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MedChemExpress atm inhibitor

<t>ROS‐ATM‐CBP</t> signalling pathway activates PARP1 lactylation. (A, B) Intracellular ROS and lactate levels in HL‐1 cells treated with 1 µM doxorubicin for 0, 2 and 4 h. (C) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation. HL‐1 cells were stimulated by doxorubicin (1 µM for 0, 2 and 4 h), and the cells were lysed and immunoprecipitated using an anti‐PARP1 antibody, followed by detection of Pan‐KLA. (D) Schematic of the effect of SIRT1 activation on the lactylation level of PARP1 in mice. DOX (5 mg/kg) or the same volume of saline was administered intraperitoneally once weekly. One week before the DOX treatment, mice were pre‐treated with resveratrol (SIRT1 activator, 10 mg/kg/day) via daily intraperitoneal injections. (E) The SIRT1 activity was detected. (F–H) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation and protein expression of SIRT1. (I) Schematic of the effect of CBP inhibition on the lactylation level of PARP1 in mice. DOX (5 mg/kg) or the same volume of saline was administered intraperitoneally once weekly. One week before the DOX treatment, mice were pre‐treated with SGC‐CBP30 <t>(CBP</t> <t>inhibitor,</t> 15 mg/kg/day) via daily intraperitoneal injections. (J) The CBP activity was detected. (K–M) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation and protein expression of CBP. (A–C) Based on the central limit theorem, the data were considered to be normally distributed. Relative protein levels were calculated as fold changes vs the first group. Data are presented as mean ± SD. Statistical significance was assessed by one‐way ANOVA with Tukey multiple comparisons test ( P values adjusted for 3 comparisons). (D–M) Relative protein levels were calculated as fold changes vs. the first group. Data are presented as mean ± SD. Statistical significance was assessed by two‐way ANOVA with Bonferroni multiple comparisons test ( p ‐values adjusted for 9 comparisons). ns p > .05, * p < .05, ** p < .01, *** p < .001.

Atm Inhibitor, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 95/100, based on 77 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ku+55933/KU-55933/pmc13478851-211-0-30
Average 95 stars, based on 77 article reviews

atm inhibitor - by Bioz Stars, 2026-10

95/100 stars

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1) Product Images from "ROS‐ATM‐CBP axis‐mediated PARP1 lactylation aggravates doxorubicin‐induced cardiotoxicity"

Article Title: ROS‐ATM‐CBP axis‐mediated PARP1 lactylation aggravates doxorubicin‐induced cardiotoxicity

Journal: Clinical and Translational Medicine

doi: 10.1002/ctm2.70745

ROS‐ATM‐CBP signalling pathway activates PARP1 lactylation. (A, B) Intracellular ROS and lactate levels in HL‐1 cells treated with 1 µM doxorubicin for 0, 2 and 4 h. (C) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation. HL‐1 cells were stimulated by doxorubicin (1 µM for 0, 2 and 4 h), and the cells were lysed and immunoprecipitated using an anti‐PARP1 antibody, followed by detection of Pan‐KLA. (D) Schematic of the effect of SIRT1 activation on the lactylation level of PARP1 in mice. DOX (5 mg/kg) or the same volume of saline was administered intraperitoneally once weekly. One week before the DOX treatment, mice were pre‐treated with resveratrol (SIRT1 activator, 10 mg/kg/day) via daily intraperitoneal injections. (E) The SIRT1 activity was detected. (F–H) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation and protein expression of SIRT1. (I) Schematic of the effect of CBP inhibition on the lactylation level of PARP1 in mice. DOX (5 mg/kg) or the same volume of saline was administered intraperitoneally once weekly. One week before the DOX treatment, mice were pre‐treated with SGC‐CBP30 (CBP inhibitor, 15 mg/kg/day) via daily intraperitoneal injections. (J) The CBP activity was detected. (K–M) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation and protein expression of CBP. (A–C) Based on the central limit theorem, the data were considered to be normally distributed. Relative protein levels were calculated as fold changes vs the first group. Data are presented as mean ± SD. Statistical significance was assessed by one‐way ANOVA with Tukey multiple comparisons test ( P values adjusted for 3 comparisons). (D–M) Relative protein levels were calculated as fold changes vs. the first group. Data are presented as mean ± SD. Statistical significance was assessed by two‐way ANOVA with Bonferroni multiple comparisons test ( p ‐values adjusted for 9 comparisons). ns p > .05, * p < .05, ** p < .01, *** p < .001.

