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body weight topotecan accord  (MedChemExpress)


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    MedChemExpress body weight topotecan accord
    Body Weight Topotecan Accord, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/body weight topotecan accord/product/MedChemExpress
    Average 94 stars, based on 33 article reviews
    body weight topotecan accord - by Bioz Stars, 2026-03
    94/100 stars

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    Influence of KSQ‐4279 on AKT and ERK transduction and analysis of KSQ‐4279 binding with ABCB1/ABCG2/ABCC1. ( A ) Western blot showed the action of KSQ‐4279 on AKT and ERK transduction. GAPDH was as an input control. ( B ) Bar graphs for the relative protein expression of the various signaling molecules detected in (A). Data were reported as mean ± SD (* p < 0.05; ** p < 0.01; *** p < 0.001). ( C ) Binding of KSQ‐4279 with ABCB1, ABCG2, and ABCC1 were assessed by CETSAs. Aliquots of cell lysates incubated with DMSO or KSQ‐4279 (10 µM) were heated at indicated temperatures, and the presence of KSQ‐4279‐bound ABCB1/ABCG2/ABCC1 proteins was analyzed via western blots. ( D ) Molecular docking of (a and b) KSQ‐4279, (c) paclitaxel, and (d) vincristine with to substrate‐binding region of ABCB1. ( E ) Molecular docking of (a and b) KSQ‐4279, (c) mitoxantrone, and (d) <t>topotecan</t> to the substrate‐binding area of ABCG2. ( F ) Molecular docking of (a and b) KSQ‐4279, and (c) doxorubicin to the substrate‐binding domain of ABCC1. Molecular 3D structures were obtained from the web of PubChem ( https://pubchem.ncbi.nlm.nih.gov/ ), and the crystal structures of ABC transporters were obtained from the web of Protein Data Bank ( https://www.rcsb.org/ ). The docking was performed by using software of AutoDock Vina.
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    Influence of KSQ‐4279 on AKT and ERK transduction and analysis of KSQ‐4279 binding with ABCB1/ABCG2/ABCC1. ( A ) Western blot showed the action of KSQ‐4279 on AKT and ERK transduction. GAPDH was as an input control. ( B ) Bar graphs for the relative protein expression of the various signaling molecules detected in (A). Data were reported as mean ± SD (* p < 0.05; ** p < 0.01; *** p < 0.001). ( C ) Binding of KSQ‐4279 with ABCB1, ABCG2, and ABCC1 were assessed by CETSAs. Aliquots of cell lysates incubated with DMSO or KSQ‐4279 (10 µM) were heated at indicated temperatures, and the presence of KSQ‐4279‐bound ABCB1/ABCG2/ABCC1 proteins was analyzed via western blots. ( D ) Molecular docking of (a and b) KSQ‐4279, (c) paclitaxel, and (d) vincristine with to substrate‐binding region of ABCB1. ( E ) Molecular docking of (a and b) KSQ‐4279, (c) mitoxantrone, and (d) <t>topotecan</t> to the substrate‐binding area of ABCG2. ( F ) Molecular docking of (a and b) KSQ‐4279, and (c) doxorubicin to the substrate‐binding domain of ABCC1. Molecular 3D structures were obtained from the web of PubChem ( https://pubchem.ncbi.nlm.nih.gov/ ), and the crystal structures of ABC transporters were obtained from the web of Protein Data Bank ( https://www.rcsb.org/ ). The docking was performed by using software of AutoDock Vina.
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    Influence of KSQ‐4279 on AKT and ERK transduction and analysis of KSQ‐4279 binding with ABCB1/ABCG2/ABCC1. ( A ) Western blot showed the action of KSQ‐4279 on AKT and ERK transduction. GAPDH was as an input control. ( B ) Bar graphs for the relative protein expression of the various signaling molecules detected in (A). Data were reported as mean ± SD (* p < 0.05; ** p < 0.01; *** p < 0.001). ( C ) Binding of KSQ‐4279 with ABCB1, ABCG2, and ABCC1 were assessed by CETSAs. Aliquots of cell lysates incubated with DMSO or KSQ‐4279 (10 µM) were heated at indicated temperatures, and the presence of KSQ‐4279‐bound ABCB1/ABCG2/ABCC1 proteins was analyzed via western blots. ( D ) Molecular docking of (a and b) KSQ‐4279, (c) paclitaxel, and (d) vincristine with to substrate‐binding region of ABCB1. ( E ) Molecular docking of (a and b) KSQ‐4279, (c) mitoxantrone, and (d) <t>topotecan</t> to the substrate‐binding area of ABCG2. ( F ) Molecular docking of (a and b) KSQ‐4279, and (c) doxorubicin to the substrate‐binding domain of ABCC1. Molecular 3D structures were obtained from the web of PubChem ( https://pubchem.ncbi.nlm.nih.gov/ ), and the crystal structures of ABC transporters were obtained from the web of Protein Data Bank ( https://www.rcsb.org/ ). The docking was performed by using software of AutoDock Vina.
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    Influence of KSQ‐4279 on AKT and ERK transduction and analysis of KSQ‐4279 binding with ABCB1/ABCG2/ABCC1. ( A ) Western blot showed the action of KSQ‐4279 on AKT and ERK transduction. GAPDH was as an input control. ( B ) Bar graphs for the relative protein expression of the various signaling molecules detected in (A). Data were reported as mean ± SD (* p < 0.05; ** p < 0.01; *** p < 0.001). ( C ) Binding of KSQ‐4279 with ABCB1, ABCG2, and ABCC1 were assessed by CETSAs. Aliquots of cell lysates incubated with DMSO or KSQ‐4279 (10 µM) were heated at indicated temperatures, and the presence of KSQ‐4279‐bound ABCB1/ABCG2/ABCC1 proteins was analyzed via western blots. ( D ) Molecular docking of (a and b) KSQ‐4279, (c) paclitaxel, and (d) vincristine with to substrate‐binding region of ABCB1. ( E ) Molecular docking of (a and b) KSQ‐4279, (c) mitoxantrone, and (d) topotecan to the substrate‐binding area of ABCG2. ( F ) Molecular docking of (a and b) KSQ‐4279, and (c) doxorubicin to the substrate‐binding domain of ABCC1. Molecular 3D structures were obtained from the web of PubChem ( https://pubchem.ncbi.nlm.nih.gov/ ), and the crystal structures of ABC transporters were obtained from the web of Protein Data Bank ( https://www.rcsb.org/ ). The docking was performed by using software of AutoDock Vina.

