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    ATCC cells
    Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/hepg2+c3a+cells/C3A+(HepG2%2FC3A)%3B+Hepatocellular+Carcinoma%3B+Human/pm41735377-214-25-29
    Average 94 stars, based on 2 article reviews
    cells - by Bioz Stars, 2026-10
    94/100 stars

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    Modification:

    Article Title: Proliferative Cell Targeting and Epithelial Cell Turnover Fuels Hepatitis E Virus Replication in Human Intestinal Enteroids
    Article Snippet: HIEs culture and experimentation was performed under the approval of the Ethical Committee comite KU Leuven (approval number G-2024-8519-R2(AMD). .. HepG2/C3A cells (ATCC CRL-10741) were cultivated in Dulbecco's Modified Eagle Medium (DMEM, Gibco), supplemented with 10% inactivated fetal bovine serum (FBS, Gibco), 2 mM L-glutamine (Gibco), 0.75 g/L sodium bicarbonate (Gibco) and 1 mM sodium pyruvate (Gibco). .. For seeding of HepG2/C3A cells, plates were coated with 100 μg/mL rat tail collagen (Sigma-Aldrich) and 0.02 M glacial acetic acid in PBS for a minimum of 2 h at 37 °C.

    other:

    Article Title: Compositions for the treatment of Fabry disease
    Article Snippet: Variant #21 Expression Vector Produces Plasma α-Gal a Activity In Vitro and In Vivo The levels and activity of secreted human α-Gal A were evaluated in various mouse, cynomolgus monkey and human primary cells and cell lines after transduction with variant #4 or variant #21 expression vectors.



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    (A) Global histone succinylation measured by LC-MS/MS <t>in</t> <t>HepG2/C3A</t> cells following 48 hours of sodium succinate treatment. (B) Global histone succinylation in 3D cultured HepG2/C3A spheroids following 48 hours and 1 week of sodium succinate treatment. (C) Comparison of the relative abundance of succinyl-lysine residues in H3 and H4, in either treated or untreated, cultured cells (2D) or spheroids (3D). (D) Structure of the nucleosome with H3K64 residues highlighted to demonstrate solvent accessibility. (E) Abundance of succinyl-CoA in the nuclear fraction (left) and non-nuclear fraction (right) following sodium succinate treatment. (F) Total count of HepG2/C3A cells treated with 10 mM sodium succinate continuously for 48 to 144 hours, cell count taken every 48 hours. Data are shown as mean ± SEM; * p-value <0 . 05 in two-tailed Student’s t-test .
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    (A) Global histone succinylation measured by LC-MS/MS in HepG2/C3A cells following 48 hours of sodium succinate treatment. (B) Global histone succinylation in 3D cultured HepG2/C3A spheroids following 48 hours and 1 week of sodium succinate treatment. (C) Comparison of the relative abundance of succinyl-lysine residues in H3 and H4, in either treated or untreated, cultured cells (2D) or spheroids (3D). (D) Structure of the nucleosome with H3K64 residues highlighted to demonstrate solvent accessibility. (E) Abundance of succinyl-CoA in the nuclear fraction (left) and non-nuclear fraction (right) following sodium succinate treatment. (F) Total count of HepG2/C3A cells treated with 10 mM sodium succinate continuously for 48 to 144 hours, cell count taken every 48 hours. Data are shown as mean ± SEM; * p-value <0 . 05 in two-tailed Student’s t-test .

    Journal: bioRxiv

    Article Title: Histone succinylation directly inhibits Jumonji domain demethylases and stabilizes repressive chromatin states

    doi: 10.64898/2026.05.29.728167

    Figure Lengend Snippet: (A) Global histone succinylation measured by LC-MS/MS in HepG2/C3A cells following 48 hours of sodium succinate treatment. (B) Global histone succinylation in 3D cultured HepG2/C3A spheroids following 48 hours and 1 week of sodium succinate treatment. (C) Comparison of the relative abundance of succinyl-lysine residues in H3 and H4, in either treated or untreated, cultured cells (2D) or spheroids (3D). (D) Structure of the nucleosome with H3K64 residues highlighted to demonstrate solvent accessibility. (E) Abundance of succinyl-CoA in the nuclear fraction (left) and non-nuclear fraction (right) following sodium succinate treatment. (F) Total count of HepG2/C3A cells treated with 10 mM sodium succinate continuously for 48 to 144 hours, cell count taken every 48 hours. Data are shown as mean ± SEM; * p-value <0 . 05 in two-tailed Student’s t-test .