Figure Legend Snippet: ROS‐ATM‐CBP signalling pathway activates PARP1 lactylation. (A, B) Intracellular ROS and lactate levels in HL‐1 cells treated with 1 µM doxorubicin for 0, 2 and 4 h. (C) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation. HL‐1 cells were stimulated by doxorubicin (1 µM for 0, 2 and 4 h), and the cells were lysed and immunoprecipitated using an anti‐PARP1 antibody, followed by detection of Pan‐KLA. (D) Schematic of the effect of SIRT1 activation on the lactylation level of PARP1 in mice. DOX (5 mg/kg) or the same volume of saline was administered intraperitoneally once weekly. One week before the DOX treatment, mice were pre‐treated with resveratrol (SIRT1 activator, 10 mg/kg/day) via daily intraperitoneal injections. (E) The SIRT1 activity was detected. (F–H) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation and protein expression of SIRT1. (I) Schematic of the effect of CBP inhibition on the lactylation level of PARP1 in mice. DOX (5 mg/kg) or the same volume of saline was administered intraperitoneally once weekly. One week before the DOX treatment, mice were pre‐treated with SGC‐CBP30 (CBP inhibitor, 15 mg/kg/day) via daily intraperitoneal injections. (J) The CBP activity was detected. (K–M) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation and protein expression of CBP. (A–C) Based on the central limit theorem, the data were considered to be normally distributed. Relative protein levels were calculated as fold changes vs the first group. Data are presented as mean ± SD. Statistical significance was assessed by one‐way ANOVA with Tukey multiple comparisons test ( P values adjusted for 3 comparisons). (D–M) Relative protein levels were calculated as fold changes vs. the first group. Data are presented as mean ± SD. Statistical significance was assessed by two‐way ANOVA with Bonferroni multiple comparisons test ( p ‐values adjusted for 9 comparisons). ns p > .05, * p < .05, ** p < .01, *** p < .001.

Techniques Used: Immunoprecipitation, Western Blot, Activation Assay, Saline, Activity Assay, Expressing, Inhibition

Model showing the molecular signalling cascade of CBP‐PARP1 lactylation–PARylation axis. The schematic depicts how oxidative stress‐induced ROS activates the ATM‐CBP‐PARP1 signalling pathway via a lactylation–PARylation cascade to promote cardiomyocyte apoptosis.

Figure Legend Snippet: Model showing the molecular signalling cascade of CBP‐PARP1 lactylation–PARylation axis. The schematic depicts how oxidative stress‐induced ROS activates the ATM‐CBP‐PARP1 signalling pathway via a lactylation–PARylation cascade to promote cardiomyocyte apoptosis.

Techniques Used:

other:

Article Title: PARP inhibitor BMN673 triggers PARylation-mediated ATF4-GDF15 pathway to drive autophagy and ferroptosis in ataxia telangiectasia mutated gene-deficient colorectal cancer cells
Article Snippet: Chloroquine (HY-17589A), bafilomycin A1 (HY-100558), rapamycin (HY-10219), and KU-55933 (HY-12016) were purchased from MedChemExpress.

Article Title: Transcriptomics-guided high-throughput drug screening identifies potent therapies for P53 pathway altered DIPG/DMG
Article Snippet: The reagents SN-38 (Cat# HY-13704), Olaparib (Cat# HY-10162), SCH900776 (Cat# HY-15532), AZ20 (Cat# HY-15557), KU-55933 (Cat# HY-12016), and Adavosertib (Cat# HY-10993) were purchased from MedChemExpress.

Article Title: E0703 targets ERβ to facilitate the upregulation of GLI3, thereby alleviating irradiation-induced DNA damage on lymphocytes.
Article Snippet: To measure cell viability, CCK-8 (Shanghai Topscience Co., Ltd.) and Calcein AM/propidium iodide (PI) Double Staining Kit (DOJINDO, Japan) were employed according to the manufacturers’ instructions.

