the right panel. (E and F) LNCaP shSOD2 and DU145 shSOD2 cells were treated with or without DOX to induce SOD2 knockdown. Apoptosis was assessed by Annexin V-APC/PI staining and flow cytometry in LNCaP shSOD2 (E) and DU145 shSOD2 (F) cells treated with DMSO or 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of apoptotic cell percentage is shown in the right panel. (G and H) ΔΨm assessment by JC-1 staining and flow cytometry in quiescent LNCaP shSOD2 (G) and DU145 shSOD2 (H) cells treated with either DMSO or 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of cells with low ΔΨm is shown in the right panel. Cont: proliferating control cells; Qsct: quiescent cells. ΔΨm: mitochondrial membrane potential. Data are presented as mean ± SD from three independent experiments. ∗ p < 0.05 and ∗∗∗ p < 0.001 versus indicated group.

    Journal: iScience

    Article Title: GUTK induces apoptosis in reactivating quiescent prostate cancer cells via Aurora A-mediated stabilization of SOD2

    doi: 10.1016/j.isci.2026.115739

    Figure Lengend Snippet: SOD2 knockdown rescues GUTK-induced apoptosis and ΔΨm loss in reactivating quiescent PCa cells (A and B) Immunoblot analysis of SOD2 protein levels in quiescent LNCaP (A) and DU145 (B) cells treated with 20 μM GUTK for 12–48 h during cell cycle re-entry. β-actin and GAPDH served as loading controls. Quantification of relative protein levels is shown in the right panel. (C and D) Validation of SOD2 knockdown by immunoblot analysis in LNCaP (C) and DU145 (D) cells transfected with shSOD2. β-actin or GAPDH served as loading controls. Quantification of protein levels is shown in the right panel. (E and F) LNCaP shSOD2 and DU145 shSOD2 cells were treated with or without DOX to induce SOD2 knockdown. Apoptosis was assessed by Annexin V-APC/PI staining and flow cytometry in LNCaP shSOD2 (E) and DU145 shSOD2 (F) cells treated with DMSO or 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of apoptotic cell percentage is shown in the right panel. (G and H) ΔΨm assessment by JC-1 staining and flow cytometry in quiescent LNCaP shSOD2 (G) and DU145 shSOD2 (H) cells treated with either DMSO or 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of cells with low ΔΨm is shown in the right panel. Cont: proliferating control cells; Qsct: quiescent cells. ΔΨm: mitochondrial membrane potential. Data are presented as mean ± SD from three independent experiments. ∗ p < 0.05 and ∗∗∗ p < 0.001 versus indicated group.

    Article Snippet: Sections were subjected to hematoxylin and eosin (H&E) staining or immunohistochemical staining using primary antibodies against Ki-67 (ab16667, Abcam, Shanghai, China), SOD2 (ET1701-54, HUABIO, Hangzhou, China), Cleaved Caspase 3 (#9661, Cell Signaling Technology, Danvers, USA) and Aurora A (ET1609-22, HUABIO, Hangzhou, China).

    Techniques: Knockdown, Western Blot, Biomarker Discovery, Transfection, Staining, Flow Cytometry, Control, Membrane

    SOD2 overexpression exacerbates GUTK-induced apoptosis and ΔΨm loss in reactivating quiescent PCa cells (A and B) Immunoblot validation of SOD2 overexpression in LNCaP (A) and DU145 (B) cells stably transfected with empty vector (EV) or SOD2 expression construct (SOD2 OE). GAPDH served as the loading control. Quantification of relative protein levels is shown in the right panel. (C and D) Annexin V-FITC/PI staining and flow cytometry analysis of EV control or SOD2 OE LNCaP (C) and DU145 (D) cells treated with or without 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of apoptotic cell percentages is shown in the right panel. (E and F) ΔΨm analysis by JC-1 staining and flow cytometry in EV control or SOD2 OE LNCaP (E) and DU145 (F) cells treated with or without 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of cells with low ΔΨm is shown in the right panel. ΔΨm: mitochondrial membrane potential. Data are presented as mean ± SD from three independent experiments. ∗∗∗ p < 0.001 versus indicated group.

