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anti c ebpβ  (Santa Cruz Biotechnology)


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    Structured Review

    Santa Cruz Biotechnology anti c ebpβ
    Anti C Ebpβ, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 974 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/c+ebp+%CE%B2/C%2FEBP+%CE%B2/pm42883696-275-35-37
    Average 96 stars, based on 974 article reviews
    anti c ebpβ - by Bioz Stars, 2026-10
    96/100 stars

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    Related Articles

    Saline:

    Article Title: Microbial chaperonin 60 inhibits osteoclast differentiation by interfering with RANK/RANKL binding and overexpression of lipocalin2.
    Article Snippet: .. The proteins were transferred to polyvinylidene fluoride (PVDF) membranes (Millipore, Bedford, MA, USA) and blocked with 6 % dry non-fat skim milk in Tris-buffered saline with 0.05 % Tween 20 (TBST) for 1 h. Afterward, the membranes were washed with TBST and incubated overnight at 4 ◦C with the following primary antibodies: β-actin (1:5000 dilution, GTX109639; GeneTex), LCN2 (1:500 dilution, AF1857; R&D Systems), TRAF5 (1:500 dilution, 12868-1; ProteinTech), PLCγ1 (1:1000 dilution, 2822S; Cell Signaling), NFATc1 (1:500 dilution, sc-7294; Santa Cruz Biotechnology), MITF (1:250 dilution, sc-56725; Santa Cruz Biotechnology), c-Fos (1:1000 dilution, 2250; Cell Signaling), C/EBP-β (1:500 dilution, sc-7962; Santa Cruz Biotechnology), RANK (1:500 dilution, sc-374,360; Santa Cruz Biotechnology), NFκB (1:1000 dilution, 8242; Cell Signaling), phosphoNFκB (1:1000 dilution, 3033; Cell Signaling). ..

    Incubation:

    Article Title: Microbial chaperonin 60 inhibits osteoclast differentiation by interfering with RANK/RANKL binding and overexpression of lipocalin2.
    Article Snippet: .. The proteins were transferred to polyvinylidene fluoride (PVDF) membranes (Millipore, Bedford, MA, USA) and blocked with 6 % dry non-fat skim milk in Tris-buffered saline with 0.05 % Tween 20 (TBST) for 1 h. Afterward, the membranes were washed with TBST and incubated overnight at 4 ◦C with the following primary antibodies: β-actin (1:5000 dilution, GTX109639; GeneTex), LCN2 (1:500 dilution, AF1857; R&D Systems), TRAF5 (1:500 dilution, 12868-1; ProteinTech), PLCγ1 (1:1000 dilution, 2822S; Cell Signaling), NFATc1 (1:500 dilution, sc-7294; Santa Cruz Biotechnology), MITF (1:250 dilution, sc-56725; Santa Cruz Biotechnology), c-Fos (1:1000 dilution, 2250; Cell Signaling), C/EBP-β (1:500 dilution, sc-7962; Santa Cruz Biotechnology), RANK (1:500 dilution, sc-374,360; Santa Cruz Biotechnology), NFκB (1:1000 dilution, 8242; Cell Signaling), phosphoNFκB (1:1000 dilution, 3033; Cell Signaling). ..

    Article Title: TTK Inhibition Alleviates Postinjury Neointimal Formation and Atherosclerosis
    Article Snippet: Equal amounts of total protein in each group were resolved and separated on SDS‐PAGE, and subsequently transferred onto PVDF membranes (EMD Millipore, Billerica, MA, USA). .. After blocking with 5% skim milk or 5% BSA in TBST, the membranes were incubated at 4 °C overnight with primary antibodies against TTK (AF6028, R&D Systems), TTK (A2500, Abclonal), IRF1 (#8478, CST), E2F4 (10923‐1‐AP, Proteintech), C/EBP β (sc‐7962, Santa Cruz), α‐SMA (ab5694, Abcam), SM22α (ab10135, Abcam), calponin (ab46794, Abcam), p120‐catenin (12180‐1‐AP, Proteintech), p‐p120 (Thr310) (bs‐12990R, Bioss), HA (ab9110, Abcam), β‐catenin (51067‐2‐AP, Proteintech), N‐cadherin (ab18203, Abcam), SRF (16821‐1‐AP, Proteintech), MYOCD (SAB4200539, Sigma‐Aldrich), Cre Recombinase (#15036, CST), H3 (AF0009, Beyotime), β‐tubulin (AC015, Abclonal) and β‐actin (AC026, Abclonal). .. After incubation with horseradish peroxidase (HRP)‐conjugated secondary antibodies of the appropriate species for 1 h at room temperature, protein bands on the membrane were visualized on a BioSpectrum imaging system (UVP, USA) using ECL solution, and the expression levels of proteins were evaluated with ImageJ software.

