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ldn 57444  (MedChemExpress)


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    Structured Review

    MedChemExpress ldn 57444
    USP20 directly interacts with GPX4. ( A ) Immunoblot analysis of target proteins in sorafenib-resistant 769-P and A549 cells following 24 h treatment with specific deubiquitinase inhibitors. ML-323: 10 μM, GSK2643943A: 10 μM, XL177A: 10 μM, Spautin-1: 10 μM, IU1: 10 μM, AZ1: 10 μM, MF-094: 10 μM, <t>LDN-57444:</t> 10 μM, TCID: 10 μM, PR-619: 10 μM, BAY11-7082: 10 μM, EOAI3402143: 2.5 μM, ML364: 10 μM, b-AP15: 0.5 μM. ( B ) HEK293T cells were transfected with GST-GPX4 and Flag-USP. The cell lysate was applied with GST pull-down, then analyzed with immunoblot for indicated proteins. ( C ) 769-P and A549 cells were subjected to immunoprecipitate with anti-GPX4 antibodies, then analyzed with immunoblot for indicated proteins. ( D ) Overview of USP20 structures. ( E-F ) HEK293T cells transfected with the indicated USP20 structures and Flag-GPX4 were subjected to pull-down with GSH beads or immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( G ) 769-P and A549 cells were subjected to subcellular fractionation, then analyzed with immunoblot for indicated proteins. ( H ) Overview of GPX4 isoforms structures. ( I ) HEK293T cells transfected with the indicated GPX4 isoforms and GST-USP20 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( J ) HEK293T cells transfected with the GST-USP20 WT/C154S and Flag-GPX4 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins.
    Ldn 57444, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ldn 57444 - by Bioz Stars, 2026-07
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    Images

    1) Product Images from "USP20 governs tyrosine kinase inhibitors resistance through ferroptosis evasion by targeting GPX4 in cancers"

    Article Title: USP20 governs tyrosine kinase inhibitors resistance through ferroptosis evasion by targeting GPX4 in cancers

    Journal: Redox Biology

    doi: 10.1016/j.redox.2026.104086

    USP20 directly interacts with GPX4. ( A ) Immunoblot analysis of target proteins in sorafenib-resistant 769-P and A549 cells following 24 h treatment with specific deubiquitinase inhibitors. ML-323: 10 μM, GSK2643943A: 10 μM, XL177A: 10 μM, Spautin-1: 10 μM, IU1: 10 μM, AZ1: 10 μM, MF-094: 10 μM, LDN-57444: 10 μM, TCID: 10 μM, PR-619: 10 μM, BAY11-7082: 10 μM, EOAI3402143: 2.5 μM, ML364: 10 μM, b-AP15: 0.5 μM. ( B ) HEK293T cells were transfected with GST-GPX4 and Flag-USP. The cell lysate was applied with GST pull-down, then analyzed with immunoblot for indicated proteins. ( C ) 769-P and A549 cells were subjected to immunoprecipitate with anti-GPX4 antibodies, then analyzed with immunoblot for indicated proteins. ( D ) Overview of USP20 structures. ( E-F ) HEK293T cells transfected with the indicated USP20 structures and Flag-GPX4 were subjected to pull-down with GSH beads or immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( G ) 769-P and A549 cells were subjected to subcellular fractionation, then analyzed with immunoblot for indicated proteins. ( H ) Overview of GPX4 isoforms structures. ( I ) HEK293T cells transfected with the indicated GPX4 isoforms and GST-USP20 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( J ) HEK293T cells transfected with the GST-USP20 WT/C154S and Flag-GPX4 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins.
    Figure Legend Snippet: USP20 directly interacts with GPX4. ( A ) Immunoblot analysis of target proteins in sorafenib-resistant 769-P and A549 cells following 24 h treatment with specific deubiquitinase inhibitors. ML-323: 10 μM, GSK2643943A: 10 μM, XL177A: 10 μM, Spautin-1: 10 μM, IU1: 10 μM, AZ1: 10 μM, MF-094: 10 μM, LDN-57444: 10 μM, TCID: 10 μM, PR-619: 10 μM, BAY11-7082: 10 μM, EOAI3402143: 2.5 μM, ML364: 10 μM, b-AP15: 0.5 μM. ( B ) HEK293T cells were transfected with GST-GPX4 and Flag-USP. The cell lysate was applied with GST pull-down, then analyzed with immunoblot for indicated proteins. ( C ) 769-P and A549 cells were subjected to immunoprecipitate with anti-GPX4 antibodies, then analyzed with immunoblot for indicated proteins. ( D ) Overview of USP20 structures. ( E-F ) HEK293T cells transfected with the indicated USP20 structures and Flag-GPX4 were subjected to pull-down with GSH beads or immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( G ) 769-P and A549 cells were subjected to subcellular fractionation, then analyzed with immunoblot for indicated proteins. ( H ) Overview of GPX4 isoforms structures. ( I ) HEK293T cells transfected with the indicated GPX4 isoforms and GST-USP20 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( J ) HEK293T cells transfected with the GST-USP20 WT/C154S and Flag-GPX4 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins.

