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  • 96
    Millipore anti bax
    Effect of PT on the release of apoptosis-related proteins and MMP in RI-T cells. (A) Changes of <t>Bcl-X</t> L , Bcl-2, and <t>Bax</t> expressions in RI-T cells treated with PT. (B) Cells stained with rhodamine 123 were counted with a FACStar flow cytometer. The graph shows percentages of rhodamine 123 negative cells. * P
    Anti Bax, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 427 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore bax
    Altered Bcl-xl and <t>DAPK-2</t> expression in EpoR-HM erythroblasts. (Ai) Levels of Bcl-xl in expanded wt-EpoR, EpoR-HM, and EpoR-H erythroblasts were assayed (by Western blotting) at 2 time points—directly following cytokine withdrawal and at 30 minutes of Epo exposure. Note the decreased Bcl-xl levels in EpoR-HM erythroblasts. For comparison, <t>Bax</t> levels also were analyzed. (Aii) Bcl-xl expression in wt-EpoR, EpoR-HM, and EpoR-H erythroblasts also was analyzed in Ter119-depleted, CD71 high erythroblasts. (B) Defective survival of EpoR-HM CD71 high Kit neg erythroblasts and rescue of survival potential by PY343 in EpoR-H. Kit pos progenitor cells were prepared from wt-EpoR, EpoR-HM, and EpoR-H bone marrow and were expanded in SP34-EX media. At day 3 of culture, CD71 and Ter119 marker expression was assayed and cells were costained with annexin-V. Relative frequencies of annexin-V–positive cells among CD71 pos subpopulations of EpoR-HM, EpoR-H, and wt-EpoR erythroblasts are graphed. Expanded cells also were shifted to differentiation medium, and frequencies of annexin-V and Ter119–copositive cells were analyzed. (C) Elevated DAPK-2 expression in EpoR-HM erythroblasts. Death-associated protein kinase-2 (DAPK-2) expression in wt-EpoR, EpoR-HM, and EpoR-H erythroblasts was assayed by Western blotting (and digital densitometry). Note the several fold increase in DAPK-2 levels in EpoR-HM erythroblasts (representative of 3 independent experiments). For Bcl-xl, plotted quantitation values are mean values plus or minus SE; n = 3 wt-EpoR, EpoR-HM, and EpoR-H mice per group, x = 2 experiments. For annexin-V staining, plotted values are mean values plus or minus SE; n = 3 wt-EpoR, EpoR-HM, and EpoR-H mice per group, x = 4 experiments.
    Bax, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 1064 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bax/product/Millipore
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    95
    ABclonal bax
    Genistein reduce the protein expression of Notch-1 and induce the expression of <t>Bax/Bcl-2,</t> <t>Caspase-8.</t> Western blot analysis were carried out to demonstrated the of expression of Notch-1, Bax, Bcl-2 and Caspase-8 in HT-29 cells treated by genistein (200 μmol/L) and TNF-α (10 ng/ml) respectively for 48 h. Density of the bands were quantified by a densitometry analysis. Data are presented after normalization by β-actin. The data shown are representative of three independent experiments. (* p
    Bax, supplied by ABclonal, used in various techniques. Bioz Stars score: 95/100, based on 184 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bax/product/ABclonal
    Average 95 stars, based on 184 article reviews
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    95
    Cell Signaling Technology Inc bax
    HgCl 2 induced apoptosis is reduced in KO mice a) TUNEL nuclear staining in renal cortex, 24h after HgCl 2 treatment and b) quantitation which shows reduced TUNEL positive nuclei in KO group. c) Cleaved <t>caspase</t> 3 and activated <t>Bax</t> levels are lower by Western blot in KO kidney compared to WT (d e). **, P
    Bax, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 13298 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bax/product/Cell Signaling Technology Inc