    Article Title: Shared Mechanisms in Pparγ1sv and Pparγ2 Expression in 3T3-L1 Cells: Studies on Epigenetic and Positive Feedback Regulation of Pparγ during Adipogenesis
    Article Snippet: .. Following electrophoresis, proteins were transferred to PVDF membrane and blocked with 1% Western Blocking Reagent (Sigma-Aldrich) at 25°C for 1 h. The membrane was then incubated overnight at 16°C with antibodies against PPAR γ (A3409A, Perseus Proteomics), C/EBP β (sc-150, Santa Cruz Biotechnology), or GAPDH (G8795, Sigma-Aldrich). .. Chemiluminescence signals were visualized using ImmunoStar LD (Fujifilm Wako) and detected with an ImageQuant800 (Cytiva).

    Article Title: TTK Inhibition Alleviates Postinjury Neointimal Formation and Atherosclerosis.
    Article Snippet: Equal amounts of total protein in each group were resolved and separated on SDS-PAGE, and subsequently transferred onto PVDF membranes (EMD Millipore, Billerica, MA, USA). .. After blocking with 5% skim milk or 5% BSA in TBST, the membranes were incubated at 4 °C overnight with primary antibodies against TTK (AF6028, R&D Systems), TTK (A2500, Abclonal), IRF1 (#8478, CST), E2F4 (10923-1-AP, Proteintech), C/EBP β (sc-7962, Santa Cruz), α-SMA (ab5694, Abcam), SM22α (ab10135, Abcam), calponin (ab46794, Abcam), p120-catenin (12180-1-AP, Proteintech), p-p120 (Thr310) (bs-12990R, Bioss), HA (ab9110, Abcam), β- catenin (51067-2-AP, Proteintech), N-cadherin (ab18203, Abcam), SRF (16821-1-AP, Proteintech), MYOCD (SAB4200539, Sigma-Aldrich), Cre Recombinase (#15036, CST), H3 (AF0009, Beyotime), β-tubulin (AC015, Abclonal) and β-actin (AC026, Abclonal). .. After incubation with horseradish peroxidase (HRP)-conjugated secondary antibodies of the appropriate species for 1 h at room temperature, protein bands on the membrane were visualized on a BioSpectrum imaging system (UVP, USA) using ECL solution, and the expression levels of proteins were evaluated with ImageJ software. siRNA Transfection: Small interfering RNAs (siRNAs) against TTK, CEP55, NCAPH, IRF1, E2F4, C/EBPβ, and a scrambled siRNA were designed and synthesized by RiboBio (Guangzhou, China).

    Blocking Assay:

    Article Title: TTK Inhibition Alleviates Postinjury Neointimal Formation and Atherosclerosis
    Article Snippet: Equal amounts of total protein in each group were resolved and separated on SDS‐PAGE, and subsequently transferred onto PVDF membranes (EMD Millipore, Billerica, MA, USA). .. After blocking with 5% skim milk or 5% BSA in TBST, the membranes were incubated at 4 °C overnight with primary antibodies against TTK (AF6028, R&D Systems), TTK (A2500, Abclonal), IRF1 (#8478, CST), E2F4 (10923‐1‐AP, Proteintech), C/EBP β (sc‐7962, Santa Cruz), α‐SMA (ab5694, Abcam), SM22α (ab10135, Abcam), calponin (ab46794, Abcam), p120‐catenin (12180‐1‐AP, Proteintech), p‐p120 (Thr310) (bs‐12990R, Bioss), HA (ab9110, Abcam), β‐catenin (51067‐2‐AP, Proteintech), N‐cadherin (ab18203, Abcam), SRF (16821‐1‐AP, Proteintech), MYOCD (SAB4200539, Sigma‐Aldrich), Cre Recombinase (#15036, CST), H3 (AF0009, Beyotime), β‐tubulin (AC015, Abclonal) and β‐actin (AC026, Abclonal). .. After incubation with horseradish peroxidase (HRP)‐conjugated secondary antibodies of the appropriate species for 1 h at room temperature, protein bands on the membrane were visualized on a BioSpectrum imaging system (UVP, USA) using ECL solution, and the expression levels of proteins were evaluated with ImageJ software.