    Article Snippet: The human hepatocellular carcinoma HepG2/C3A cell line was obtained from the American Type Culture Collection (ATCC, CRL-10741).

    Techniques: Liquid Chromatography with Mass Spectroscopy, Cell Culture, Comparison, Solvent, Cell Characterization, Two Tailed Test

    (A) Schematic of peptide pull-down technique used to identify potential protein interactors with histone succinylation. (B) Volcano plot of fold change and significance of enrichment of nuclear proteins from HepG2/C3A cells to a Ksu synthetic peptide vs. Kac synthetic peptide. (C) Volcano plot of fold change and significance of enrichment of bromodomain proteins to Ksu synthetic histone peptide as compared to the Kac peptide, and (D) Ksu synthetic histone peptide as compared to an unmodified peptide. (E) Volcano plot of fold change and significance of enrichment of JmjC domain demethylases to Ksu synthetic histone peptide as compared to an Kac peptide and (F) Ksu synthetic histone peptide as compared to an unmodified peptide. (G) Crystal structure (PDB 6F6D) of an unmodified histone H3 peptide in the catalytic site of KDM6B. (H) Boltz2 model of a Ksu peptide (AARK(succinyl)A) in the catalytic site of KDM6B. (I) Enrichment of JmjC-domain demethylases to the chromatin-bound proteome of HepG2/C3A cells treated with 10 mM sodium succinate for 48 hours. A -log2 p-value greater than 4 indicates significant enrichment .

    Journal: bioRxiv

    Article Title: Histone succinylation directly inhibits Jumonji domain demethylases and stabilizes repressive chromatin states

    doi: 10.64898/2026.05.29.728167

    Figure Lengend Snippet: (A) Schematic of peptide pull-down technique used to identify potential protein interactors with histone succinylation. (B) Volcano plot of fold change and significance of enrichment of nuclear proteins from HepG2/C3A cells to a Ksu synthetic peptide vs. Kac synthetic peptide. (C) Volcano plot of fold change and significance of enrichment of bromodomain proteins to Ksu synthetic histone peptide as compared to the Kac peptide, and (D) Ksu synthetic histone peptide as compared to an unmodified peptide. (E) Volcano plot of fold change and significance of enrichment of JmjC domain demethylases to Ksu synthetic histone peptide as compared to an Kac peptide and (F) Ksu synthetic histone peptide as compared to an unmodified peptide. (G) Crystal structure (PDB 6F6D) of an unmodified histone H3 peptide in the catalytic site of KDM6B. (H) Boltz2 model of a Ksu peptide (AARK(succinyl)A) in the catalytic site of KDM6B. (I) Enrichment of JmjC-domain demethylases to the chromatin-bound proteome of HepG2/C3A cells treated with 10 mM sodium succinate for 48 hours. A -log2 p-value greater than 4 indicates significant enrichment .

    Article Snippet: The human hepatocellular carcinoma HepG2/C3A cell line was obtained from the American Type Culture Collection (ATCC, CRL-10741).

    Techniques:

    (A) Known targets of JmjC domain demethylase family enzymes. (B) Relative abundance of methylation on targets of JmjC domain demethylases in HepG2/C3A cells treated with sodium succinate. (C) Relative abundance of methylation on targets of JmjC domain demethylases in HepG2/C3A 3D cells treated with sodium succinate. (D) ChIP-MS shows co-enrichment of succinylated histone peptides with H3K27me3 peptides. Data are shown as mean ± SEM; *p-value <0 . 05, **p-value <0 . 01 in two-tailed Student’s t-test .