    Average 95 stars, based on 13298 article reviews
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    99
    Cell Signaling Technology Inc total bax
    rHMGB1 exerted no effect on protein expression of <t>Bax</t> and Bcl2 in neonatal rat cardiomyocytes. (A) Western blot analysis of <t>cytosolic</t> Bax (cyto-Bax) in the presence of rHMGB1. (B)Total cellular protein expression of Bax. (C) Total cellular protein expression of Bcl2. β-actin served as a loading control. Results are means ± SEM. Each experiment was repeated three times.
    Total Bax, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/total bax/product/Cell Signaling Technology Inc
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    bax  (Abcam)
    94
    Abcam bax
    Upper panel- Representative western blotting detection of p65, <t>p53,</t> securin, <t>bax</t> and β-actin in mouse bone marrow (BM), esophagus and stomach cells after exposure with RAN extract with or without lime. For BM, cells were collected after 60, 120 and 180 days, whereas for esophagus and stomach, cells were collected only after 180 days of exposure. β-actin was used as loading control. Lower panel- Quantitative densitometric analysis of the level of proteins of the above mentioned genes in bone marrow, esophagus and stomach cells after 180 days of exposure was shown. The values are the mean ± SD of three independent experiments. The values are normalized to respective β-actin values. * p
    Bax, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 4743 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bax/product/Abcam
    Average 94 stars, based on 4743 article reviews
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    88
    Novoprotein bax a
    Upper panel- Representative western blotting detection of p65, <t>p53,</t> securin, <t>bax</t> and β-actin in mouse bone marrow (BM), esophagus and stomach cells after exposure with RAN extract with or without lime. For BM, cells were collected after 60, 120 and 180 days, whereas for esophagus and stomach, cells were collected only after 180 days of exposure. β-actin was used as loading control. Lower panel- Quantitative densitometric analysis of the level of proteins of the above mentioned genes in bone marrow, esophagus and stomach cells after 180 days of exposure was shown. The values are the mean ± SD of three independent experiments. The values are normalized to respective β-actin values. * p
    Bax A, supplied by Novoprotein, used in various techniques. Bioz Stars score: 88/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bax a/product/Novoprotein
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    94
    Millipore anti bax antibody
    lncRNA <t>F11‐AS1/miR‐211‐5p/NR1I3</t> axis regulates the proliferation, apoptosis, migration and invasion of HepG2.2.15 cells. A, The mRNA expression of <t>Bax,</t> Bcl‐2 and PCNA in HepG2.2.15 cells after transduction determined by RT‐qPCR. B, The protein expression of Bax, Bcl‐2 and PCNA in HepG2.2.15 cells after transduction measured by Western blot analysis. C, The proliferative ability of HepG2.2.15 cells after transduction assessed by CCK‐8 assay. D, the apoptosis rate of HepG2.2.15 cells after transduction evaluated by TUNEL staining. E, The migration ability of HepG2.2.15 cells after transduction assessed by scratch test (×40). F, The invasion ability of HepG2.2.15 cells after transduction determined by Transwell assay (×200). Data were measurement data and expressed by mean ± standard deviation. * P
    Anti Bax Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 259 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti bax antibody/product/Millipore
    Average 94 stars, based on 259 article reviews
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    Image Search Results