    Techniques Used: Western Blot, Transfection, Fractionation



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    MedChemExpress ldn 57444
    USP20 directly interacts with GPX4. ( A ) Immunoblot analysis of target proteins in sorafenib-resistant 769-P and A549 cells following 24 h treatment with specific deubiquitinase inhibitors. ML-323: 10 μM, GSK2643943A: 10 μM, XL177A: 10 μM, Spautin-1: 10 μM, IU1: 10 μM, AZ1: 10 μM, MF-094: 10 μM, <t>LDN-57444:</t> 10 μM, TCID: 10 μM, PR-619: 10 μM, BAY11-7082: 10 μM, EOAI3402143: 2.5 μM, ML364: 10 μM, b-AP15: 0.5 μM. ( B ) HEK293T cells were transfected with GST-GPX4 and Flag-USP. The cell lysate was applied with GST pull-down, then analyzed with immunoblot for indicated proteins. ( C ) 769-P and A549 cells were subjected to immunoprecipitate with anti-GPX4 antibodies, then analyzed with immunoblot for indicated proteins. ( D ) Overview of USP20 structures. ( E-F ) HEK293T cells transfected with the indicated USP20 structures and Flag-GPX4 were subjected to pull-down with GSH beads or immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( G ) 769-P and A549 cells were subjected to subcellular fractionation, then analyzed with immunoblot for indicated proteins. ( H ) Overview of GPX4 isoforms structures. ( I ) HEK293T cells transfected with the indicated GPX4 isoforms and GST-USP20 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( J ) HEK293T cells transfected with the GST-USP20 WT/C154S and Flag-GPX4 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins.
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    Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and <t>trichostatin</t> <t>A</t> (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1
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    PR-619 DUB inhibitor decreased HIF2α protein level. (A) The list of DUB inhibitors in our study. DUB inhibitors including: ML323, ML364, EOAI3402143, XL117A, DUBs-IN-2, Spautin-1, IU1, GSK2643943, AZ1, MF-094, <t>LDN-57444,</t> TCID, PR-619, BAY117082, b-AP15. (B) EPAS1 gene status in OS-RC-2, 786-O, SW839, and ACHN, respectively. (C) HIF2α protein level was tested by WB after DUB inhibitors treatment in OS-RC-2 cells. (D) The effects of 5 candidate DUB inhibitors on HIF2α protein expression were further tested in 786-O and SW839 cells. HIF2α protein expression was tested by WB. Five candidate DUB inhibitors were ML364, DUBs-IN-2, GSK2643943, LDN-57444, and PR-619. DUB, deubiquitinating enzyme; HIF2α, hypoxia inducible factor 2α; WB, Western blotting.
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    PR-619 DUB inhibitor decreased HIF2α protein level. (A) The list of DUB inhibitors in our study. DUB inhibitors including: ML323, ML364, EOAI3402143, XL117A, DUBs-IN-2, Spautin-1, IU1, GSK2643943, AZ1, <t>MF-094,</t> LDN-57444, TCID, PR-619, BAY117082, b-AP15. (B) EPAS1 gene status in OS-RC-2, 786-O, SW839, and ACHN, respectively. (C) HIF2α protein level was tested by WB after DUB inhibitors treatment in OS-RC-2 cells. (D) The effects of 5 candidate DUB inhibitors on HIF2α protein expression were further tested in 786-O and SW839 cells. HIF2α protein expression was tested by WB. Five candidate DUB inhibitors were ML364, DUBs-IN-2, GSK2643943, LDN-57444, and PR-619. DUB, deubiquitinating enzyme; HIF2α, hypoxia inducible factor 2α; WB, Western blotting.
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    PR-619 DUB inhibitor decreased HIF2α protein level. (A) The list of DUB inhibitors in our study. DUB inhibitors including: ML323, ML364, EOAI3402143, XL117A, DUBs-IN-2, Spautin-1, IU1, GSK2643943, AZ1, <t>MF-094,</t> LDN-57444, TCID, PR-619, BAY117082, b-AP15. (B) EPAS1 gene status in OS-RC-2, 786-O, SW839, and ACHN, respectively. (C) HIF2α protein level was tested by WB after DUB inhibitors treatment in OS-RC-2 cells. (D) The effects of 5 candidate DUB inhibitors on HIF2α protein expression were further tested in 786-O and SW839 cells. HIF2α protein expression was tested by WB. Five candidate DUB inhibitors were ML364, DUBs-IN-2, GSK2643943, LDN-57444, and PR-619. DUB, deubiquitinating enzyme; HIF2α, hypoxia inducible factor 2α; WB, Western blotting.
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    Image Search Results


