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Procell Inc human glioma cell line u87 mg
Evaluation of GS Rg1 Effect on the Viability and Proliferation of Human <t>Glioblastoma</t> <t>U87-MG</t> and U251-MG Cells using MTT and BrdU assays, Respectively. U87-MG(A and B) and U251-MG (C and D) cells were treated with 0, 5, 10 and 20 μM of GS Rg1 for 48 h, respectively. The viabilities were determined as percent compared to the controls. GS Rg1 inhibits proliferative properties of U87-MG and U251-MG cells in a concentration-dependent manner. The results are presented as mean ± SD from three independent experiments. (∗: p < 0.05, ∗∗: p < 0.01,and ∗∗∗: p < 0.001).
Human Glioma Cell Line U87 Mg, supplied by Procell Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/u87-mg+cells/cell+glial+lines+u87/pmc13280443-60-1-22
Average 86 stars, based on 1 article reviews
human glioma cell line u87 mg - by Bioz Stars, 2026-09
86/100 stars

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1) Product Images from "NF-κB signaling pathway mediates the anti-tumor effect of Ginsenoside Rg1 in glioblastoma"

Article Title: NF-κB signaling pathway mediates the anti-tumor effect of Ginsenoside Rg1 in glioblastoma

Journal: Biochemistry and Biophysics Reports

doi: 10.1016/j.bbrep.2026.102548

Evaluation of GS Rg1 Effect on the Viability and Proliferation of Human Glioblastoma U87-MG and U251-MG Cells using MTT and BrdU assays, Respectively. U87-MG(A and B) and U251-MG (C and D) cells were treated with 0, 5, 10 and 20 μM of GS Rg1 for 48 h, respectively. The viabilities were determined as percent compared to the controls. GS Rg1 inhibits proliferative properties of U87-MG and U251-MG cells in a concentration-dependent manner. The results are presented as mean ± SD from three independent experiments. (∗: p < 0.05, ∗∗: p < 0.01,and ∗∗∗: p < 0.001).
Figure Legend Snippet: Evaluation of GS Rg1 Effect on the Viability and Proliferation of Human Glioblastoma U87-MG and U251-MG Cells using MTT and BrdU assays, Respectively. U87-MG(A and B) and U251-MG (C and D) cells were treated with 0, 5, 10 and 20 μM of GS Rg1 for 48 h, respectively. The viabilities were determined as percent compared to the controls. GS Rg1 inhibits proliferative properties of U87-MG and U251-MG cells in a concentration-dependent manner. The results are presented as mean ± SD from three independent experiments. (∗: p < 0.05, ∗∗: p < 0.01,and ∗∗∗: p < 0.001).

Techniques Used: Concentration Assay

Inhibition of MMP-2 and MMP-9 mRNA expression and activity of Extracellular Cathepsin B by GS Rg1 in U87-MG and U251-MG Cells. MMP2 (A and D) and MMP9 (B and E) expression levels were evaluated by reverse transcription-quantitative PCR. GS Rg1 at concentrations 5, 10 and 20 μM inhibited mRNA expression of MMP-2 and MMP-9, respectively. (C and F) Evaluation of GS Rg1 effect on proteolytic activity of extracellular Cathepsin B secreted from U87-MG and U251-MG cell line. GS Rg1 at concentrations 5, 10 and 20 μM inhibited activity of cathepsin, respectively. The values are given as mean ± SD compared with the control (∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001).
Figure Legend Snippet: Inhibition of MMP-2 and MMP-9 mRNA expression and activity of Extracellular Cathepsin B by GS Rg1 in U87-MG and U251-MG Cells. MMP2 (A and D) and MMP9 (B and E) expression levels were evaluated by reverse transcription-quantitative PCR. GS Rg1 at concentrations 5, 10 and 20 μM inhibited mRNA expression of MMP-2 and MMP-9, respectively. (C and F) Evaluation of GS Rg1 effect on proteolytic activity of extracellular Cathepsin B secreted from U87-MG and U251-MG cell line. GS Rg1 at concentrations 5, 10 and 20 μM inhibited activity of cathepsin, respectively. The values are given as mean ± SD compared with the control (∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001).