Article Title: GPI inactivation mediates pentose phosphate pathway flux switch-on inducing temozolomide resistance in glioma stem cell.
Article Snippet: Temozolomide (TMZ) resistance in glioblastoma (GBM) remains a substantial clinical challenge.. Targeting glioma stem cells (GSCs) represents a promising strategy to overcome chemoresistance and tumor recurrence.. In this study, we found that GSCs maintain chemoresistance by increasing pentose phosphate pathway (PPP) flux compared with differentiated tumor cells.

Protein-Protein interactions:

Article Title: E0703 targets ERβ to facilitate the upregulation of GLI3, thereby alleviating irradiation-induced DNA damage on lymphocytes
Article Snippet: To measure cell viability, CCK-8 (Shanghai Topscience Co., Ltd.) and Calcein AM/propidium iodide (PI) Double Staining Kit (DOJINDO, Japan) were employed according to the manufacturers’ instructions. .. KU-55933 (ATM antagonist), BML-277 (CHK2 antagonist), AZD9496 (ERα antagonist), PHTPP (ERβ antagonist), and SBI0640756 (eIF4G1 antagonist) were all purchased from MedChemExpress to inhibit the corresponding signaling pathways. .. KU-55933 (ATM antagonist), BML-277 (CHK2 antagonist), AZD9496 (ERα antagonist), PHTPP (ERβ antagonist), and SBI0640756 (eIF4G1 antagonist) were all purchased from MedChemExpress to inhibit the corresponding signaling pathways.

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Journal: Clinical and Translational Medicine

Article Title: ROS‐ATM‐CBP axis‐mediated PARP1 lactylation aggravates doxorubicin‐induced cardiotoxicity

doi: 10.1002/ctm2.70745

Figure Lengend Snippet: ROS‐ATM‐CBP signalling pathway activates PARP1 lactylation. (A, B) Intracellular ROS and lactate levels in HL‐1 cells treated with 1 µM doxorubicin for 0, 2 and 4 h. (C) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation. HL‐1 cells were stimulated by doxorubicin (1 µM for 0, 2 and 4 h), and the cells were lysed and immunoprecipitated using an anti‐PARP1 antibody, followed by detection of Pan‐KLA. (D) Schematic of the effect of SIRT1 activation on the lactylation level of PARP1 in mice. DOX (5 mg/kg) or the same volume of saline was administered intraperitoneally once weekly. One week before the DOX treatment, mice were pre‐treated with resveratrol (SIRT1 activator, 10 mg/kg/day) via daily intraperitoneal injections. (E) The SIRT1 activity was detected. (F–H) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation and protein expression of SIRT1. (I) Schematic of the effect of CBP inhibition on the lactylation level of PARP1 in mice. DOX (5 mg/kg) or the same volume of saline was administered intraperitoneally once weekly. One week before the DOX treatment, mice were pre‐treated with SGC‐CBP30 (CBP inhibitor, 15 mg/kg/day) via daily intraperitoneal injections. (J) The CBP activity was detected. (K–M) Representative immunoprecipitation, western blots and quantification for detecting PARP1 lactylation and protein expression of CBP. (A–C) Based on the central limit theorem, the data were considered to be normally distributed. Relative protein levels were calculated as fold changes vs the first group. Data are presented as mean ± SD. Statistical significance was assessed by one‐way ANOVA with Tukey multiple comparisons test ( P values adjusted for 3 comparisons). (D–M) Relative protein levels were calculated as fold changes vs. the first group. Data are presented as mean ± SD. Statistical significance was assessed by two‐way ANOVA with Bonferroni multiple comparisons test ( p ‐values adjusted for 9 comparisons). ns p > .05, * p < .05, ** p < .01, *** p < .001.

Article Snippet: ATM inhibitor (KU‐55933; #HY‐12016; 10 μM; 2 h); LDHA inhibitor (Galloflavin; #HY‐W040118; 10 −5 M; 24 h) and CBP activator (CTB; #HY‐134964; 10 −4 M; 24 h) were obtained from MedChemExpress.

Techniques: Immunoprecipitation, Western Blot, Activation Assay, Saline, Activity Assay, Expressing, Inhibition

Journal: Clinical and Translational Medicine

Article Title: ROS‐ATM‐CBP axis‐mediated PARP1 lactylation aggravates doxorubicin‐induced cardiotoxicity

doi: 10.1002/ctm2.70745

Figure Lengend Snippet: Model showing the molecular signalling cascade of CBP‐PARP1 lactylation–PARylation axis. The schematic depicts how oxidative stress‐induced ROS activates the ATM‐CBP‐PARP1 signalling pathway via a lactylation–PARylation cascade to promote cardiomyocyte apoptosis.