    Article Title: Shared Mechanisms in Pparγ1sv and Pparγ2 Expression in 3T3-L1 Cells: Studies on Epigenetic and Positive Feedback Regulation of Pparγ during Adipogenesis
    Article Snippet: .. Following electrophoresis, proteins were transferred to PVDF membrane and blocked with 1% Western Blocking Reagent (Sigma-Aldrich) at 25°C for 1 h. The membrane was then incubated overnight at 16°C with antibodies against PPAR γ (A3409A, Perseus Proteomics), C/EBP β (sc-150, Santa Cruz Biotechnology), or GAPDH (G8795, Sigma-Aldrich). .. Chemiluminescence signals were visualized using ImmunoStar LD (Fujifilm Wako) and detected with an ImageQuant800 (Cytiva).

    Article Title: TTK Inhibition Alleviates Postinjury Neointimal Formation and Atherosclerosis.
    Article Snippet: Equal amounts of total protein in each group were resolved and separated on SDS-PAGE, and subsequently transferred onto PVDF membranes (EMD Millipore, Billerica, MA, USA). .. After blocking with 5% skim milk or 5% BSA in TBST, the membranes were incubated at 4 °C overnight with primary antibodies against TTK (AF6028, R&D Systems), TTK (A2500, Abclonal), IRF1 (#8478, CST), E2F4 (10923-1-AP, Proteintech), C/EBP β (sc-7962, Santa Cruz), α-SMA (ab5694, Abcam), SM22α (ab10135, Abcam), calponin (ab46794, Abcam), p120-catenin (12180-1-AP, Proteintech), p-p120 (Thr310) (bs-12990R, Bioss), HA (ab9110, Abcam), β- catenin (51067-2-AP, Proteintech), N-cadherin (ab18203, Abcam), SRF (16821-1-AP, Proteintech), MYOCD (SAB4200539, Sigma-Aldrich), Cre Recombinase (#15036, CST), H3 (AF0009, Beyotime), β-tubulin (AC015, Abclonal) and β-actin (AC026, Abclonal). .. After incubation with horseradish peroxidase (HRP)-conjugated secondary antibodies of the appropriate species for 1 h at room temperature, protein bands on the membrane were visualized on a BioSpectrum imaging system (UVP, USA) using ECL solution, and the expression levels of proteins were evaluated with ImageJ software. siRNA Transfection: Small interfering RNAs (siRNAs) against TTK, CEP55, NCAPH, IRF1, E2F4, C/EBPβ, and a scrambled siRNA were designed and synthesized by RiboBio (Guangzhou, China).

    Electrophoresis:

    Article Title: Shared Mechanisms in Pparγ1sv and Pparγ2 Expression in 3T3-L1 Cells: Studies on Epigenetic and Positive Feedback Regulation of Pparγ during Adipogenesis
    Article Snippet: .. Following electrophoresis, proteins were transferred to PVDF membrane and blocked with 1% Western Blocking Reagent (Sigma-Aldrich) at 25°C for 1 h. The membrane was then incubated overnight at 16°C with antibodies against PPAR γ (A3409A, Perseus Proteomics), C/EBP β (sc-150, Santa Cruz Biotechnology), or GAPDH (G8795, Sigma-Aldrich). .. Chemiluminescence signals were visualized using ImmunoStar LD (Fujifilm Wako) and detected with an ImageQuant800 (Cytiva).

    Membrane:

    Article Title: Shared Mechanisms in Pparγ1sv and Pparγ2 Expression in 3T3-L1 Cells: Studies on Epigenetic and Positive Feedback Regulation of Pparγ during Adipogenesis
    Article Snippet: .. Following electrophoresis, proteins were transferred to PVDF membrane and blocked with 1% Western Blocking Reagent (Sigma-Aldrich) at 25°C for 1 h. The membrane was then incubated overnight at 16°C with antibodies against PPAR γ (A3409A, Perseus Proteomics), C/EBP β (sc-150, Santa Cruz Biotechnology), or GAPDH (G8795, Sigma-Aldrich). .. Chemiluminescence signals were visualized using ImmunoStar LD (Fujifilm Wako) and detected with an ImageQuant800 (Cytiva).