    Effect of PT on the release of apoptosis-related proteins and MMP in RI-T cells. (A) Changes of Bcl-X L , Bcl-2, and Bax expressions in RI-T cells treated with PT. (B) Cells stained with rhodamine 123 were counted with a FACStar flow cytometer. The graph shows percentages of rhodamine 123 negative cells. * P

    Journal: Experimental & Molecular Medicine

    Article Title: Parthenolide-induced apoptosis of hepatic stellate cells and anti-fibrotic effects in an in vivo rat model

    doi: 10.3858/emm.2012.44.7.051

    Figure Lengend Snippet: Effect of PT on the release of apoptosis-related proteins and MMP in RI-T cells. (A) Changes of Bcl-X L , Bcl-2, and Bax expressions in RI-T cells treated with PT. (B) Cells stained with rhodamine 123 were counted with a FACStar flow cytometer. The graph shows percentages of rhodamine 123 negative cells. * P

    Article Snippet: Samples were then probed with anti-α-SMA, anti-Bax, anti-Bcl-2, anti-Bcl-XL , anti-caspase-3, anti-poly-(ADP-ribose)-polymerase (PARP), anti-GFAP (Millipore), and anti-actin (Santa Cruz Biotechnology, SantaCruz, CA) antibodies.

    Techniques: Staining, Flow Cytometry, Cytometry

    Docetaxel is killing the cells through a non-apoptotic mechanism. ( a ) MDA-MB-231 cells stably expressing vector or BAD were treated with DMSO control (left) or 125 nM docetaxel (middle) and subjected to western blot. Right: Protein band quantification was performed. Student’s t -test; no statistical significance. ( b ) Cells were treated with 125 nM docetaxel for 3 days prior to immunoprecipitation (IP) with 6A7 BAX antibody. Vimentin antibody was used as a negative control. Input lanes were also probed with cleaved caspase-3 antibody (right). ( c ) Cells were treated with 125 nM docetaxel for 5 days and stained with Annexin V-647 and PI daily and analyzed via flow cytometry. The Annexin V+/PI− population is graphed. Student’s t -test; no statistical significance between vector and BAD. Right: Dot plots from flow cytometric analysis. Annexin V positive cells are on the x-axis, PI positive cells are on the y-axis. Time, in days, is increasing to the right.

    Journal: Scientific Reports

    Article Title: BAD sensitizes breast cancer cells to docetaxel with increased mitotic arrest and necroptosis

    doi: 10.1038/s41598-019-57282-1

    Figure Lengend Snippet: Docetaxel is killing the cells through a non-apoptotic mechanism. ( a ) MDA-MB-231 cells stably expressing vector or BAD were treated with DMSO control (left) or 125 nM docetaxel (middle) and subjected to western blot. Right: Protein band quantification was performed. Student’s t -test; no statistical significance. ( b ) Cells were treated with 125 nM docetaxel for 3 days prior to immunoprecipitation (IP) with 6A7 BAX antibody. Vimentin antibody was used as a negative control. Input lanes were also probed with cleaved caspase-3 antibody (right). ( c ) Cells were treated with 125 nM docetaxel for 5 days and stained with Annexin V-647 and PI daily and analyzed via flow cytometry. The Annexin V+/PI− population is graphed. Student’s t -test; no statistical significance between vector and BAD. Right: Dot plots from flow cytometric analysis. Annexin V positive cells are on the x-axis, PI positive cells are on the y-axis. Time, in days, is increasing to the right.

    Article Snippet: BAD, tubulin and BAX conformational antibody clone 6A7 were from Sigma-Aldrich.

    Techniques: Multiple Displacement Amplification, Stable Transfection, Expressing, Plasmid Preparation, Western Blot, Immunoprecipitation, Negative Control, Staining, Flow Cytometry, Cytometry

    Bax/Bcl-2 ratio in ARPE-19 cells following treatment with vital dyes. Confluent ARPE-19 cells were treated with 0.05 mg/ml indocyanine green (ICG), acid violet (AcV), brilliant blue (BriB) and methyl blue (MetB) for 3 minutes in BSS. Total RNA and proteins were extracted to assess Bax ( A ) and Bcl-2 ( C ) mRNA expression and Bax ( B ) and Bcl-2 ( D ) protein expression by real-time PCR and Western blot respectively. GAPDH was used as the internal control. Representative Western blot gel ( Top ) of proapoptotic protein Bax ( B ) and antiapoptotic protein Bcl-2 ( D ). The numbers to the left are molecular weights in kilodaltons (kDa). Bottom : average densitometry results from three independent experiments. ( E ) Bax/Bcl-2 protein ratio. Data are mean ± SE and represent the average results of 3 independent experiments run in duplicate. * is p

