Malvidin-3-galactoside chloride
Based on 1 publication(s) in Google Scholar
Malvidin-3-galactoside chloride, an anthocyanin monomer, induces hepatocellular carcinoma (HCC) cells cycle arrest and apoptosis. Malvidin-3-galactoside chloride inhibits the production and accumulation of ROS. Malvidin-3-galactoside chloride has anti-tumor function.
For research use only. We do not sell to patients.
- Purity : 99.63%
- CAS No.: 30113-37-2
- Formula: C23H25ClO12
- Molecular Weight:528.89
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Storage:
-20°C, sealed storage, away from moisture and light
* In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture and light)
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Biological Activity
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Chemical Information
- Protocols
- Purity & Documentation
- References
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Help & FAQs
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Malvidin-3-galactoside chloride (Standard)ROS Inhibitor
Publications Citing Use of MedChemExpress (MCE) Malvidin-3-galactoside chloride
MoreAll Endogenous Metabolite Isoforms
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Biological Activity
Description
IC50 & Target
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Human Endogenous Metabolite |
In Vitro
Malvidin-3-galactoside chloride (50, 100, 200 μg/mL; for 24, 48, 72 h) displays obvious cytotoxicity on Huh-7 cells and has no significant effect with 50 and 100 μg/mL for 48 h. Malvidin-3-galactoside chloride has a notable cytotoxic effect against Huh-7 cells at 72 h[1].
Malvidin-3-galactoside chloride (50-200 μg/mL) arrests the cells in the S phase, accompanied by the cells in the G1 phase decreased, and the cells in the S phase increased[1].
Malvidin-3-galactoside chloride (50-200 μg/mL; for 72 h) induces cell apoptosis in Huh-7 cells[1].
Malvidin-3-galactoside chloride (50-200 μg/mL; for 72 h) markedly increased the levels of caspase-3, cleaved-caspase-3 and cleaved-PARP in a dose-dependent manner[1].
Malvidin-3-galactoside chloride (50-200 μg/mL; for 12 h) inhibits the production and accumulation of ROS[1].
Malvidin-3-galactoside chloride (50-200 μg/mL; for 12 h) dramatically reduces the level of phosphorylation ERK (p-ERK) in a dose-dependent manner. Malvidin-3-galactoside chloride with 200 μg/mL markedly increases the phosphorylation level of p38 and JNK (p-p38 and p-JNK)[1].
Malvidin-3-galactoside chloride (50-200 μg/mL; for 12 h) inhibits the migration and invasion in Huh-7 cells[1].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only. Further protocols information, click here.
Chemical Information
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CAS No. 30113-37-2
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Appearance Solid
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Molecular Weight 528.89
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Formula C23H25ClO12
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Color Brown to black
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SMILES
COC1=C(O)C(OC)=CC(C2=C(O[C@H]3[C@@H]([C@H]([C@H]([C@@H](CO)O3)O)O)O)C=C4C(C=C(O)C=C4O)=[O+]2)=C1.[Cl-]
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Structure Classification
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Initial Source
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Shipping
Room temperature in continental US; may vary elsewhere.
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Storage
-20°C, sealed storage, away from moisture and light
* In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture and light)
Publications (1)
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Journal Impact Factor
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Most Recent
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Food Chem
Flavonoid-mediated metabolic underpinning quality variation in red bud-sport pear mutants. [Abstract]2025 Oct 15:489:144992. PMID: 40466530
Protocols
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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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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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ROS/oxidative-stress fluorescent staining
ROS/oxidative-stress fluorescent staining uses cell-permeant fluorogenic probes that become fluorescent after oxidation inside cells or tissues; commonly used examples include DCFH-DA/DCFDA for broad cellular oxidant detection, DHE for superoxide-related signal detection, MitoSOX for mitochondrial superoxide-related signal detection, and CellROX probes for oxidative-stress-associated fluorescence readouts. The assay detects probe oxidation rather than a single ROS species unless the probe and analysis method have been chemically validated for that species. DCFH-DA enters cells, is deacetylated by intracellular esterases to DCFH, and produces fluorescent DCF after oxidation, so the readout is used as an operational measure of total cellular oxidative stress rather than a species-specific ROS measurement. DHE and MitoSOX can report superoxide-related oxidation, but red fluorescence alone can include non-specific ethidium-like oxidation products; HPLC or optimized spectral approaches are
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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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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.
Purity & Documentation
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Data Sheet (277 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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Handling Instructions (2659 KB)
References
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
Malvidin-3-galactoside chloride Related Classifications
HY-N6623 Related Classifications
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