    USP20 directly interacts with GPX4. ( A ) Immunoblot analysis of target proteins in sorafenib-resistant 769-P and A549 cells following 24 h treatment with specific deubiquitinase inhibitors. ML-323: 10 μM, GSK2643943A: 10 μM, XL177A: 10 μM, Spautin-1: 10 μM, IU1: 10 μM, AZ1: 10 μM, MF-094: 10 μM, LDN-57444: 10 μM, TCID: 10 μM, PR-619: 10 μM, BAY11-7082: 10 μM, EOAI3402143: 2.5 μM, ML364: 10 μM, b-AP15: 0.5 μM. ( B ) HEK293T cells were transfected with GST-GPX4 and Flag-USP. The cell lysate was applied with GST pull-down, then analyzed with immunoblot for indicated proteins. ( C ) 769-P and A549 cells were subjected to immunoprecipitate with anti-GPX4 antibodies, then analyzed with immunoblot for indicated proteins. ( D ) Overview of USP20 structures. ( E-F ) HEK293T cells transfected with the indicated USP20 structures and Flag-GPX4 were subjected to pull-down with GSH beads or immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( G ) 769-P and A549 cells were subjected to subcellular fractionation, then analyzed with immunoblot for indicated proteins. ( H ) Overview of GPX4 isoforms structures. ( I ) HEK293T cells transfected with the indicated GPX4 isoforms and GST-USP20 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( J ) HEK293T cells transfected with the GST-USP20 WT/C154S and Flag-GPX4 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins.

    Journal: Redox Biology

    Article Title: USP20 governs tyrosine kinase inhibitors resistance through ferroptosis evasion by targeting GPX4 in cancers

    doi: 10.1016/j.redox.2026.104086

    Figure Lengend Snippet: USP20 directly interacts with GPX4. ( A ) Immunoblot analysis of target proteins in sorafenib-resistant 769-P and A549 cells following 24 h treatment with specific deubiquitinase inhibitors. ML-323: 10 μM, GSK2643943A: 10 μM, XL177A: 10 μM, Spautin-1: 10 μM, IU1: 10 μM, AZ1: 10 μM, MF-094: 10 μM, LDN-57444: 10 μM, TCID: 10 μM, PR-619: 10 μM, BAY11-7082: 10 μM, EOAI3402143: 2.5 μM, ML364: 10 μM, b-AP15: 0.5 μM. ( B ) HEK293T cells were transfected with GST-GPX4 and Flag-USP. The cell lysate was applied with GST pull-down, then analyzed with immunoblot for indicated proteins. ( C ) 769-P and A549 cells were subjected to immunoprecipitate with anti-GPX4 antibodies, then analyzed with immunoblot for indicated proteins. ( D ) Overview of USP20 structures. ( E-F ) HEK293T cells transfected with the indicated USP20 structures and Flag-GPX4 were subjected to pull-down with GSH beads or immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( G ) 769-P and A549 cells were subjected to subcellular fractionation, then analyzed with immunoblot for indicated proteins. ( H ) Overview of GPX4 isoforms structures. ( I ) HEK293T cells transfected with the indicated GPX4 isoforms and GST-USP20 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins. ( J ) HEK293T cells transfected with the GST-USP20 WT/C154S and Flag-GPX4 were subjected to immunoprecipitate with anti-Flag antibody, then analyzed with immunoblot for indicated proteins.