    Journal: PLoS ONE

    Article Title: Retinal Pigmented Epithelial Cells Cytotoxicity and Apoptosis through Activation of the Mitochondrial Intrinsic Pathway: Role Of Indocyanine Green, Brilliant Blue and Implications for Chromovitrectomy

    doi: 10.1371/journal.pone.0064094

    Figure Lengend Snippet: Bax/Bcl-2 ratio in ARPE-19 cells following treatment with vital dyes. Confluent ARPE-19 cells were treated with 0.05 mg/ml indocyanine green (ICG), acid violet (AcV), brilliant blue (BriB) and methyl blue (MetB) for 3 minutes in BSS. Total RNA and proteins were extracted to assess Bax ( A ) and Bcl-2 ( C ) mRNA expression and Bax ( B ) and Bcl-2 ( D ) protein expression by real-time PCR and Western blot respectively. GAPDH was used as the internal control. Representative Western blot gel ( Top ) of proapoptotic protein Bax ( B ) and antiapoptotic protein Bcl-2 ( D ). The numbers to the left are molecular weights in kilodaltons (kDa). Bottom : average densitometry results from three independent experiments. ( E ) Bax/Bcl-2 protein ratio. Data are mean ± SE and represent the average results of 3 independent experiments run in duplicate. * is p

    Article Snippet: Primary antibodies Bax, BcL-2, cytochrome c, and caspase-9, were purchased from EMD Millipore Corporation (Billerica, MA, USA).

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Western Blot

    Interdependence of Bak and Bax activation. (A) A Bak mutant (m2, I85A/N86A) that fails to be bound by Bcl-xL and Mcl-1 sensitizes BaxBak DKO cells to camptothecin. GFP-Bak or GFP-Bak m2 was stably expressed in BaxBak DKO cells. Cells were treated with 1 μM camptothecin and Cyt.c release was examined. The experiment was repeated twice and representative data were shown as average±SD. (B) Bak expression levels in transiently expressed or stably expressed cells shown by Western blotting. Asteries indicate degraded Bak bands. (C) Caspase-3/7 acitivity was measured in indicated cell lines transiently transfected with GFP-Bax, GFP-Bak or in combination with GFP-Mcl-1 or GFP-Bcl-xL (1:3 ratio of DNA amount). Fold change was normalized with cells transfected with GFP-C1 vector control. The experiment was repeated twice and representative data were shown as average±SD. (D) Bak activation occurs normally in wild type cells in response to camptothecin and ABT-737 treatment detected by immunoprecipitation with anti-Bak (ab-1) antibody. Asteria indicates the light chain of Ig. (E) Bak activation indicated by Bak foci. GFP-Bak was stably expressed in Bak KO and BaxBak DKO cells. Cells were treated with 20 μM ABT-737, 1 μM camptothecin or 50 ng/ml TRAIL plus 375 μM 5-FU in the presence of 10 μM Q-VD for 24 h. (F) Bak activation in GFP-Bak stably expressing cells. Cells were treated and immnuoprecipitated as in (D). (G) Bcl-xL, VDAC2 and Mcl-1 express normally in Bax KO and Bak KO cells. The p-value was obtained using the Student’s t-test.*, p

    Journal: Oncogene

    Article Title: Predominant requirement of Bax for apoptosis in HCT116 cells is determined by Mcl-1's inhibitory effect on Bak

    doi: 10.1038/onc.2011.497

    Figure Lengend Snippet: Interdependence of Bak and Bax activation. (A) A Bak mutant (m2, I85A/N86A) that fails to be bound by Bcl-xL and Mcl-1 sensitizes BaxBak DKO cells to camptothecin. GFP-Bak or GFP-Bak m2 was stably expressed in BaxBak DKO cells. Cells were treated with 1 μM camptothecin and Cyt.c release was examined. The experiment was repeated twice and representative data were shown as average±SD. (B) Bak expression levels in transiently expressed or stably expressed cells shown by Western blotting. Asteries indicate degraded Bak bands. (C) Caspase-3/7 acitivity was measured in indicated cell lines transiently transfected with GFP-Bax, GFP-Bak or in combination with GFP-Mcl-1 or GFP-Bcl-xL (1:3 ratio of DNA amount). Fold change was normalized with cells transfected with GFP-C1 vector control. The experiment was repeated twice and representative data were shown as average±SD. (D) Bak activation occurs normally in wild type cells in response to camptothecin and ABT-737 treatment detected by immunoprecipitation with anti-Bak (ab-1) antibody. Asteria indicates the light chain of Ig. (E) Bak activation indicated by Bak foci. GFP-Bak was stably expressed in Bak KO and BaxBak DKO cells. Cells were treated with 20 μM ABT-737, 1 μM camptothecin or 50 ng/ml TRAIL plus 375 μM 5-FU in the presence of 10 μM Q-VD for 24 h. (F) Bak activation in GFP-Bak stably expressing cells. Cells were treated and immnuoprecipitated as in (D). (G) Bcl-xL, VDAC2 and Mcl-1 express normally in Bax KO and Bak KO cells. The p-value was obtained using the Student’s t-test.*, p