    Western Blot:

    Article Title: Shared Mechanisms in Pparγ1sv and Pparγ2 Expression in 3T3-L1 Cells: Studies on Epigenetic and Positive Feedback Regulation of Pparγ during Adipogenesis
    Article Snippet: .. Following electrophoresis, proteins were transferred to PVDF membrane and blocked with 1% Western Blocking Reagent (Sigma-Aldrich) at 25°C for 1 h. The membrane was then incubated overnight at 16°C with antibodies against PPAR γ (A3409A, Perseus Proteomics), C/EBP β (sc-150, Santa Cruz Biotechnology), or GAPDH (G8795, Sigma-Aldrich). .. Chemiluminescence signals were visualized using ImmunoStar LD (Fujifilm Wako) and detected with an ImageQuant800 (Cytiva).



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    Image Search Results


    C/EBP-β is downregulated in sorafenib-resistant hepatocellular carcinoma cells. ( A ) The inhibition ratio (%) of parental (HepG2, Huh7) and sorafenib-resistant (HepG2-R, Huh7-R) HCC cells was measured by CCK-8 assay after treatment with a gradient of sorafenib concentrations for 48 h. The calculated IC 50 values are indicated on the dose-response curves. Data are presented as mean ± SD (n=3). ( B ) The relative mRNA and protein expression levels of C/EBP-β in parental and sorafenib-resistant cell lines were determined by RT-qPCR (bar graphs) and Western blot (gel images), respectively. GAPDH was used as an internal control. Data in the bar graphs are presented as mean ± SD from three independent experiments. ** P < 0.01 compared to the corresponding parental cells.

    Journal: Journal of Hepatocellular Carcinoma

    Article Title: C/EBP-β Mediates the Reversal of Sorafenib Resistance by Tunicamycin in Hepatocellular Carcinoma

    doi: 10.2147/JHC.S587037

    Figure Lengend Snippet: C/EBP-β is downregulated in sorafenib-resistant hepatocellular carcinoma cells. ( A ) The inhibition ratio (%) of parental (HepG2, Huh7) and sorafenib-resistant (HepG2-R, Huh7-R) HCC cells was measured by CCK-8 assay after treatment with a gradient of sorafenib concentrations for 48 h. The calculated IC 50 values are indicated on the dose-response curves. Data are presented as mean ± SD (n=3). ( B ) The relative mRNA and protein expression levels of C/EBP-β in parental and sorafenib-resistant cell lines were determined by RT-qPCR (bar graphs) and Western blot (gel images), respectively. GAPDH was used as an internal control. Data in the bar graphs are presented as mean ± SD from three independent experiments. ** P < 0.01 compared to the corresponding parental cells.

    Article Snippet: The following primary antibodies were used for Western blot and immunohistochemistry: C/EBP-β (A0711, Abclonal, China), p53 (ET1601-13, HUABIO, China), Bax (ET1603-34, HUABIO, China), Bcl-2 (ET1702-53, HUABIO, China), Cleaved Caspase-3 (ET1602-47, HUABIO, China), GAPDH (K200102M, Solarbio, China), and Ki-67 (PT0321R, Immunoway, China).

    Techniques: Inhibition, CCK-8 Assay, Expressing, Quantitative RT-PCR, Western Blot, Control

    Tunicamycin (TM) reverses sorafenib resistance by upregulating C/EBP-β. ( A ) Western blot analysis of C/EBP-β protein levels in parental Huh7 and resistant Huh7-R cells treated with increasing concentrations of TM (0, 2, 4, 8 μM) for 48 h. ( B ) RT-qPCR analysis of relative C/EBP-β mRNA levels in cells treated as in ( A ). ( C ) Cell viability of Huh7-R cells was measured by CCK-8 assay. Cells were treated with 8 μM sorafenib alone or in combination with TM (2, 4, 8 μM) for the indicated durations. Parental Huh7 cells treated with 8 μM sorafenib served as a sensitive control. ( D ) Clonogenic potential of cells treated as in ( C ). Representative images (left) and quantification (right) are shown. ( E ) Western blot validation of C/EBP-β overexpression (C/EBP-β-oe) and knockdown (shC/EBP-β) in Huh7-R cells under various treatment conditions. ( F ) Cell viability (CCK-8) of genetically modified or unmodified Huh7-R cells treated with sorafenib (8 μM) with or without TM (4 μM) for 48 h. ( G ) Cell viability (CCK-8) of HepG2-R cells treated as in ( F ). ( H ) Clonogenic potential of Huh7-R cells treated as in ( F ). ( I ) Clonogenic potential of HepG2-R cells treated as in ( F ). The “+” and “-” signs indicate the presence or absence of the specified treatment, respectively. All quantitative data are presented as mean ± SD from three independent experiments. * P < 0.05, ** P < 0.01, and *** P < 0.001 compared between indicated groups.

