FLT3-IN-43
FLT3-IN-43 is an orally active inhibitor of tubulin and FLT3 kinase, with an IC50 of 3.6 μM against tubulin and an IC50 of 58.6 nM against human FLT3 kinase. FLT3-IN-43 binds to the colchicine-binding site on tubulin to inhibit microtubule polymerization. FLT3-IN-43 suppresses FLT3 kinase activity. FLT3-IN-43 disrupts the cellular microtubule network. Tubulin-IN-69 induces cell cycle arrest. Tubulin-IN-69 induces tumor cell apoptosis. FLT3-IN-43 is used for research on acute myeloid leukemia and solid tumors including colorectal cancer, lung adenocarcinoma, and breast cancer.
For research use only. We do not sell to patients.
- Formula: C20H20N4O3
- Molecular Weight:364.40
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Storage:
Please store the product under the recommended conditions in the Certificate of Analysis.
Biological Activity
Description
IC50 & Target
[1]|
tubulin 3.6 μM (IC50) |
FLT3 58.6 nM (IC50) |
Cellular Effect
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Cell Line
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Type | Value | Description | References |
|---|---|---|---|---|
| HCT-116 | IC50 |
0.015 μM
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Antiproliferative activity against human HCT116 colorectal carcinoma cells assessed by MTT assay after 72 h incubation.
Antiproliferative activity against human HCT116 colorectal carcinoma cells assessed by MTT assay after 72 h incubation.
|
42571759 |
| A549 | IC50 |
0.021 μM
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Antiproliferative activity against human A549 lung adenocarcinoma cells assessed by MTT assay after 72 h incubation.
Antiproliferative activity against human A549 lung adenocarcinoma cells assessed by MTT assay after 72 h incubation.
|
42571759 |
| MDA-MB-231 | IC50 |
0.025 μM
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Antiproliferative activity against human MDA-MB-231 breast carcinoma cells assessed by MTT assay after 72 h incubation.
Antiproliferative activity against human MDA-MB-231 breast carcinoma cells assessed by MTT assay after 72 h incubation.
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42571759 |
| MOLM-13 | IC50 |
3.3 nM
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Antiproliferative activity against FLT3-ITD mutant MOLM-13 leukemia cells assessed by MTT assay after 72 h incubation.
Antiproliferative activity against FLT3-ITD mutant MOLM-13 leukemia cells assessed by MTT assay after 72 h incubation.
|
42571759 |
| MV4-11 | IC50 |
6.3 nM
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Antiproliferative activity against FLT3-ITD mutant MV4-11 leukemia cells assessed by MTT assay after 72 h incubation.
Antiproliferative activity against FLT3-ITD mutant MV4-11 leukemia cells assessed by MTT assay after 72 h incubation.
|
42571759 |
| HL-60 | IC50 |
9.9 nM
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Antiproliferative activity against FLT3 wild-type HL60 leukemia cells assessed by MTT assay after 72 h incubation.
Antiproliferative activity against FLT3 wild-type HL60 leukemia cells assessed by MTT assay after 72 h incubation.
|
42571759 |
In Vitro
FLT3-IN-43 (compound 6h) (15-25 nM; 72 h) exhibits nanomolar antiproliferative potency against HCT116, A549, and MDA-MB-231 human solid tumor cell lines, with IC50 values ranging from 15 nM to 25 nM[1].
FLT3-IN-43 (72 h) exhibits exceptionally potent antiproliferative activity against FLT3-driven leukemia cell lines, with no observable toxicity to normal human PBMC at concentrations up to 10 μM[1].
FLT3-IN-43 potently inhibits in vitro tubulin polymerization with an IC50 of 3.6 μM[1].
FLT3-IN-43 (1-10 μM; 2 h, 1.5 h) specifically occupies the colchicine binding site on tubulin in HCT116 cells[1].
FLT3-IN-43 (15-30 nM; 24 h) disrupts the cellular microtubule network of HCT116 cells in a concentration-dependent manner, inducing perinuclear contraction of microtubule structures[1].
FLT3-IN-43 40 min) is a potent, highly selective FLT3 kinase inhibitor with an IC50 of 58.6 nM, showing minimal inhibitory activity against the off-target homologous kinases c-KIT, PDGFRα, and PDGFRβ[1].
FLT3-IN-43 (15-60 nM; 8 h) effectively inhibits the FLT3 signaling pathway in MOLM-13 cells through concentration-dependent reduction of phosphorylated FLT3 and phosphorylated STAT5 protein levels[1].
FLT3-IN-43 (5-15 nM; 12-24 h) produces a sequential, time-dependent dual phase arrest phenotype in MOLM-13 cells, with early 12 h G2/M arrest characteristic of tubulin inhibition, transitioning to 24 h G0/G1 arrest characteristic of FLT3 kinase inhibition[1].