    Article Snippet: Anti-Bax NT and anti-Bak NT were from Upstate (Waltham, MA), anti-Bak ab-1 from Calbiochem (San Diego, CA), anti-PARP from Biomol (Plymouth, PA), anti-VADC2 from Abcam (Cambridge, MA), anti-Mcl-1 from Santa Cruz Biotechnology or Abcam (Cambridge, MA) and anti-Actin from Sigma.

    Techniques: Activation Assay, Mutagenesis, Stable Transfection, Expressing, Western Blot, Transfection, Plasmid Preparation, Immunoprecipitation

    Comparison of Bax/Bak-mediated cell death in HCT116 and MEF cells. (A-B) Caspase-3/7 activity in indicated MEF (A) or HCT116 (B) cell lines treated with 0.2 μM staurosporine. Fold change of caspase activity was normalized to untreated controls. The experiment was repeated twice and representative data were shown as average±SD. (C-D) Caspase-3/7 activity (C) or Cyt.c release (D) in indicated MEF cell lines treated with ABT-737. The experiment was repeated twice and representative data were shown as average±SD. (E-F) Cyt.c release in HCT116 (E) or MEF (F) cells transfected with GFP-tagged BH-3 only proteins and GFP-Bcl-xS for 24 hrs. GFP-C1 vector was used as a control. The experiment was repeated twice and representative data were shown as average±SD. The p-value was obtained using the Student’s t-test. *, p

    Journal: Oncogene

    Article Title: Predominant requirement of Bax for apoptosis in HCT116 cells is determined by Mcl-1's inhibitory effect on Bak

    doi: 10.1038/onc.2011.497

    Figure Lengend Snippet: Comparison of Bax/Bak-mediated cell death in HCT116 and MEF cells. (A-B) Caspase-3/7 activity in indicated MEF (A) or HCT116 (B) cell lines treated with 0.2 μM staurosporine. Fold change of caspase activity was normalized to untreated controls. The experiment was repeated twice and representative data were shown as average±SD. (C-D) Caspase-3/7 activity (C) or Cyt.c release (D) in indicated MEF cell lines treated with ABT-737. The experiment was repeated twice and representative data were shown as average±SD. (E-F) Cyt.c release in HCT116 (E) or MEF (F) cells transfected with GFP-tagged BH-3 only proteins and GFP-Bcl-xS for 24 hrs. GFP-C1 vector was used as a control. The experiment was repeated twice and representative data were shown as average±SD. The p-value was obtained using the Student’s t-test. *, p

    Article Snippet: Anti-Bax NT and anti-Bak NT were from Upstate (Waltham, MA), anti-Bak ab-1 from Calbiochem (San Diego, CA), anti-PARP from Biomol (Plymouth, PA), anti-VADC2 from Abcam (Cambridge, MA), anti-Mcl-1 from Santa Cruz Biotechnology or Abcam (Cambridge, MA) and anti-Actin from Sigma.