    Journal: iScience

    Article Title: GUTK induces apoptosis in reactivating quiescent prostate cancer cells via Aurora A-mediated stabilization of SOD2

    doi: 10.1016/j.isci.2026.115739

    Figure Lengend Snippet: SOD2 overexpression exacerbates GUTK-induced apoptosis and ΔΨm loss in reactivating quiescent PCa cells (A and B) Immunoblot validation of SOD2 overexpression in LNCaP (A) and DU145 (B) cells stably transfected with empty vector (EV) or SOD2 expression construct (SOD2 OE). GAPDH served as the loading control. Quantification of relative protein levels is shown in the right panel. (C and D) Annexin V-FITC/PI staining and flow cytometry analysis of EV control or SOD2 OE LNCaP (C) and DU145 (D) cells treated with or without 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of apoptotic cell percentages is shown in the right panel. (E and F) ΔΨm analysis by JC-1 staining and flow cytometry in EV control or SOD2 OE LNCaP (E) and DU145 (F) cells treated with or without 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of cells with low ΔΨm is shown in the right panel. ΔΨm: mitochondrial membrane potential. Data are presented as mean ± SD from three independent experiments. ∗∗∗ p < 0.001 versus indicated group.

    Article Snippet: Sections were subjected to hematoxylin and eosin (H&E) staining or immunohistochemical staining using primary antibodies against Ki-67 (ab16667, Abcam, Shanghai, China), SOD2 (ET1701-54, HUABIO, Hangzhou, China), Cleaved Caspase 3 (#9661, Cell Signaling Technology, Danvers, USA) and Aurora A (ET1609-22, HUABIO, Hangzhou, China).

    Techniques: Over Expression, Western Blot, Biomarker Discovery, Stable Transfection, Transfection, Plasmid Preparation, Expressing, Construct, Control, Staining, Flow Cytometry, Membrane

    GUTK downregulates Aurora A expression during the reactivation of quiescent PCa cells (A and B) RT-PCR analysis of SOD2 mRNA levels in quiescent LNCaP (A) and DU145 (B) cells treated with or without 20 μM GUTK for the indicated times during cell cycle re-entry. (C and D) Quiescent LNCaP and DU145 cells were induced to re-enter the cell cycle and simultaneously exposed to 10 μM MG132 or DMSO for the indicated times. Immunoblot analysis of SOD2 protein was performed in quiescent LNCaP (C) and DU145 (D) cells. GAPDH served as the loading control. Quantification of relative protein levels is shown in the lower panel. (E and F) Quiescent LNCaP and DU145 cells were induced to re-enter the cell cycle for 6 h and then exposed to 50 μM CHX or DMSO for the indicated times. Immunoblot analysis of SOD2 and Aurora A proteins was performed in quiescent LNCaP (E) and DU145 (F) cells. β-actin or GAPDH served as loading control. Quantification of relative protein levels is shown in the lower panel. (G and H) Immunoblot analysis of Aurora A protein levels in quiescent LNCaP (G) and DU145 (H) cells treated with 20 μM GUTK for the indicated times during cell cycle re-entry. β-actin served as loading control. Quantification of relative protein levels is shown in the lower panel. (I and J) RT-PCR analysis of Aurora A mRNA levels in quiescent LNCaP (I) and DU145 (J) cells treated with 20 μM GUTK for the indicated times during cell cycle re-entry. Cont: proliferating control cells; Qsct: quiescent cells; CHX: cycloheximide. Data are presented as mean ± SD from three independent experiments. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 versus indicated group. ns: not significant.