FLT3-IN-43 (5-30 nM; 24 h) induces robust, concentration-dependent apoptosis in MOLM-13 leukemia cells[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:HCT116 human colorectal carcinoma cells
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Concentration:15 nM; 30 nM
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Incubation Time:24 h
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Result:Resulted in partial collapse of the microtubule network with residual microtubule structures visible around cell nuclei at 15 nM.
Caused further disruption, with only sparse residual perinuclear microtubule structures remaining at 30 nM, producing a microtubule reorganization pattern identical to that observed with 30 nM colchicine.
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Cell Line:FLT3-ITD mutant MOLM-13 human acute myeloid leukemia cells
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Concentration:15 nM; 30 nM; 60 nM
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Incubation Time:8 h
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Result:Suppressed FLT3 phosphorylation and downstream STAT5 phosphorylation in MOLM-13 cells in a clear dose-dependent manner, an effect not observed for the pure tubulin inhibitor colchicine.
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Cell Line:FLT3-ITD mutant MOLM-13 human acute myeloid leukemia cells
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Concentration:5 nM; 10 nM; 15 nM
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Incubation Time:12 h; 24 h
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Result:Increased the proportion of MOLM-13 cells arrested at the G2/M phase from 14.83% in untreated control cells to 41.50% after 12 h of treatment.
Increased the proportion of cells arrested at the G0/G1 phase from 56.96% in untreated control cells to 77.00% after 24 h of treatment.
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Cell Line:FLT3-ITD mutant MOLM-13 human acute myeloid leukemia cells
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Concentration:5 nM; 15 nM; 30 nM
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Incubation Time:24 h
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Result:Increased the percentage of apoptotic MOLM-13 cells in a concentration-dependent manner, raising the apoptosis rate from 1.62% in vehicle control cells to 3.29% at 5 nM, 30.78% at 15 nM, and 49.06% at 30 nM.
Parmacokinetics
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 female)[1]
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Dosage:15 mg/kg; 30 mg/kg
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Administration:p.o.; once daily; 21 consecutive days
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Result:Achieved 63% inhibition of tumor growth at 30 mg/kg dose relative to the vehicle control group.
Showed no notable body weight loss in any treatment group relative to the control.
Revealed no significant pathological lesions or notable organ toxicity in H&E stained histopathological sections of heart, liver, and kidney tissues under the experimental conditions.
Chemical Information
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Molecular Weight 364.40
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Formula C20H20N4O3
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SMILES
COC1=C(OC)C(OC)=CC(NC2=NNC(C3=CC=CC4=C3C=CN4)=C2)=C1
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Shipping
Room temperature in continental US; may vary elsewhere.
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Storage
Please store the product under the recommended conditions in the Certificate of Analysis.
Protocols
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Kinase activity and phosphorylation assays
Kinase activity assays measure the ability of kinases to transfer phosphate groups from ATP to specific substrates, while phosphorylation assays detect the presence and levels of phosphorylated proteins. Common methods include radiolabeled ATP incorporation (e. g. ,), ADP release detection via bioluminescence (e. g. ,[3]), enzyme-linked immunosorbent assays (ELISA) for phospho-specific epitopes (e. g. ,[6]), and microtiter-based formats for high-throughput screening (e. g. ,[8]). The ADP-Glo assay quantifies kinase activity by measuring ADP produced during phosphorylation using a luciferase-based system. Radiometric assays involve autoradiography or scintillation counting after incorporation of 32P-labeled ATP into substrate proteins. ELISA-based approaches rely on phospho-specific antibodies to detect activated kinases in cell lysates or purified samples.
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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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Cell Cytotoxicity Assay
Cytotoxicity assays are usually based on the assessment of cell membrane damage, which can also be indirectly detected by measuring cell viability. Detection methods include MTT assay, CKK-8 assay, LDH assay and ATP assay, etc.
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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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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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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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Protocol for Kinase activity and phosphorylation assays
Kinase activity assays measure transfer of phosphate from ATP to a protein or peptide substrate, generating phosphorylated substrate, ADP, or incorporated radiolabeled phosphate as the readout; phosphorylation assays measure site-specific phosphorylation in cells or tissues as a proxy for kinase-pathway activation, inhibition, or substrate regulation. Phosphorylation can be detected by phospho-specific Western blot, immunoprecipitation kinase assay, phospho-immunofluorescence, phospho-flow cytometry, luminescent ADP detection, radiolabeled ATP incorporation, or reporter-based pathway assays, and these readouts can be applied to cancer cells, primary neurons, mouse tumors, organoids, inflammatory macrophages, ferroptosis studies, and mitophagy studies when the kinase target is biologically relevant.
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Breast Cancer Modeling
Breast cancer is a heterogeneous cancer, and it has been distinguished into four subtypes: luminal A, luminal B, HER2-positive and basal-like. Molecular mutations, epigenetic alterations, hormone exposure and immune microenvironment are related to the progression of breast cancer.
Purity & Documentation
References
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)