    Techniques: Activity Assay, Transfection, Plasmid Preparation

    Bak deficiency provides no protection against many apoptotic stimuli. (A) Cell viability assay in wild type, Bak KO, Bax KO and BaxBak DKO cells with 500 μM indomethacin and 120 μM sulindac acid treatment for 48h. Cell viability was measured with Promega’s CellTiter-Glo luminescent cell viability assay and normalized to non-treatment controls. The experiment was repeated three times and representative data were shown as average±SD. Since non-treated cells proliferate at a greater rate than the treated cells, this assay underestimates the survival rate of treated cells. (B) PARP cleavage in indicated cell lines with 1 μM camptothecin and 500 μM indomethacin treatment. (C) Cyt. c release in indicated cell lines with 1 μM camptothecin (camp), 500 μM indomethacin (indo) and 20 μM ABT-737. The experiment was repeated three times and representative data were shown as average±SD. (D) Caspase-3/7 activity in indicated cell lines with 20 μM ABT-737 treatment. The experiment was repeated twice and representative data were shown as average±SD. (E) Caspase-3/7 activity in indicated cell lines with different concentrations of ABT-737 for 24h. Representative data were shown as average±SD. (F) Clonogenic assay of tested cell lines with 120 μM sulindac acid, 0.2 μM staurosporine and 20 μM ABT-737 treatment. The experiment was repeated three times and a representative image was shown. The p-value was obtained using the Student’s t-test. *, p

    Journal: Oncogene

    Article Title: Predominant requirement of Bax for apoptosis in HCT116 cells is determined by Mcl-1's inhibitory effect on Bak

    doi: 10.1038/onc.2011.497

    Figure Lengend Snippet: Bak deficiency provides no protection against many apoptotic stimuli. (A) Cell viability assay in wild type, Bak KO, Bax KO and BaxBak DKO cells with 500 μM indomethacin and 120 μM sulindac acid treatment for 48h. Cell viability was measured with Promega’s CellTiter-Glo luminescent cell viability assay and normalized to non-treatment controls. The experiment was repeated three times and representative data were shown as average±SD. Since non-treated cells proliferate at a greater rate than the treated cells, this assay underestimates the survival rate of treated cells. (B) PARP cleavage in indicated cell lines with 1 μM camptothecin and 500 μM indomethacin treatment. (C) Cyt. c release in indicated cell lines with 1 μM camptothecin (camp), 500 μM indomethacin (indo) and 20 μM ABT-737. The experiment was repeated three times and representative data were shown as average±SD. (D) Caspase-3/7 activity in indicated cell lines with 20 μM ABT-737 treatment. The experiment was repeated twice and representative data were shown as average±SD. (E) Caspase-3/7 activity in indicated cell lines with different concentrations of ABT-737 for 24h. Representative data were shown as average±SD. (F) Clonogenic assay of tested cell lines with 120 μM sulindac acid, 0.2 μM staurosporine and 20 μM ABT-737 treatment. The experiment was repeated three times and a representative image was shown. The p-value was obtained using the Student’s t-test. *, p

    Article Snippet: Anti-Bax NT and anti-Bak NT were from Upstate (Waltham, MA), anti-Bak ab-1 from Calbiochem (San Diego, CA), anti-PARP from Biomol (Plymouth, PA), anti-VADC2 from Abcam (Cambridge, MA), anti-Mcl-1 from Santa Cruz Biotechnology or Abcam (Cambridge, MA) and anti-Actin from Sigma.

    Techniques: Viability Assay, Cell Viability Assay, Activity Assay, Clonogenic Assay

    Bak is kept in check by Mcl-1 in Bax KO cells. (A) BH3-only proteins display different killing profiles to Bax KO cells shown by caspase-3/7 activity normalized to GFP-C1 vector control. BH3-only proteins were transiently expressed in the indicated cell lines and caspase-3/7 activity was measured 18 h after transfection. The experiment was repeated three times and representative data were shown as average±SD. (B) Noxa and NBK sensitize Bax KO cells to ABT-737. Puma, NBK or Noxa was transiently transfected and 20 μMABT-737 was added to the cells during transfection. Caspase-3/7 activity was measured 24 h after transfection and normalized to GFP-C1 vector control. The experiment was repeated twice and representative data were shown as average±SD. (C) Bcl-xS sensitizes cells to ABT-737 and Noxa sensitizes Bax KO cells to NBK. Untagged Bcl-xS, GFP-NBK and GFP-Noxa were transiently transfected and 20 μM ABT-737 was added during transfection. The experiment was repeated twice and representative data were shown as average±SD. (D-E) Protein levels of transiently expressed pro-and anti-apoptotic genes detected by Western blotting in HCT116 WT cells (E) and BaxBak DKO HCT116 cells (E). The p-value was obtained using the Student’s t-test.*, p