    Journal: MedComm

    Article Title: KSQ‐4279, an Inhibitor of Ubiquitin Specific Peptidase 1, Enhanced the Chemotherapeutic Efficacy in ABCB1/ABCG2/ABCC1‐Mediated Multidrug Resistant Cancers

    doi: 10.1002/mco2.70517

    Figure Lengend Snippet: Influence of KSQ‐4279 on AKT and ERK transduction and analysis of KSQ‐4279 binding with ABCB1/ABCG2/ABCC1. ( A ) Western blot showed the action of KSQ‐4279 on AKT and ERK transduction. GAPDH was as an input control. ( B ) Bar graphs for the relative protein expression of the various signaling molecules detected in (A). Data were reported as mean ± SD (* p < 0.05; ** p < 0.01; *** p < 0.001). ( C ) Binding of KSQ‐4279 with ABCB1, ABCG2, and ABCC1 were assessed by CETSAs. Aliquots of cell lysates incubated with DMSO or KSQ‐4279 (10 µM) were heated at indicated temperatures, and the presence of KSQ‐4279‐bound ABCB1/ABCG2/ABCC1 proteins was analyzed via western blots. ( D ) Molecular docking of (a and b) KSQ‐4279, (c) paclitaxel, and (d) vincristine with to substrate‐binding region of ABCB1. ( E ) Molecular docking of (a and b) KSQ‐4279, (c) mitoxantrone, and (d) topotecan to the substrate‐binding area of ABCG2. ( F ) Molecular docking of (a and b) KSQ‐4279, and (c) doxorubicin to the substrate‐binding domain of ABCC1. Molecular 3D structures were obtained from the web of PubChem ( https://pubchem.ncbi.nlm.nih.gov/ ), and the crystal structures of ABC transporters were obtained from the web of Protein Data Bank ( https://www.rcsb.org/ ). The docking was performed by using software of AutoDock Vina.

    Article Snippet: Doxorubicin (HY‐15142A), paclitaxel (HY‐B0015), vincristine (HY‐N0488), topotecan (HY‐13768), and verapamil (HY‐14275) were from supplier of MedChem Express (Monmouth Junction, NJ, USA).

    Techniques: Transduction, Binding Assay, Western Blot, Control, Expressing, Incubation, Software

    Journal: Cell Reports Medicine

    Article Title: CAN-Scan: A multi-omic phenotype-driven precision oncology platform identifies prognostic biomarkers of therapy response for colorectal cancer

    doi: 10.1016/j.xcrm.2025.102053

    Figure Lengend Snippet:

    Article Snippet: Topotecan Hydrochloride , MedChemExpress , Cat# HY-13768A.

    Techniques: Recombinant, Red Blood Cell Lysis, Sequencing, Software