KZL-064
KZL-064 is an orally active HDAC1 ligand that directly binds to HDAC1. KZL-064 inhibits the proliferation, migration, and invasion of hepatocellular carcinoma cells, and induces apoptosis and G2/M phase cell cycle arrest. The antiproliferative, proapoptotic, and cell cycle regulatory effects of KZL-064 are partially dependent on HDAC1, while its inhibitory effects on migration and invasion also involve HDAC1-independent mechanisms. KZL-064 is applicable to hepatocellular carcinoma research.
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- CAS. Nr.: 2773345-67-6
- Formel: C17H15F3N4O
- Molecular Weight:348.32
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Speicherung:
Please store the product under the recommended conditions in the Certificate of Analysis.
Biologische Aktivität
Beschreibung
IC50 & Target
[1]|
HDAC1 |
In Vitro
KZL-064 (2.5 or 10 nM; up to 4 days) inhibits the proliferation/viability of MHCC97-H and HUH7 cells in a time- and dose-dependent manner[1].
KZL-064 (2.0 nM; 24 h) inhibits colony formation in MHCC97-H and HUH7 cells, but does not affect the clonal growth of normal LX2 cells[1].
KZL-064 (1-2.5 nM; 24 h) exerts a significant anti-migratory effect on MHCC97-H and HUH7 hepatocellular carcinoma cells at nanomolar concentrations[1].
KZL-064 (1-2.5 nM; 24 h) significantly impairs the invasive capacity of MHCC97-H human hepatocellular carcinoma cells at low nanomolar concentrations[1].
Under the same exposure conditions, KZL-064 exerts a stronger antiproliferative effect on HDAC1-overexpressing MHCC97-H cells, while HDAC1 knockdown only slightly reduces cellular sensitivity to KZL-064; HDAC1 knockdown does not abrogate the inhibitory effect of KZL-064 on cell migration and invasion[1].
KZL-064 (1-10 nM; 1 h) directly and preferentially binds to the HDAC1 protein in MHCC97-H cells to enhance its thermal stability, and no interaction with HDAC2 or HDAC8 is detected under the same experimental conditions[1].
KZL-064 (10-50 μM) binds to recombinant HDAC1 protein in a concentration-dependent manner in BLI assays, with a KD of 7.54 × 10-5[1].
KZL-064 (2.5-10 nM; 24 h) induces G2/M phase arrest in MHCC97-H cells, a process that is partially dependent on HDAC1; even when HDAC1 expression is knocked down, this compound still retains significant anti-proliferative and pro-apoptotic activities[1].
KZL-064 (2.5 nM; 24 h) induces significant G2/M phase arrest in MHCC97-H cells, while HDAC1 knockdown partially reverses this cell cycle arrest[1].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only. Further protocols information, click here.
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Cell Line:MHCC97-H; HUH7
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Concentration:2.5, 10 nM
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Incubation Time:Up to 4 days
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Result:Reduced cell viability in a time- and dose-dependent manner in both cell lines.
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Cell Line:MHCC97-H; HUH7; LX2
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Concentration:2 nM
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Incubation Time:24 h
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Result:Suppressed colony formation in MHCC97-H and HUH7 cells.
Did not affect clonogenic growth of normal LX2 cells.
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Cell Line:MHCC97-H; HUH7
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Concentration:1 nM, 2.5 nM
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Incubation Time:24 h
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Result:Reduced migration of MHCC97-H cells.
Reduced migration of HUH7 cells.
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Cell Line:MHCC97-H
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Concentration:1 nM, 2.5 nM
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Incubation Time:24 h
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Result:Reduced invasion of MHCC97-H cells.
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Cell Line:MHCC97-H
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Concentration:2.5 nM
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Incubation Time:24 h
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Result:Induced pronounced G2/M-phase arrest.
HDAC1 knockdown partially attenuated the G2/M-phase arrest.