Techniques Used: Inhibition, Expressing, Activity Assay, Reverse Transcription, Real-time Polymerase Chain Reaction, Control

Stimulation of Caspase-3 and Caspase-9 activity by GS Rg1 in U87-MG and U251-MG cells. (A and C) GS Rg1 increased activity of Caspase-3 in a concentration-dependent manner. (B and D) GS Rg1 increased activity of Caspase-9 in a concentration-dependent manner. The values are given as mean ± SD compared with the control (∗: p < 0.05, ∗∗: p < 0.01, and ∗∗∗: p < 0.001).
Figure Legend Snippet: Stimulation of Caspase-3 and Caspase-9 activity by GS Rg1 in U87-MG and U251-MG cells. (A and C) GS Rg1 increased activity of Caspase-3 in a concentration-dependent manner. (B and D) GS Rg1 increased activity of Caspase-9 in a concentration-dependent manner. The values are given as mean ± SD compared with the control (∗: p < 0.05, ∗∗: p < 0.01, and ∗∗∗: p < 0.001).

Techniques Used: Activity Assay, Concentration Assay, Control

Effect of GS Rg1 on transcriptional expression of proteins involved in Survival of Glioblastoma Cells. Transcriptional expression of IKK2(A and G), survivin (B and H), c-Myc (C and I), hTERT (D and J), NEMO (NF-κB regulators) (E and K), STAT3(F and L) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.
Figure Legend Snippet: Effect of GS Rg1 on transcriptional expression of proteins involved in Survival of Glioblastoma Cells. Transcriptional expression of IKK2(A and G), survivin (B and H), c-Myc (C and I), hTERT (D and J), NEMO (NF-κB regulators) (E and K), STAT3(F and L) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.

Techniques Used: Expressing, Control

Effect of GS Rg1 on transcriptional expression of proteins involved in apoptosis of Glioblastoma Cells. Transcriptional expression of Bax (A and I), Caspase-3 (B and J), Caspase-9 (C and K), Bcl-2 (D and L), Bax/Bcl-2 (E and M), Blf-1(F and N), Bcl-xl (G and O) and p21(H and P) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.
Figure Legend Snippet: Effect of GS Rg1 on transcriptional expression of proteins involved in apoptosis of Glioblastoma Cells. Transcriptional expression of Bax (A and I), Caspase-3 (B and J), Caspase-9 (C and K), Bcl-2 (D and L), Bax/Bcl-2 (E and M), Blf-1(F and N), Bcl-xl (G and O) and p21(H and P) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.

Techniques Used: Expressing, Control

Effect of GS Rg1 on transcriptional expression of proteins involved in invasion and media pH change of Glioblastoma Cells. Transcriptional expression of MMP14 (A and G), Cathepsin B (B and H), uPA (C and I), uPAR (D and J), CA9 (E and K) and NHE1(F and L) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.
Figure Legend Snippet: Effect of GS Rg1 on transcriptional expression of proteins involved in invasion and media pH change of Glioblastoma Cells. Transcriptional expression of MMP14 (A and G), Cathepsin B (B and H), uPA (C and I), uPAR (D and J), CA9 (E and K) and NHE1(F and L) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.

Techniques Used: Expressing, Control

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Article Title: Novel piperazine based benzamide derivatives as potential anti-glioblastoma agents inhibiting cell proliferation and cell cycle progression.
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Article Snippet: U87‐MG cel ls (cat. no. CL‐0238) were obtained from Procell Life Science & Technology Co., Ltd.

Article Title: Effects of endoplasmic reticulum stress-mediated CREB3L1 on apoptosis of glioma cells
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Image Search Results