    Article Snippet: Sunitinib (cat. no. HY-10255A), Ferrostatin-1 (Fer-1; cat. no. HY-100579), IKE (cat. no. HY-114481), RSL3 (cat. no. HY-100218A), MG-132 (cat. no. HY-13259), Chloroquine (CQ; cat. no. HY-17589A), SAS (cat. no. HY-14655), artemisinin (cat. no. HY-B0094), ML-323 (cat. no. HY-17543), XL177A (cat. no. HY-138794), Spautin-1 (cat. no. HY-12990), IU1 (cat. no. HY-13817), AZ1 (cat. no. HY-117370), MF-094 (cat. no. HY-112438), LDN-57444 (cat. no. HY-18637), TCID (cat. no. HY-18638), PR-619 (cat. no. HY-13814), BAY11-7082 (cat. no. HY-13453), EOAI3402143 (cat. no. HY-111408), ML364 (cat. no. HY-100900), and b-AP15 (cat. no. HY-13989) were purchased from MedChemExpress.

    Techniques: Western Blot, Transfection, Fractionation

    Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and trichostatin A (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1

    Journal: Biology Direct

    Article Title: LDN-57444 sensitizes hepatocellular carcinoma cells to sorafenib by promoting ferroptosis through histone deacetylase 2 (HDAC2) inhibition

    doi: 10.1186/s13062-026-00735-1

    Figure Lengend Snippet: Binding analysis of LDN-57444 with HDAC2. (A) Chemical structures and molecular weights (MW) of LDN-57444, BindingDB compounds, and trichostatin A (TSA). (B , C) Molecular docking simulations of the drugs with HDAC2 were conducted using iGEMDOCK software. The HDAC2 structure (PDB ID: 4LXZ) was obtained from the Protein Data Bank. The binding site was prepared with a 10 Å radius, and energy-minimized compounds were introduced into the simulation. Docking protocols included 80 generations per ligand and a population size of 300 random individuals. Conformations were generated 10 times using a genetic evolutionary algorithm, and total fitness energy was calculated as the sum of van der Waals, hydrogen bonding, and electrostatic energies, where applicable ( B ). Docking energies highlighted in green or grey indicate stronger drug binding to specific amino acid residues. Representative docking poses for each compound bound to HDAC2 are depicted ( C ). (D) Hep3B cells were treated with 40 µM LDN-57444 or 10 µM TSA for 1 h, and a cellular thermal shift assay (CETSA) was performed to evaluate the thermal stability of HDAC1, HDAC2, and UCH-L1

    Article Snippet: Erastin (#HY-15763), LDN-57444 (#HY-18637), and trichostatin A (#HY-15144) were purchased from MedChemExpress.

    Techniques: Binding Assay, Software, Generated, Thermal Shift Assay

    PR-619 DUB inhibitor decreased HIF2α protein level. (A) The list of DUB inhibitors in our study. DUB inhibitors including: ML323, ML364, EOAI3402143, XL117A, DUBs-IN-2, Spautin-1, IU1, GSK2643943, AZ1, MF-094, LDN-57444, TCID, PR-619, BAY117082, b-AP15. (B) EPAS1 gene status in OS-RC-2, 786-O, SW839, and ACHN, respectively. (C) HIF2α protein level was tested by WB after DUB inhibitors treatment in OS-RC-2 cells. (D) The effects of 5 candidate DUB inhibitors on HIF2α protein expression were further tested in 786-O and SW839 cells. HIF2α protein expression was tested by WB. Five candidate DUB inhibitors were ML364, DUBs-IN-2, GSK2643943, LDN-57444, and PR-619. DUB, deubiquitinating enzyme; HIF2α, hypoxia inducible factor 2α; WB, Western blotting.