Techniques:

Inhibition of ATM restores NSCLC cells to IFN-γ by inducing DNA damage response (A) Cell viability of A549 (left panel) or PC-9 (right panel) treated with IFN-γ (1000 ng/ml) and/or KU-55933 (10 μM) for 24 h are shown. Data are presented as mean ± SD. * p < 0.05. (B) Expression of γH2AX and b-Actin (loading control) in A549 (left panel) or PC-9 (right panel) cells treated with IFN-γ (1000 ng/ml) and/or KU-55933 (10 μM) for 24 h are shown.

Journal: Biochemistry and Biophysics Reports

Article Title: ATM inhibition restores IFN-γ sensitivity and induces ferroptosis in NSCLC via DNA damage response

doi: 10.1016/j.bbrep.2026.102568

Figure Lengend Snippet: Inhibition of ATM restores NSCLC cells to IFN-γ by inducing DNA damage response (A) Cell viability of A549 (left panel) or PC-9 (right panel) treated with IFN-γ (1000 ng/ml) and/or KU-55933 (10 μM) for 24 h are shown. Data are presented as mean ± SD. * p < 0.05. (B) Expression of γH2AX and b-Actin (loading control) in A549 (left panel) or PC-9 (right panel) cells treated with IFN-γ (1000 ng/ml) and/or KU-55933 (10 μM) for 24 h are shown.

Article Snippet: IFN-γ was purchased from Biolegend, and ATM inhibitor KU-55933 was purchased from MedChem Express.

Techniques: Inhibition, Expressing, Control

Inhibition of ATM in combination with IFN-γ induce ferroptosis in NSCLCs Cell viability of A549 (A) or PC-9 (B) treated with the indicated combination of IFN-γ (1000 ng/ml), KU-55933 (10 μM), Ferrostatin-1 (5 μM), and Liproxstatin-1 (5 μM) for 24 h are shown. Data are presented as mean ± SD. * p < 0.05.

Journal: Biochemistry and Biophysics Reports

Article Title: ATM inhibition restores IFN-γ sensitivity and induces ferroptosis in NSCLC via DNA damage response

doi: 10.1016/j.bbrep.2026.102568

Figure Lengend Snippet: Inhibition of ATM in combination with IFN-γ induce ferroptosis in NSCLCs Cell viability of A549 (A) or PC-9 (B) treated with the indicated combination of IFN-γ (1000 ng/ml), KU-55933 (10 μM), Ferrostatin-1 (5 μM), and Liproxstatin-1 (5 μM) for 24 h are shown. Data are presented as mean ± SD. * p < 0.05.

Article Snippet: IFN-γ was purchased from Biolegend, and ATM inhibitor KU-55933 was purchased from MedChem Express.

Techniques: Inhibition

ATM inhibition in combination with IFN-γ alters glutathione metabolism in NSCLC Cells were treated with IFN-γ (1000 ng/mL) and/or KU-55933 (10 μM) for 24 h, and then the intracellular levels of GSH and GSSG were quantified. The results of total glutathione (A), GSH (B), GSSG (C), and GSH/GSSG ratio (D) are shown. * p < 0.05.

Journal: Biochemistry and Biophysics Reports

Article Title: ATM inhibition restores IFN-γ sensitivity and induces ferroptosis in NSCLC via DNA damage response

doi: 10.1016/j.bbrep.2026.102568

Figure Lengend Snippet: ATM inhibition in combination with IFN-γ alters glutathione metabolism in NSCLC Cells were treated with IFN-γ (1000 ng/mL) and/or KU-55933 (10 μM) for 24 h, and then the intracellular levels of GSH and GSSG were quantified. The results of total glutathione (A), GSH (B), GSSG (C), and GSH/GSSG ratio (D) are shown. * p < 0.05.

Article Snippet: IFN-γ was purchased from Biolegend, and ATM inhibitor KU-55933 was purchased from MedChem Express.