ZNF25 knockdown inhibits proliferation and migration of A172 and U87-MG Cells. (A) The silencing efficiency of siRNAs for ZNF25 knockdown in A172 cells detected by RT-qPCR. (B) The silencing efficiency of siRNAs for ZNF25 knockdown in U87-MG cells detected by RT-qPCR. (C) ZNF25 protein levels in A172 cells were analyzed by Western blotting at 72 hours post-transfection with si ZNF25 and siNC. GAPDH was used as a loading control. (D) ZNF25 protein levels in U87-MG cells were analyzed by Western blotting at 72 hours post-transfection with si ZNF25 and siNC. GAPDH was used as a loading control. (E) Bar graph showing the quantification of protein expression in A172 cells. The band intensities from Western blot analysis were quantified using ImageJ software. Data are presented as mean ± SD (n=3 independent experiment, Student’s t-test). (F) Bar graph showing the quantification of protein expression in U87-MG cells. The band intensities from Western blot analysis were quantified using ImageJ software. Data are presented as mean ± SD (n=3 independent experiment, Student’s t-test). (G–H) Cell viability was determined by CCK-8 assay in A172 and U87-MG cells after transfection with si ZNF25 and siNC. Data are presented as the mean ± SD of at least three independent experiments compared with the siNC group at the corresponding time point. (I) Representative microscopic images of the wound area at 36h after scratching in A172 cells transfected with si ZNF25 and siNC. Scale bar, 400 μm. (J) Quantitative analysis of the wound closure rate of A172 cells at 36h post-transfection with si ZNF25 and siNC. (K) Representative microscopic images of the wound area at 36h after scratching in U87-MG cells transfected with si ZNF25 and siNC. Scale bar, 400μm. (L) Quantitative analysis of wound closure rate in U87-MG cells at 36h post-transfection, with si ZNF25 and siNC. Data are shown as mean ± SD from n = 6 independent experiments. Statistical significance was determined by Student’s t-test. (* P <0.05, ** P< 0.01, *** P < 0.001, **** P < 0.0001).

Journal: Frontiers in Oncology

Article Title: ZNF25 as an immunotherapy target: pan-cancer biomarker potential and mechanistic exploration in glioma

doi: 10.3389/fonc.2026.1631383

Figure Lengend Snippet: ZNF25 knockdown inhibits proliferation and migration of A172 and U87-MG Cells. (A) The silencing efficiency of siRNAs for ZNF25 knockdown in A172 cells detected by RT-qPCR. (B) The silencing efficiency of siRNAs for ZNF25 knockdown in U87-MG cells detected by RT-qPCR. (C) ZNF25 protein levels in A172 cells were analyzed by Western blotting at 72 hours post-transfection with si ZNF25 and siNC. GAPDH was used as a loading control. (D) ZNF25 protein levels in U87-MG cells were analyzed by Western blotting at 72 hours post-transfection with si ZNF25 and siNC. GAPDH was used as a loading control. (E) Bar graph showing the quantification of protein expression in A172 cells. The band intensities from Western blot analysis were quantified using ImageJ software. Data are presented as mean ± SD (n=3 independent experiment, Student’s t-test). (F) Bar graph showing the quantification of protein expression in U87-MG cells. The band intensities from Western blot analysis were quantified using ImageJ software. Data are presented as mean ± SD (n=3 independent experiment, Student’s t-test). (G–H) Cell viability was determined by CCK-8 assay in A172 and U87-MG cells after transfection with si ZNF25 and siNC. Data are presented as the mean ± SD of at least three independent experiments compared with the siNC group at the corresponding time point. (I) Representative microscopic images of the wound area at 36h after scratching in A172 cells transfected with si ZNF25 and siNC. Scale bar, 400 μm. (J) Quantitative analysis of the wound closure rate of A172 cells at 36h post-transfection with si ZNF25 and siNC. (K) Representative microscopic images of the wound area at 36h after scratching in U87-MG cells transfected with si ZNF25 and siNC. Scale bar, 400μm. (L) Quantitative analysis of wound closure rate in U87-MG cells at 36h post-transfection, with si ZNF25 and siNC. Data are shown as mean ± SD from n = 6 independent experiments. Statistical significance was determined by Student’s t-test. (* P <0.05, ** P< 0.01, *** P < 0.001, **** P < 0.0001).

Article Snippet: Glioma cells U87-MG were obtained from the American Type Culture Collection (ATCC, Manassas, USA), and A172 were purchased from Xiamen Immocell Biotechnology Co. Ltd.

Techniques: Knockdown, Migration, Quantitative RT-PCR, Western Blot, Transfection, Control, Expressing, Software, CCK-8 Assay

Functional enrichment analysis and molecular verification of ZNF25 knockdown. (A) The volcano plot visualized all identified DEGs in U87-MG cells, which were screened by the criteria of adjusted P-value (padj) < 0.05 and ∣log 2 FC∣>1. (B) Top 10 enriched GO terms across all categories. (C) Top 10 enriched KEGG pathways. (D) Western blot analysis of p-AKT protein levels in A172 and U87-MG cells at 72h after transfection with si ZNF25 and siNC. GAPDH was used as a loading control. (E) Bar graph showing the quantification of protein expression in U87-MG cells corresponding to (D) . Data are presented as mean ± SD (n = 3 independent experiment, Student’s t-test). (* P < 0.05, ** P < 0.01).