    Journal: Journal of Hepatocellular Carcinoma

    Article Title: C/EBP-β Mediates the Reversal of Sorafenib Resistance by Tunicamycin in Hepatocellular Carcinoma

    doi: 10.2147/JHC.S587037

    Figure Lengend Snippet: Tunicamycin (TM) reverses sorafenib resistance by upregulating C/EBP-β. ( A ) Western blot analysis of C/EBP-β protein levels in parental Huh7 and resistant Huh7-R cells treated with increasing concentrations of TM (0, 2, 4, 8 μM) for 48 h. ( B ) RT-qPCR analysis of relative C/EBP-β mRNA levels in cells treated as in ( A ). ( C ) Cell viability of Huh7-R cells was measured by CCK-8 assay. Cells were treated with 8 μM sorafenib alone or in combination with TM (2, 4, 8 μM) for the indicated durations. Parental Huh7 cells treated with 8 μM sorafenib served as a sensitive control. ( D ) Clonogenic potential of cells treated as in ( C ). Representative images (left) and quantification (right) are shown. ( E ) Western blot validation of C/EBP-β overexpression (C/EBP-β-oe) and knockdown (shC/EBP-β) in Huh7-R cells under various treatment conditions. ( F ) Cell viability (CCK-8) of genetically modified or unmodified Huh7-R cells treated with sorafenib (8 μM) with or without TM (4 μM) for 48 h. ( G ) Cell viability (CCK-8) of HepG2-R cells treated as in ( F ). ( H ) Clonogenic potential of Huh7-R cells treated as in ( F ). ( I ) Clonogenic potential of HepG2-R cells treated as in ( F ). The “+” and “-” signs indicate the presence or absence of the specified treatment, respectively. All quantitative data are presented as mean ± SD from three independent experiments. * P < 0.05, ** P < 0.01, and *** P < 0.001 compared between indicated groups.

    Article Snippet: The following primary antibodies were used for Western blot and immunohistochemistry: C/EBP-β (A0711, Abclonal, China), p53 (ET1601-13, HUABIO, China), Bax (ET1603-34, HUABIO, China), Bcl-2 (ET1702-53, HUABIO, China), Cleaved Caspase-3 (ET1602-47, HUABIO, China), GAPDH (K200102M, Solarbio, China), and Ki-67 (PT0321R, Immunoway, China).

    Techniques: Western Blot, Quantitative RT-PCR, CCK-8 Assay, Control, Biomarker Discovery, Over Expression, Knockdown, Genetically Modified

    TM and C/EBP-β overexpression cooperatively suppress sorafenib-resistant tumor growth in vivo. Nude mice were treated with sorafenib (15 mg/kg/day) alone (control), sorafenib plus tunicamycin (TM, 0.04 mg/kg/day), sorafenib plus C/EBP-β overexpression (C/EBP-β-oe), or a combination of sorafenib, TM, and C/EBP-β-oe. ( A – D ) Subcutaneous xenograft model using Huh7-R cells. ( A ) Representative images of excised tumors from each treatment group on day 38. ( B ) Tumor growth curves measured over a 38-day treatment period. Data are presented as mean ± SD (n=6 mice per group). **P< 0.01 and ***P< 0.001 compared with the sorafenib-only group. ## P< 0.01 compared between indicated groups. ( C ) H&E staining of tumor sections showing tumor morphology and cell density. Scale bars, 50 μm. ( D ) Immunohistochemical staining for C/EBP-β and proliferation marker Ki-67 in tumor tissues. Scale bars, 50 μm. ( E and F ) Orthotopic xenograft model of Huh7-R cells. ( E ) Representative images of the liver illustrating intrahepatic tumor burden at the experimental endpoint. ( F ) Representative H&E staining of liver sections from the orthotopic model, with insets providing magnified views of tumor foci. Scale bars: 100 μm (main) and 50 μm (inset). The “+” and “-” signs indicate the presence or absence of the specified treatment, respectively.