    Journal: Oncogene

    Article Title: Predominant requirement of Bax for apoptosis in HCT116 cells is determined by Mcl-1's inhibitory effect on Bak

    doi: 10.1038/onc.2011.497

    Figure Lengend Snippet: Bak is kept in check by Mcl-1 in Bax KO cells. (A) BH3-only proteins display different killing profiles to Bax KO cells shown by caspase-3/7 activity normalized to GFP-C1 vector control. BH3-only proteins were transiently expressed in the indicated cell lines and caspase-3/7 activity was measured 18 h after transfection. The experiment was repeated three times and representative data were shown as average±SD. (B) Noxa and NBK sensitize Bax KO cells to ABT-737. Puma, NBK or Noxa was transiently transfected and 20 μMABT-737 was added to the cells during transfection. Caspase-3/7 activity was measured 24 h after transfection and normalized to GFP-C1 vector control. The experiment was repeated twice and representative data were shown as average±SD. (C) Bcl-xS sensitizes cells to ABT-737 and Noxa sensitizes Bax KO cells to NBK. Untagged Bcl-xS, GFP-NBK and GFP-Noxa were transiently transfected and 20 μM ABT-737 was added during transfection. The experiment was repeated twice and representative data were shown as average±SD. (D-E) Protein levels of transiently expressed pro-and anti-apoptotic genes detected by Western blotting in HCT116 WT cells (E) and BaxBak DKO HCT116 cells (E). The p-value was obtained using the Student’s t-test.*, p

    Article Snippet: Anti-Bax NT and anti-Bak NT were from Upstate (Waltham, MA), anti-Bak ab-1 from Calbiochem (San Diego, CA), anti-PARP from Biomol (Plymouth, PA), anti-VADC2 from Abcam (Cambridge, MA), anti-Mcl-1 from Santa Cruz Biotechnology or Abcam (Cambridge, MA) and anti-Actin from Sigma.

    Techniques: Activity Assay, Plasmid Preparation, Transfection, Western Blot

    Generation of Bak KO and BaxBak DKO HCT116 cells. (A) Schematic diagram of gene targeting of Bak locus. The top panel shows BH3, BH1, BH2 and the transmembrane (TM) domains of Bak protein in orange, green, pink and blue. The exons encoding the corresponding domains are labeled in the same color in the Bak genomic locus and are shown as rectangles. Shaded regions of rectangles represent coding exons. Triangles indicate LoxP sites. (B) Confirmation of Bak knockout by Western blot. #29, 36, 44 and 49 are homozygous Bak KO and #2 and #19 are homozgyous BaxBak DKO clones. Asterisk indicates a non-specific band detected by anti-Bax antibody. (C). No truncated or aberrant Bak was produced in Bak KO and BaxBak DKO HCT116 cells. Bak KO and BaxBak DKO MEFs were used as a control. anti-Bak NT recognizes the N-terminal region of Bak. (D) Final Bak ORF sequence after gene targeting. Sequence underlined is introduced by the targeting vector. LoxP site is shown in red. The two premature stop codons are shown as bold italic. Alternating coding exons are shown in black or blue color. Note that exon 1 is a non-coding exon.

    Journal: Oncogene

    Article Title: Predominant requirement of Bax for apoptosis in HCT116 cells is determined by Mcl-1's inhibitory effect on Bak