    Journal: iScience

    Article Title: GUTK induces apoptosis in reactivating quiescent prostate cancer cells via Aurora A-mediated stabilization of SOD2

    doi: 10.1016/j.isci.2026.115739

    Figure Lengend Snippet: GUTK downregulates Aurora A expression during the reactivation of quiescent PCa cells (A and B) RT-PCR analysis of SOD2 mRNA levels in quiescent LNCaP (A) and DU145 (B) cells treated with or without 20 μM GUTK for the indicated times during cell cycle re-entry. (C and D) Quiescent LNCaP and DU145 cells were induced to re-enter the cell cycle and simultaneously exposed to 10 μM MG132 or DMSO for the indicated times. Immunoblot analysis of SOD2 protein was performed in quiescent LNCaP (C) and DU145 (D) cells. GAPDH served as the loading control. Quantification of relative protein levels is shown in the lower panel. (E and F) Quiescent LNCaP and DU145 cells were induced to re-enter the cell cycle for 6 h and then exposed to 50 μM CHX or DMSO for the indicated times. Immunoblot analysis of SOD2 and Aurora A proteins was performed in quiescent LNCaP (E) and DU145 (F) cells. β-actin or GAPDH served as loading control. Quantification of relative protein levels is shown in the lower panel. (G and H) Immunoblot analysis of Aurora A protein levels in quiescent LNCaP (G) and DU145 (H) cells treated with 20 μM GUTK for the indicated times during cell cycle re-entry. β-actin served as loading control. Quantification of relative protein levels is shown in the lower panel. (I and J) RT-PCR analysis of Aurora A mRNA levels in quiescent LNCaP (I) and DU145 (J) cells treated with 20 μM GUTK for the indicated times during cell cycle re-entry. Cont: proliferating control cells; Qsct: quiescent cells; CHX: cycloheximide. Data are presented as mean ± SD from three independent experiments. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 versus indicated group. ns: not significant.

    Article Snippet: Sections were subjected to hematoxylin and eosin (H&E) staining or immunohistochemical staining using primary antibodies against Ki-67 (ab16667, Abcam, Shanghai, China), SOD2 (ET1701-54, HUABIO, Hangzhou, China), Cleaved Caspase 3 (#9661, Cell Signaling Technology, Danvers, USA) and Aurora A (ET1609-22, HUABIO, Hangzhou, China).

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

    Aurora A overexpression suppresses SOD2 expression and attenuates GUTK-induced apoptosis in reactivating quiescent PCa cells (A and B) RT-PCR validation of Aurora A mRNA overexpression in LNCaP (A) and DU145 (B) cells stably transfected with either empty vector (EV) or an Aurora A expression construct (Aurora A OE). (C and D) Immunoblot analysis of Aurora A and SOD2 protein levels in quiescent EV control or Aurora A OE LNCaP (C) and DU145 (D) cells at the indicated times after cell cycle re-entry. GAPDH served as the loading control. Quantification of relative protein levels is shown in the right panel. (E and F) Apoptosis analysis by Annexin V-FITC/PI staining and flow cytometry in EV control or Aurora A OE LNCaP (E) and DU145 (F) cells treated with or without 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of apoptotic cell percentages is shown in the right panel. (G and H) ΔΨm analysis by JC-1 staining and flow cytometry in quiescent EV control and Aurora A OE LNCaP (G) and DU145 (H) cells treated with or without 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of cells with low ΔΨm is shown in the right panel. ΔΨm: mitochondrial membrane potential. Data are presented as mean ± SD from three independent experiments. ∗∗ p < 0.01 and ∗∗∗ p < 0.001 versus indicated group.

    Journal: iScience

    Article Title: GUTK induces apoptosis in reactivating quiescent prostate cancer cells via Aurora A-mediated stabilization of SOD2

    doi: 10.1016/j.isci.2026.115739

    Figure Lengend Snippet: Aurora A overexpression suppresses SOD2 expression and attenuates GUTK-induced apoptosis in reactivating quiescent PCa cells (A and B) RT-PCR validation of Aurora A mRNA overexpression in LNCaP (A) and DU145 (B) cells stably transfected with either empty vector (EV) or an Aurora A expression construct (Aurora A OE). (C and D) Immunoblot analysis of Aurora A and SOD2 protein levels in quiescent EV control or Aurora A OE LNCaP (C) and DU145 (D) cells at the indicated times after cell cycle re-entry. GAPDH served as the loading control. Quantification of relative protein levels is shown in the right panel. (E and F) Apoptosis analysis by Annexin V-FITC/PI staining and flow cytometry in EV control or Aurora A OE LNCaP (E) and DU145 (F) cells treated with or without 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of apoptotic cell percentages is shown in the right panel. (G and H) ΔΨm analysis by JC-1 staining and flow cytometry in quiescent EV control and Aurora A OE LNCaP (G) and DU145 (H) cells treated with or without 20 μM GUTK for the indicated times during cell cycle re-entry. Quantification of cells with low ΔΨm is shown in the right panel. ΔΨm: mitochondrial membrane potential. Data are presented as mean ± SD from three independent experiments. ∗∗ p < 0.01 and ∗∗∗ p < 0.001 versus indicated group.