    Journal: bioRxiv

    Article Title: Histone succinylation directly inhibits Jumonji domain demethylases and stabilizes repressive chromatin states

    doi: 10.64898/2026.05.29.728167

    Figure Lengend Snippet: (A) Known targets of JmjC domain demethylase family enzymes. (B) Relative abundance of methylation on targets of JmjC domain demethylases in HepG2/C3A cells treated with sodium succinate. (C) Relative abundance of methylation on targets of JmjC domain demethylases in HepG2/C3A 3D cells treated with sodium succinate. (D) ChIP-MS shows co-enrichment of succinylated histone peptides with H3K27me3 peptides. Data are shown as mean ± SEM; *p-value <0 . 05, **p-value <0 . 01 in two-tailed Student’s t-test .

    Article Snippet: The human hepatocellular carcinoma HepG2/C3A cell line was obtained from the American Type Culture Collection (ATCC, CRL-10741).

    Techniques: Methylation, Two Tailed Test

    Binding site view of the PZ-3022 (1) PANK3 AMP-PNP complex (PDB ID: 6PE6 ) showing the spatial proximity of the cyclopropyl to the ATP-binding pocket of the enzyme. B) Pantazine PZ-3890 CoA elevation dose response in human C3A cells demonstrating a “hook effect” and an optimal activity window of 1–30 μM for this compound.

    Journal: Journal of Medicinal Chemistry

    Article Title: Discovery of Sulfonamide Pantothenate Kinase Activators and Elucidation of the Role of Isoform Selectivity in Cellular Pantothenate Kinase Activation

    doi: 10.1021/acs.jmedchem.5c03452

    Figure Lengend Snippet: Binding site view of the PZ-3022 (1) PANK3 AMP-PNP complex (PDB ID: 6PE6 ) showing the spatial proximity of the cyclopropyl to the ATP-binding pocket of the enzyme. B) Pantazine PZ-3890 CoA elevation dose response in human C3A cells demonstrating a “hook effect” and an optimal activity window of 1–30 μM for this compound.

    Article Snippet: Human C3A (HepG2/C3A) cells (ATCC CRL-10741) were used for cellular assays.

    Techniques: Binding Assay, Activity Assay

    Correlation Analysis and Surface Plasmon Resonance. A. Correlation analysis of the difference between K i of PANK1β and PANK3 vs C3A CoA elevation. The green-to-red scale shows the difference in K i between PANK1β and PANK3, while the size of the circles indicates the level of CoA elevation. B–E Surface Plasmon Resonance trace showing the binding of 20 and 21 to PANK3 and PANK1β in the presence of 1 mM ATP. B. 20 with PANK3. C. 20 with PANK1β. D. 21 with PANK3. E. 21 with PANK1β. The green data line was fit to a kinetic model shown in the black line. The association ( K a ), dissociation ( K d ), binding equilibrium ( K D ) constants, residence time (RT), and response units (RU) are shown in each panel.

    Journal: Journal of Medicinal Chemistry

    Article Title: Discovery of Sulfonamide Pantothenate Kinase Activators and Elucidation of the Role of Isoform Selectivity in Cellular Pantothenate Kinase Activation

    doi: 10.1021/acs.jmedchem.5c03452

    Figure Lengend Snippet: Correlation Analysis and Surface Plasmon Resonance. A. Correlation analysis of the difference between K i of PANK1β and PANK3 vs C3A CoA elevation. The green-to-red scale shows the difference in K i between PANK1β and PANK3, while the size of the circles indicates the level of CoA elevation. B–E Surface Plasmon Resonance trace showing the binding of 20 and 21 to PANK3 and PANK1β in the presence of 1 mM ATP. B. 20 with PANK3. C. 20 with PANK1β. D. 21 with PANK3. E. 21 with PANK1β. The green data line was fit to a kinetic model shown in the black line. The association ( K a ), dissociation ( K d ), binding equilibrium ( K D ) constants, residence time (RT), and response units (RU) are shown in each panel.

    Article Snippet: Human C3A (HepG2/C3A) cells (ATCC CRL-10741) were used for cellular assays.

    Techniques: SPR Assay, Binding Assay