Techniques: Inhibition

Knocking down SKA2-induced cell-cycle arrest and apoptosis through the SKA2/ROS/ATM axis in GC cell lines (A) Western blotting analysis of γ-H2AX (Ser139), ATM, p -ATM (Ser1981), p -Chk2 (Thr68), and SKA2 expression in SNU638 and NUGC3 SKA2-knockdown cell lines. (B) Western blotting analysis of SKA2 overexpression in SNU638 and NUGC3 SKA2-knockdown cell lines using antibodies against γ-H2AX (Ser139), ATM, p -ATM (Ser1981), p -Chk2 (Thr68), and SKA2. (C) Western blotting analysis of KU-55933 treatment in SNU638 and NUGC3 SKA2-knockdown cell lines using antibodies against cyclin D1, cyclin A2, cyclin B1, p -Chk2 (Thr68), PARP, Cleaved-Caspase3, JNK, p -JNK (Thr183/Tyr185), ATM, p -ATM (Ser1981), and SKA2. (D) Western blotting analysis of BML-277 treatment in SNU638 and NUGC3 SKA2-knockdown cell lines using antibodies against cyclin D1, cyclin A2, cyclin B1, p -Chk2 (Thr68), and SKA2. (E) Western blotting analysis of P38, p-P38 (Thr180/Tyr182), ERK, p -ERK1/2 (Thr202/Tyr204), JNK, p -JNK (Thr183/Tyr185), and SKA2 expression in SNU638 and NUGC3 SKA2-knockdown cell lines. (F) Western blotting analysis of the rescue effect of SKA2 overexpression on MAPK pathway markers (ERK, p -ERK1/2, JNK, and p -JNK) in SNU638 and NUGC3 SKA2-knockdown cell lines. (G) Western blotting analysis of JNK-IN-8 treatment in SNU638 SKA2-knockdown cell lines using antibodies against PARP, cleaved-caspase3, JNK, p -JNK (Thr183/Tyr185), and SKA2. α-Tubulin was used as the internal control for all blots. Representative blotting images are shown from 3 independent experiments.

Journal: iScience

Article Title: SKA2 promotes gastric cancer progression by regulating glutathione metabolism

doi: 10.1016/j.isci.2026.115202

Figure Lengend Snippet: Knocking down SKA2-induced cell-cycle arrest and apoptosis through the SKA2/ROS/ATM axis in GC cell lines (A) Western blotting analysis of γ-H2AX (Ser139), ATM, p -ATM (Ser1981), p -Chk2 (Thr68), and SKA2 expression in SNU638 and NUGC3 SKA2-knockdown cell lines. (B) Western blotting analysis of SKA2 overexpression in SNU638 and NUGC3 SKA2-knockdown cell lines using antibodies against γ-H2AX (Ser139), ATM, p -ATM (Ser1981), p -Chk2 (Thr68), and SKA2. (C) Western blotting analysis of KU-55933 treatment in SNU638 and NUGC3 SKA2-knockdown cell lines using antibodies against cyclin D1, cyclin A2, cyclin B1, p -Chk2 (Thr68), PARP, Cleaved-Caspase3, JNK, p -JNK (Thr183/Tyr185), ATM, p -ATM (Ser1981), and SKA2. (D) Western blotting analysis of BML-277 treatment in SNU638 and NUGC3 SKA2-knockdown cell lines using antibodies against cyclin D1, cyclin A2, cyclin B1, p -Chk2 (Thr68), and SKA2. (E) Western blotting analysis of P38, p-P38 (Thr180/Tyr182), ERK, p -ERK1/2 (Thr202/Tyr204), JNK, p -JNK (Thr183/Tyr185), and SKA2 expression in SNU638 and NUGC3 SKA2-knockdown cell lines. (F) Western blotting analysis of the rescue effect of SKA2 overexpression on MAPK pathway markers (ERK, p -ERK1/2, JNK, and p -JNK) in SNU638 and NUGC3 SKA2-knockdown cell lines. (G) Western blotting analysis of JNK-IN-8 treatment in SNU638 SKA2-knockdown cell lines using antibodies against PARP, cleaved-caspase3, JNK, p -JNK (Thr183/Tyr185), and SKA2. α-Tubulin was used as the internal control for all blots. Representative blotting images are shown from 3 independent experiments.

Article Snippet: KU-55933 , sangon biotech , Cat# A423600.

Techniques: Western Blot, Expressing, Knockdown, Over Expression, Control

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atm inhibitor (MedChemExpress)

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