    Journal: Translational Andrology and Urology

    Article Title: USP10 regulates HIF2α stability by deubiquitinating HIF2α regardless of VHL status in kidney cancer

    doi: 10.21037/tau-2025-aw-778

    Figure Lengend Snippet: PR-619 DUB inhibitor decreased HIF2α protein level. (A) The list of DUB inhibitors in our study. DUB inhibitors including: ML323, ML364, EOAI3402143, XL117A, DUBs-IN-2, Spautin-1, IU1, GSK2643943, AZ1, MF-094, LDN-57444, TCID, PR-619, BAY117082, b-AP15. (B) EPAS1 gene status in OS-RC-2, 786-O, SW839, and ACHN, respectively. (C) HIF2α protein level was tested by WB after DUB inhibitors treatment in OS-RC-2 cells. (D) The effects of 5 candidate DUB inhibitors on HIF2α protein expression were further tested in 786-O and SW839 cells. HIF2α protein expression was tested by WB. Five candidate DUB inhibitors were ML364, DUBs-IN-2, GSK2643943, LDN-57444, and PR-619. DUB, deubiquitinating enzyme; HIF2α, hypoxia inducible factor 2α; WB, Western blotting.

    Article Snippet: ML323 (cat#S7529), ML364 (cat#S6748), EOAI3402143 (cat#S6877), XL117A (cat#S8967), DUBs-IN-2 (cat#E0389); Spautin-1 (cat#S7888), IU1 (cat#S7134), GSK2643943 (cat#S6878), AZ1 (cat#S8904), MF-094 (cat#E1098), LDN-57444 (cat#S7135), TCID (cat#S7140), PR-619 (cat#S7130), BAY 11-7082 (cat#S2913), b-AP15 (cat#S4920), and MG132 (cat#S2619) were all purchased from Selleckchem (Shanghai, China).

    Techniques: Expressing, Western Blot

    PR-619 DUB inhibitor decreased HIF2α protein level. (A) The list of DUB inhibitors in our study. DUB inhibitors including: ML323, ML364, EOAI3402143, XL117A, DUBs-IN-2, Spautin-1, IU1, GSK2643943, AZ1, MF-094, LDN-57444, TCID, PR-619, BAY117082, b-AP15. (B) EPAS1 gene status in OS-RC-2, 786-O, SW839, and ACHN, respectively. (C) HIF2α protein level was tested by WB after DUB inhibitors treatment in OS-RC-2 cells. (D) The effects of 5 candidate DUB inhibitors on HIF2α protein expression were further tested in 786-O and SW839 cells. HIF2α protein expression was tested by WB. Five candidate DUB inhibitors were ML364, DUBs-IN-2, GSK2643943, LDN-57444, and PR-619. DUB, deubiquitinating enzyme; HIF2α, hypoxia inducible factor 2α; WB, Western blotting.

    Journal: Translational Andrology and Urology

    Article Title: USP10 regulates HIF2α stability by deubiquitinating HIF2α regardless of VHL status in kidney cancer

    doi: 10.21037/tau-2025-aw-778

    Figure Lengend Snippet: PR-619 DUB inhibitor decreased HIF2α protein level. (A) The list of DUB inhibitors in our study. DUB inhibitors including: ML323, ML364, EOAI3402143, XL117A, DUBs-IN-2, Spautin-1, IU1, GSK2643943, AZ1, MF-094, LDN-57444, TCID, PR-619, BAY117082, b-AP15. (B) EPAS1 gene status in OS-RC-2, 786-O, SW839, and ACHN, respectively. (C) HIF2α protein level was tested by WB after DUB inhibitors treatment in OS-RC-2 cells. (D) The effects of 5 candidate DUB inhibitors on HIF2α protein expression were further tested in 786-O and SW839 cells. HIF2α protein expression was tested by WB. Five candidate DUB inhibitors were ML364, DUBs-IN-2, GSK2643943, LDN-57444, and PR-619. DUB, deubiquitinating enzyme; HIF2α, hypoxia inducible factor 2α; WB, Western blotting.

    Article Snippet: ML323 (cat#S7529), ML364 (cat#S6748), EOAI3402143 (cat#S6877), XL117A (cat#S8967), DUBs-IN-2 (cat#E0389); Spautin-1 (cat#S7888), IU1 (cat#S7134), GSK2643943 (cat#S6878), AZ1 (cat#S8904), MF-094 (cat#E1098), LDN-57444 (cat#S7135), TCID (cat#S7140), PR-619 (cat#S7130), BAY 11-7082 (cat#S2913), b-AP15 (cat#S4920), and MG132 (cat#S2619) were all purchased from Selleckchem (Shanghai, China).

    Techniques: Expressing, Western Blot