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Cell Line:MHCC97-H
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Concentration:2.5, 10 nM
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Incubation Time:24 h
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Result:Increased apoptosis.
Produced greater apoptosis in HDAC1-overexpressing cells.
HDAC1 knockdown partially attenuated the apoptotic response.
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Cell Line:MHCC97-H
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Concentration:1-10 nM
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Incubation Time:1 h
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Result:Increased HDAC1 thermal stability in CETSA.
Did not produce appreciable thermal stabilization of HDAC2 or HDAC8 under the tested temperature conditions.
In Vivo
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
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Animal Model:BALB/c nude mice (4-week-old male)[1]
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Dosage:0.5 μg/kg; 1.0 μg/kg; 2.0 μg/kg
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Administration:i.g.; every 2 days; 14 days
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Result:Exhibited dose-dependent tumor growth inhibition.
Showed anti-tumor efficacy comparable to sorafenib at microgram-per-kilogram doses.
Caused no reduction in mouse body weight at the highest tested dose.
Produced no significant differences in organ weight or organ histology compared to vehicle control groups.
Induced reduced tumor cellularity and increased necrotic areas in H&E stained tumor sections.
Did not alter HDAC1 expression levels, significantly reduced Ki-67 expression, and significantly elevated p53 expression in subcutaneous tumor sections.
Chemical Information
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CAS. Nr. 2773345-67-6
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Molecular Weight 348.32
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Formel C17H15F3N4O
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SMILES
COC1=CC=C(C=C1N)N(C2=NC(C(F)(F)F)=NC3=CC=CC=C32)C
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Versand
Room temperature in continental US; may vary elsewhere.
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Speicherung
Please store the product under the recommended conditions in the Certificate of Analysis.
Protokoll
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Apoptosis
Apoptosis, also called programmed cell death, is generally characterized by distinct morphological characteristics.
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TUNEL staining for apoptotic DNA fragmentation
TUNEL staining detects DNA strand breaks by using terminal deoxynucleotidyl transferase to add labeled nucleotides to exposed 3′-OH DNA termini, generating either microscopic staining in fixed cells or tissue sections, or fluorescence/cytometric signal in cell suspensions. TUNEL positivity reflects DNA fragmentation but should not be interpreted alone as definitive apoptosis, because TUNEL can also label necrotic, autolytic, mechanically damaged, or DNA-repair-associated DNA breaks.
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Flow cytometric DNA-content cell-cycle staining
Flow cytometric DNA-content cell-cycle staining measures the fluorescence intensity of DNA-bound fluorochromes in single cells or nuclei to estimate DNA content distributions, allowing assignment of populations to G0/G1, S, and G2/M phases by DNA histogram deconvolution. Propidium iodide (PI) intercalates into DNA, and PI fluorescence is proportional to cellular DNA content when staining is performed under conditions that make DNA accessible and minimize non-DNA signal. Cells with G2/M DNA content are expected to show approximately twice the fluorescence intensity of G0/G1 cells, while S-phase cells occupy intermediate fluorescence values. PI-based DNA-content analysis can also detect cells with fractional DNA content, often reported as sub-G1, when DNA fragmentation and extraction during staining reduce retained DNA signal in apoptotic cells. DAPI is an alternative DNA fluorochrome for univariate DNA-content analysis, while bivariate approaches combining DNA content with proliferation
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Annexin V plus membrane-impermeant dye apoptosis staining
Annexin V-based apoptosis assays rely on the detection of phosphatidylserine (PS) externalization from the inner leaflet of the plasma membrane to the outer leaflet, an early biochemical hallmark of apoptosis. Fluorescently labeled Annexin V binds PS in a calcium-dependent manner, enabling identification of early apoptotic cells by flow cytometry or fluorescence microscopy. When combined with a membrane-impermeant DNA-binding dye (e. g. , propidium iodide), this approach allows discrimination between viable (Annexin V−/dye−), early apoptotic (Annexin V+/dye−), and late apoptotic or necrotic (Annexin V+/dye+) cell populations by assessing membrane integrity and PS exposure.