    Journal: Journal of Hepatocellular Carcinoma

    Article Title: C/EBP-β Mediates the Reversal of Sorafenib Resistance by Tunicamycin in Hepatocellular Carcinoma

    doi: 10.2147/JHC.S587037

    Figure Lengend Snippet: TM and C/EBP-β overexpression cooperatively suppress sorafenib-resistant tumor growth in vivo. Nude mice were treated with sorafenib (15 mg/kg/day) alone (control), sorafenib plus tunicamycin (TM, 0.04 mg/kg/day), sorafenib plus C/EBP-β overexpression (C/EBP-β-oe), or a combination of sorafenib, TM, and C/EBP-β-oe. ( A – D ) Subcutaneous xenograft model using Huh7-R cells. ( A ) Representative images of excised tumors from each treatment group on day 38. ( B ) Tumor growth curves measured over a 38-day treatment period. Data are presented as mean ± SD (n=6 mice per group). **P< 0.01 and ***P< 0.001 compared with the sorafenib-only group. ## P< 0.01 compared between indicated groups. ( C ) H&E staining of tumor sections showing tumor morphology and cell density. Scale bars, 50 μm. ( D ) Immunohistochemical staining for C/EBP-β and proliferation marker Ki-67 in tumor tissues. Scale bars, 50 μm. ( E and F ) Orthotopic xenograft model of Huh7-R cells. ( E ) Representative images of the liver illustrating intrahepatic tumor burden at the experimental endpoint. ( F ) Representative H&E staining of liver sections from the orthotopic model, with insets providing magnified views of tumor foci. Scale bars: 100 μm (main) and 50 μm (inset). The “+” and “-” signs indicate the presence or absence of the specified treatment, respectively.

    Article Snippet: The following primary antibodies were used for Western blot and immunohistochemistry: C/EBP-β (A0711, Abclonal, China), p53 (ET1601-13, HUABIO, China), Bax (ET1603-34, HUABIO, China), Bcl-2 (ET1702-53, HUABIO, China), Cleaved Caspase-3 (ET1602-47, HUABIO, China), GAPDH (K200102M, Solarbio, China), and Ki-67 (PT0321R, Immunoway, China).

    Techniques: Over Expression, In Vivo, Control, Staining, Immunohistochemical staining, Marker

    The C/EBP-β axis overcomes sorafenib resistance by inducing ROS production and apoptosis in Huh7-R cells. Huh7-R cells were treated for 48 h with sorafenib (8 μM) alone or in combination with C/EBP-β overexpression (C/EBP-β-oe), tunicamycin (TM, 4 μM), TM plus shC/EBP-β, or TM plus NAC (5 mM). Hydrogen peroxide (H 2 O 2 , 2 mM) was included as a positive control for ROS generation. ( A ) Intracellular ROS levels were detected using DCFDA staining and visualized using fluorescence microscopy. Scale bar, 200 μm. ( B ) Quantification of the relative fluorescence intensity from ( A ). ( C ) Apoptosis was detected using the TUNEL assay, with TUNEL-positive nuclei stained green and all nuclei counterstained with DAPI (blue). Scale bar, 100 μm. ( D ) Percentage of TUNEL-positive cells from ( C ). ( E ) Western blot analysis of C/EBP-β, p53, Bax, Bcl-2, and cleaved caspase-3 protein levels. GAPDH was used as an internal control. The “+” and “-” signs indicate the presence or absence of the specified treatment, respectively. All quantitative data are presented as mean ± SD from three independent experiments. * P < 0.05, ** P < 0.01, and *** P < 0.001 compared between indicated groups.

    Journal: Journal of Hepatocellular Carcinoma

    Article Title: C/EBP-β Mediates the Reversal of Sorafenib Resistance by Tunicamycin in Hepatocellular Carcinoma

    doi: 10.2147/JHC.S587037

    Figure Lengend Snippet: The C/EBP-β axis overcomes sorafenib resistance by inducing ROS production and apoptosis in Huh7-R cells. Huh7-R cells were treated for 48 h with sorafenib (8 μM) alone or in combination with C/EBP-β overexpression (C/EBP-β-oe), tunicamycin (TM, 4 μM), TM plus shC/EBP-β, or TM plus NAC (5 mM). Hydrogen peroxide (H 2 O 2 , 2 mM) was included as a positive control for ROS generation. ( A ) Intracellular ROS levels were detected using DCFDA staining and visualized using fluorescence microscopy. Scale bar, 200 μm. ( B ) Quantification of the relative fluorescence intensity from ( A ). ( C ) Apoptosis was detected using the TUNEL assay, with TUNEL-positive nuclei stained green and all nuclei counterstained with DAPI (blue). Scale bar, 100 μm. ( D ) Percentage of TUNEL-positive cells from ( C ). ( E ) Western blot analysis of C/EBP-β, p53, Bax, Bcl-2, and cleaved caspase-3 protein levels. GAPDH was used as an internal control. The “+” and “-” signs indicate the presence or absence of the specified treatment, respectively. All quantitative data are presented as mean ± SD from three independent experiments. * P < 0.05, ** P < 0.01, and *** P < 0.001 compared between indicated groups.