    Article Snippet: Sections were subjected to hematoxylin and eosin (H&E) staining or immunohistochemical staining using primary antibodies against Ki-67 (ab16667, Abcam, Shanghai, China), SOD2 (ET1701-54, HUABIO, Hangzhou, China), Cleaved Caspase 3 (#9661, Cell Signaling Technology, Danvers, USA) and Aurora A (ET1609-22, HUABIO, Hangzhou, China).

    Techniques: Over Expression, Expressing, Reverse Transcription Polymerase Chain Reaction, Biomarker Discovery, Stable Transfection, Transfection, Plasmid Preparation, Construct, Western Blot, Control, Staining, Flow Cytometry, Membrane

    GUTK combined with docetaxel enhances the reduction of orthotopic prostate tumor growth in C57BL/6 mice (A) Experimental schematic of the orthotopic prostate cancer model and treatment schedule in C57BL/6 mice established using RM-1 murine PCa cells. Mice were randomized into four groups: vehicle, GUTK, docetaxel, or combination treatment ( n = 6 per group). (B) Representative images of major organ morphology (heart, liver, spleen, lungs, kidneys) collected on day 9. (C) Daily body weight measurements throughout the experiment period. (D) Representative images of dissected tumors collected at the day 9 endpoint. (E) Tumor volume quantification at the endpoint. (F) Representative immunohistochemical staining of tumor sections for H&E, Ki-67, SOD2, Aurora A and cleaved caspase 3. Scale bars, 50 μm. Quantification of relative protein levels is shown in the lower panel. Solvent A represents Tween 80: ethanol: saline = 20: 13: 67. Solvent B represents Cremophor EL: Ethanol: 5% glucose = 1: 1: 38. Data are presented as mean ± SEM for each group. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 versus vehicle control group.

    Journal: iScience

    Article Title: GUTK induces apoptosis in reactivating quiescent prostate cancer cells via Aurora A-mediated stabilization of SOD2

    doi: 10.1016/j.isci.2026.115739

    Figure Lengend Snippet: GUTK combined with docetaxel enhances the reduction of orthotopic prostate tumor growth in C57BL/6 mice (A) Experimental schematic of the orthotopic prostate cancer model and treatment schedule in C57BL/6 mice established using RM-1 murine PCa cells. Mice were randomized into four groups: vehicle, GUTK, docetaxel, or combination treatment ( n = 6 per group). (B) Representative images of major organ morphology (heart, liver, spleen, lungs, kidneys) collected on day 9. (C) Daily body weight measurements throughout the experiment period. (D) Representative images of dissected tumors collected at the day 9 endpoint. (E) Tumor volume quantification at the endpoint. (F) Representative immunohistochemical staining of tumor sections for H&E, Ki-67, SOD2, Aurora A and cleaved caspase 3. Scale bars, 50 μm. Quantification of relative protein levels is shown in the lower panel. Solvent A represents Tween 80: ethanol: saline = 20: 13: 67. Solvent B represents Cremophor EL: Ethanol: 5% glucose = 1: 1: 38. Data are presented as mean ± SEM for each group. ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001 versus vehicle control group.

    Article Snippet: Sections were subjected to hematoxylin and eosin (H&E) staining or immunohistochemical staining using primary antibodies against Ki-67 (ab16667, Abcam, Shanghai, China), SOD2 (ET1701-54, HUABIO, Hangzhou, China), Cleaved Caspase 3 (#9661, Cell Signaling Technology, Danvers, USA) and Aurora A (ET1609-22, HUABIO, Hangzhou, China).

    Techniques: Immunohistochemical staining, Staining, Solvent, Saline, Control