Journal: Frontiers in Oncology

Article Title: ZNF25 as an immunotherapy target: pan-cancer biomarker potential and mechanistic exploration in glioma

doi: 10.3389/fonc.2026.1631383

Figure Lengend Snippet: Functional enrichment analysis and molecular verification of ZNF25 knockdown. (A) The volcano plot visualized all identified DEGs in U87-MG cells, which were screened by the criteria of adjusted P-value (padj) < 0.05 and ∣log 2 FC∣>1. (B) Top 10 enriched GO terms across all categories. (C) Top 10 enriched KEGG pathways. (D) Western blot analysis of p-AKT protein levels in A172 and U87-MG cells at 72h after transfection with si ZNF25 and siNC. GAPDH was used as a loading control. (E) Bar graph showing the quantification of protein expression in U87-MG cells corresponding to (D) . Data are presented as mean ± SD (n = 3 independent experiment, Student’s t-test). (* P < 0.05, ** P < 0.01).

Article Snippet: Glioma cells U87-MG were obtained from the American Type Culture Collection (ATCC, Manassas, USA), and A172 were purchased from Xiamen Immocell Biotechnology Co. Ltd.

Techniques: Functional Assay, Knockdown, Western Blot, Transfection, Control, Expressing

Evaluation of GS Rg1 Effect on the Viability and Proliferation of Human Glioblastoma U87-MG and U251-MG Cells using MTT and BrdU assays, Respectively. U87-MG(A and B) and U251-MG (C and D) cells were treated with 0, 5, 10 and 20 μM of GS Rg1 for 48 h, respectively. The viabilities were determined as percent compared to the controls. GS Rg1 inhibits proliferative properties of U87-MG and U251-MG cells in a concentration-dependent manner. The results are presented as mean ± SD from three independent experiments. (∗: p < 0.05, ∗∗: p < 0.01,and ∗∗∗: p < 0.001).

Journal: Biochemistry and Biophysics Reports

Article Title: NF-κB signaling pathway mediates the anti-tumor effect of Ginsenoside Rg1 in glioblastoma

doi: 10.1016/j.bbrep.2026.102548

Figure Lengend Snippet: Evaluation of GS Rg1 Effect on the Viability and Proliferation of Human Glioblastoma U87-MG and U251-MG Cells using MTT and BrdU assays, Respectively. U87-MG(A and B) and U251-MG (C and D) cells were treated with 0, 5, 10 and 20 μM of GS Rg1 for 48 h, respectively. The viabilities were determined as percent compared to the controls. GS Rg1 inhibits proliferative properties of U87-MG and U251-MG cells in a concentration-dependent manner. The results are presented as mean ± SD from three independent experiments. (∗: p < 0.05, ∗∗: p < 0.01,and ∗∗∗: p < 0.001).

Article Snippet: The human glioma cell line U87-MG (U87 Malignant Glioma, #CL-0238; Wuhan, China) and U251-MG(U251 Malignant Glioma, #CL-0237; Wuhan, China) were obtained from Procell and cultured in Dulbecco's Modified Eagle's Medium (DMEM; Gibco, Grand Island, NY, USA) supplemented with 10% fetal bovine serum (Zhejiang Tianhang Biotechnology, Huzhou, China) and 1% antibiotics (Gibco), at 37 °C in a 5% CO 2 atmosphere.

Techniques: Concentration Assay

Inhibition of MMP-2 and MMP-9 mRNA expression and activity of Extracellular Cathepsin B by GS Rg1 in U87-MG and U251-MG Cells. MMP2 (A and D) and MMP9 (B and E) expression levels were evaluated by reverse transcription-quantitative PCR. GS Rg1 at concentrations 5, 10 and 20 μM inhibited mRNA expression of MMP-2 and MMP-9, respectively. (C and F) Evaluation of GS Rg1 effect on proteolytic activity of extracellular Cathepsin B secreted from U87-MG and U251-MG cell line. GS Rg1 at concentrations 5, 10 and 20 μM inhibited activity of cathepsin, respectively. The values are given as mean ± SD compared with the control (∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001).