    Article Snippet: The following primary antibodies were used for Western blot and immunohistochemistry: C/EBP-β (A0711, Abclonal, China), p53 (ET1601-13, HUABIO, China), Bax (ET1603-34, HUABIO, China), Bcl-2 (ET1702-53, HUABIO, China), Cleaved Caspase-3 (ET1602-47, HUABIO, China), GAPDH (K200102M, Solarbio, China), and Ki-67 (PT0321R, Immunoway, China).

    Techniques: Over Expression, Positive Control, Staining, Fluorescence, Microscopy, TUNEL Assay, Western Blot, Control

    Integrated bioinformatic analyses define the C/EBP-β-dependent transcriptomic mechanism of tunicamycin in HCC. ( A ) Representative Gene Set Enrichment Analysis (GSEA) plots from the TCGA-LIHC dataset showing positive enrichment of apoptosis (TWEAK signaling) and ER stress (ATF4 activation) pathways in tumors with high C/EBP-β expression. ( B ) Venn diagram illustrating the identification of 185 intersecting genes between potential Tunicamycin (TM) targets (from SwissTarget, Pharmmapper, and DrugBank) and known hepatocellular carcinoma (HCC) disease genes (from GeneCards and OMIM). ( C ) GO (Biological Process) and KEGG pathway enrichment analysis of the 185 intersecting genes identified in (B). The bubble plot displays top enriched terms, with bubble size corresponding to gene count and color intensity reflecting the adjusted P -value. ( D ) GO enrichment analysis (Biological Process) of the 13 core genes at the intersection of TM’s potential targets and C/EBP-β-regulated differentially expressed genes. The bar chart highlights “intrinsic apoptotic signaling pathway in response to ER stress” and “multiple cell differentiation-related pathways” as the key convergent mechanisms.

    Journal: Journal of Hepatocellular Carcinoma

    Article Title: C/EBP-β Mediates the Reversal of Sorafenib Resistance by Tunicamycin in Hepatocellular Carcinoma

    doi: 10.2147/JHC.S587037

    Figure Lengend Snippet: Integrated bioinformatic analyses define the C/EBP-β-dependent transcriptomic mechanism of tunicamycin in HCC. ( A ) Representative Gene Set Enrichment Analysis (GSEA) plots from the TCGA-LIHC dataset showing positive enrichment of apoptosis (TWEAK signaling) and ER stress (ATF4 activation) pathways in tumors with high C/EBP-β expression. ( B ) Venn diagram illustrating the identification of 185 intersecting genes between potential Tunicamycin (TM) targets (from SwissTarget, Pharmmapper, and DrugBank) and known hepatocellular carcinoma (HCC) disease genes (from GeneCards and OMIM). ( C ) GO (Biological Process) and KEGG pathway enrichment analysis of the 185 intersecting genes identified in (B). The bubble plot displays top enriched terms, with bubble size corresponding to gene count and color intensity reflecting the adjusted P -value. ( D ) GO enrichment analysis (Biological Process) of the 13 core genes at the intersection of TM’s potential targets and C/EBP-β-regulated differentially expressed genes. The bar chart highlights “intrinsic apoptotic signaling pathway in response to ER stress” and “multiple cell differentiation-related pathways” as the key convergent mechanisms.

    Article Snippet: The following primary antibodies were used for Western blot and immunohistochemistry: C/EBP-β (A0711, Abclonal, China), p53 (ET1601-13, HUABIO, China), Bax (ET1603-34, HUABIO, China), Bcl-2 (ET1702-53, HUABIO, China), Cleaved Caspase-3 (ET1602-47, HUABIO, China), GAPDH (K200102M, Solarbio, China), and Ki-67 (PT0321R, Immunoway, China).

    Techniques: Activation Assay, Expressing, Cell Differentiation