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Cell migration
Cell migration is a method that plays an important role in wound healing, cell differentiation, embryonic development, etc.
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BrdU Incorporation Assay
Bromodeoxyuridine (BrdU) incorporation assay is based on the principle that BrdU, a thymidine analog, is incorporated into newly synthesized DNA during the S phase of the cell cycle, thereby serving as a marker of DNA replication and cellular proliferation. Incorporated BrdU can be detected using anti-BrdU antibodies following DNA denaturation, enabling visualization or quantification of proliferating cells through immunochemical detection methods such as immunofluorescence or immunohistochemistry.
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Apoptosis Solutions
Apoptosis is a regulated, generally non-lytic cell-death pathway that removes unwanted, damaged, infected, or abnormal cells through coordinated morphological changes, caspase activation, DNA fragmentation, and membrane remodeling. The intrinsic apoptosis pathway is controlled mainly by mitochondrial outer membrane permeabilization, BCL-2 family proteins, cytochrome c release, apoptosome formation, caspase-9 activation, and downstream executioner caspase-3/7 activation. The extrinsic apoptosis pathway is initiated by death receptors such as Fas, TNFR, and TRAIL receptors, which recruit adaptor proteins and activate caspase-8 before engaging executioner caspases or mitochondrial amplification through BID cleavage. Apoptosis is linked to many phenotypes, including cancer cell killing, tissue homeostasis, immune regulation, neurodegeneration, infection response, and treatment-induced cytotoxicity; unresolved questions include how apoptosis interacts with necroptosis, pyroptosis, ferroptos
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Cell invasion
Cell invasion is the ability of cells to migrate from one area to another via the extracellular matrix. Cell invasion is the response of normal and cancer cells to chemical and mechanical stimuli. Before migrating to a new region, the extracellular matrix is degraded by proteases within the cell. Cell invasion often occurs during wound repair, vascularization and inflammation, abnormal tissue invasion, and tumor cell metastasis.
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Protocol for Cell Cycle
Cell-cycle analysis by flow cytometry measures DNA content in single cells to estimate the fraction of cells in G0/G1, S, and G2/M phases. Propidium iodide intercalates into DNA, and after RNA removal with RNase, fluorescence intensity reflects cellular DNA content: 2N cells are assigned to G0/G1, cells between 2N and 4N to S phase, and 4N cells to G2/M. DNA-content analysis alone cannot reliably separate G0 from G1 or G2 from M. Ki-67 can distinguish quiescent G0 cells from cycling cells, EdU or BrdU incorporation marks active DNA synthesis in S phase, and phospho-histone H3 staining identifies mitotic cells within the 4N population.
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Liver Cancer Modeling
Liver cancer can be classified into primary liver cancer and secondary liver cancer. Secondary liver cancer is the metastatic liver cancer. Primary liver cancer includes hepatocellular carcinoma (HCC), intrahepatic cholangiocarcinoma (ICC) and fibrolamellar HCC, of which HCC is the most common form, accounting for approximately 90% of primary liver cancers[1]. HCC mouse models include chemical agent-induced models, transplanted tumor models, and genetic engineered models.
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Cell Viability Determination by MTT Colorimetric Assay
The following protocol uses the MTT colorimetric assay as a classic literature-established method for assessing cell viability/metabolic activity in cultured mammalian cells. MTT[3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] is reduced by metabolically active cells to a colored formazan product; the amount of formazan is quantified spectrophotometrically and provides an indirect measure of metabolically active viable cells. Importantly, MTT reduction reflects cellular oxidoreductase/metabolic activity rather than an absolute direct count of living cells, so changes in cellular metabolism can alter the signal independently of cell number.
Reinheit & Dokumentation
Verweise
Calculators
Konzentration (Stammlösung) × Volumen (Stammlösung) = Konzentration (Ziellösung) × Volumen (Ziellösung)