Journal: Biochemistry and Biophysics Reports

Article Title: NF-κB signaling pathway mediates the anti-tumor effect of Ginsenoside Rg1 in glioblastoma

doi: 10.1016/j.bbrep.2026.102548

Figure Lengend Snippet: Inhibition of MMP-2 and MMP-9 mRNA expression and activity of Extracellular Cathepsin B by GS Rg1 in U87-MG and U251-MG Cells. MMP2 (A and D) and MMP9 (B and E) expression levels were evaluated by reverse transcription-quantitative PCR. GS Rg1 at concentrations 5, 10 and 20 μM inhibited mRNA expression of MMP-2 and MMP-9, respectively. (C and F) Evaluation of GS Rg1 effect on proteolytic activity of extracellular Cathepsin B secreted from U87-MG and U251-MG cell line. GS Rg1 at concentrations 5, 10 and 20 μM inhibited activity of cathepsin, respectively. The values are given as mean ± SD compared with the control (∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001).

Article Snippet: The human glioma cell line U87-MG (U87 Malignant Glioma, #CL-0238; Wuhan, China) and U251-MG(U251 Malignant Glioma, #CL-0237; Wuhan, China) were obtained from Procell and cultured in Dulbecco's Modified Eagle's Medium (DMEM; Gibco, Grand Island, NY, USA) supplemented with 10% fetal bovine serum (Zhejiang Tianhang Biotechnology, Huzhou, China) and 1% antibiotics (Gibco), at 37 °C in a 5% CO 2 atmosphere.

Techniques: Inhibition, Expressing, Activity Assay, Reverse Transcription, Real-time Polymerase Chain Reaction, Control

Stimulation of Caspase-3 and Caspase-9 activity by GS Rg1 in U87-MG and U251-MG cells. (A and C) GS Rg1 increased activity of Caspase-3 in a concentration-dependent manner. (B and D) GS Rg1 increased activity of Caspase-9 in a concentration-dependent manner. The values are given as mean ± SD compared with the control (∗: p < 0.05, ∗∗: p < 0.01, and ∗∗∗: p < 0.001).

Journal: Biochemistry and Biophysics Reports

Article Title: NF-κB signaling pathway mediates the anti-tumor effect of Ginsenoside Rg1 in glioblastoma

doi: 10.1016/j.bbrep.2026.102548

Figure Lengend Snippet: Stimulation of Caspase-3 and Caspase-9 activity by GS Rg1 in U87-MG and U251-MG cells. (A and C) GS Rg1 increased activity of Caspase-3 in a concentration-dependent manner. (B and D) GS Rg1 increased activity of Caspase-9 in a concentration-dependent manner. The values are given as mean ± SD compared with the control (∗: p < 0.05, ∗∗: p < 0.01, and ∗∗∗: p < 0.001).

Article Snippet: The human glioma cell line U87-MG (U87 Malignant Glioma, #CL-0238; Wuhan, China) and U251-MG(U251 Malignant Glioma, #CL-0237; Wuhan, China) were obtained from Procell and cultured in Dulbecco's Modified Eagle's Medium (DMEM; Gibco, Grand Island, NY, USA) supplemented with 10% fetal bovine serum (Zhejiang Tianhang Biotechnology, Huzhou, China) and 1% antibiotics (Gibco), at 37 °C in a 5% CO 2 atmosphere.

Techniques: Activity Assay, Concentration Assay, Control

Effect of GS Rg1 on transcriptional expression of proteins involved in Survival of Glioblastoma Cells. Transcriptional expression of IKK2(A and G), survivin (B and H), c-Myc (C and I), hTERT (D and J), NEMO (NF-κB regulators) (E and K), STAT3(F and L) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.

Journal: Biochemistry and Biophysics Reports

Article Title: NF-κB signaling pathway mediates the anti-tumor effect of Ginsenoside Rg1 in glioblastoma

doi: 10.1016/j.bbrep.2026.102548

Figure Lengend Snippet: Effect of GS Rg1 on transcriptional expression of proteins involved in Survival of Glioblastoma Cells. Transcriptional expression of IKK2(A and G), survivin (B and H), c-Myc (C and I), hTERT (D and J), NEMO (NF-κB regulators) (E and K), STAT3(F and L) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.

Article Snippet: The human glioma cell line U87-MG (U87 Malignant Glioma, #CL-0238; Wuhan, China) and U251-MG(U251 Malignant Glioma, #CL-0237; Wuhan, China) were obtained from Procell and cultured in Dulbecco's Modified Eagle's Medium (DMEM; Gibco, Grand Island, NY, USA) supplemented with 10% fetal bovine serum (Zhejiang Tianhang Biotechnology, Huzhou, China) and 1% antibiotics (Gibco), at 37 °C in a 5% CO 2 atmosphere.

Techniques: Expressing, Control

Effect of GS Rg1 on transcriptional expression of proteins involved in apoptosis of Glioblastoma Cells. Transcriptional expression of Bax (A and I), Caspase-3 (B and J), Caspase-9 (C and K), Bcl-2 (D and L), Bax/Bcl-2 (E and M), Blf-1(F and N), Bcl-xl (G and O) and p21(H and P) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.

Journal: Biochemistry and Biophysics Reports

Article Title: NF-κB signaling pathway mediates the anti-tumor effect of Ginsenoside Rg1 in glioblastoma

doi: 10.1016/j.bbrep.2026.102548

Figure Lengend Snippet: Effect of GS Rg1 on transcriptional expression of proteins involved in apoptosis of Glioblastoma Cells. Transcriptional expression of Bax (A and I), Caspase-3 (B and J), Caspase-9 (C and K), Bcl-2 (D and L), Bax/Bcl-2 (E and M), Blf-1(F and N), Bcl-xl (G and O) and p21(H and P) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.

Article Snippet: The human glioma cell line U87-MG (U87 Malignant Glioma, #CL-0238; Wuhan, China) and U251-MG(U251 Malignant Glioma, #CL-0237; Wuhan, China) were obtained from Procell and cultured in Dulbecco's Modified Eagle's Medium (DMEM; Gibco, Grand Island, NY, USA) supplemented with 10% fetal bovine serum (Zhejiang Tianhang Biotechnology, Huzhou, China) and 1% antibiotics (Gibco), at 37 °C in a 5% CO 2 atmosphere.

Techniques: Expressing, Control

Effect of GS Rg1 on transcriptional expression of proteins involved in invasion and media pH change of Glioblastoma Cells. Transcriptional expression of MMP14 (A and G), Cathepsin B (B and H), uPA (C and I), uPAR (D and J), CA9 (E and K) and NHE1(F and L) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.

Journal: Biochemistry and Biophysics Reports

Article Title: NF-κB signaling pathway mediates the anti-tumor effect of Ginsenoside Rg1 in glioblastoma

doi: 10.1016/j.bbrep.2026.102548

Figure Lengend Snippet: Effect of GS Rg1 on transcriptional expression of proteins involved in invasion and media pH change of Glioblastoma Cells. Transcriptional expression of MMP14 (A and G), Cathepsin B (B and H), uPA (C and I), uPAR (D and J), CA9 (E and K) and NHE1(F and L) in U87-MG and U251-MG cell line, after treatment with GS Rg1 for 48 h. Data are shown as fold change in relative expression compared with HPRT1 on the basis of comparative Ct (2-ΔΔCt) method. Values are shown as mean ± SD. Statistically different values of ∗: p < 0.05, ∗∗: p < 0.01, ∗∗∗: p < 0.001 and ∗∗∗∗: p < 0.0001 are determined compared with the control.

Article Snippet: The human glioma cell line U87-MG (U87 Malignant Glioma, #CL-0238; Wuhan, China) and U251-MG(U251 Malignant Glioma, #CL-0237; Wuhan, China) were obtained from Procell and cultured in Dulbecco's Modified Eagle's Medium (DMEM; Gibco, Grand Island, NY, USA) supplemented with 10% fetal bovine serum (Zhejiang Tianhang Biotechnology, Huzhou, China) and 1% antibiotics (Gibco), at 37 °C in a 5% CO 2 atmosphere.

Techniques: Expressing, Control