    doi: 10.1038/onc.2011.497

    Figure Lengend Snippet: Generation of Bak KO and BaxBak DKO HCT116 cells. (A) Schematic diagram of gene targeting of Bak locus. The top panel shows BH3, BH1, BH2 and the transmembrane (TM) domains of Bak protein in orange, green, pink and blue. The exons encoding the corresponding domains are labeled in the same color in the Bak genomic locus and are shown as rectangles. Shaded regions of rectangles represent coding exons. Triangles indicate LoxP sites. (B) Confirmation of Bak knockout by Western blot. #29, 36, 44 and 49 are homozygous Bak KO and #2 and #19 are homozgyous BaxBak DKO clones. Asterisk indicates a non-specific band detected by anti-Bax antibody. (C). No truncated or aberrant Bak was produced in Bak KO and BaxBak DKO HCT116 cells. Bak KO and BaxBak DKO MEFs were used as a control. anti-Bak NT recognizes the N-terminal region of Bak. (D) Final Bak ORF sequence after gene targeting. Sequence underlined is introduced by the targeting vector. LoxP site is shown in red. The two premature stop codons are shown as bold italic. Alternating coding exons are shown in black or blue color. Note that exon 1 is a non-coding exon.

    Article Snippet: Anti-Bax NT and anti-Bak NT were from Upstate (Waltham, MA), anti-Bak ab-1 from Calbiochem (San Diego, CA), anti-PARP from Biomol (Plymouth, PA), anti-VADC2 from Abcam (Cambridge, MA), anti-Mcl-1 from Santa Cruz Biotechnology or Abcam (Cambridge, MA) and anti-Actin from Sigma.

    Techniques: Labeling, Knock-Out, Western Blot, Clone Assay, Produced, Sequencing, Plasmid Preparation

    Altered Bcl-xl and DAPK-2 expression in EpoR-HM erythroblasts. (Ai) Levels of Bcl-xl in expanded wt-EpoR, EpoR-HM, and EpoR-H erythroblasts were assayed (by Western blotting) at 2 time points—directly following cytokine withdrawal and at 30 minutes of Epo exposure. Note the decreased Bcl-xl levels in EpoR-HM erythroblasts. For comparison, Bax levels also were analyzed. (Aii) Bcl-xl expression in wt-EpoR, EpoR-HM, and EpoR-H erythroblasts also was analyzed in Ter119-depleted, CD71 high erythroblasts. (B) Defective survival of EpoR-HM CD71 high Kit neg erythroblasts and rescue of survival potential by PY343 in EpoR-H. Kit pos progenitor cells were prepared from wt-EpoR, EpoR-HM, and EpoR-H bone marrow and were expanded in SP34-EX media. At day 3 of culture, CD71 and Ter119 marker expression was assayed and cells were costained with annexin-V. Relative frequencies of annexin-V–positive cells among CD71 pos subpopulations of EpoR-HM, EpoR-H, and wt-EpoR erythroblasts are graphed. Expanded cells also were shifted to differentiation medium, and frequencies of annexin-V and Ter119–copositive cells were analyzed. (C) Elevated DAPK-2 expression in EpoR-HM erythroblasts. Death-associated protein kinase-2 (DAPK-2) expression in wt-EpoR, EpoR-HM, and EpoR-H erythroblasts was assayed by Western blotting (and digital densitometry). Note the several fold increase in DAPK-2 levels in EpoR-HM erythroblasts (representative of 3 independent experiments). For Bcl-xl, plotted quantitation values are mean values plus or minus SE; n = 3 wt-EpoR, EpoR-HM, and EpoR-H mice per group, x = 2 experiments. For annexin-V staining, plotted values are mean values plus or minus SE; n = 3 wt-EpoR, EpoR-HM, and EpoR-H mice per group, x = 4 experiments.

    Journal: Blood

    Article Title: Core erythropoietin receptor signals for late erythroblast development

    doi: 10.1182/blood-2005-02-0684

    Figure Lengend Snippet: Altered Bcl-xl and DAPK-2 expression in EpoR-HM erythroblasts. (Ai) Levels of Bcl-xl in expanded wt-EpoR, EpoR-HM, and EpoR-H erythroblasts were assayed (by Western blotting) at 2 time points—directly following cytokine withdrawal and at 30 minutes of Epo exposure. Note the decreased Bcl-xl levels in EpoR-HM erythroblasts. For comparison, Bax levels also were analyzed. (Aii) Bcl-xl expression in wt-EpoR, EpoR-HM, and EpoR-H erythroblasts also was analyzed in Ter119-depleted, CD71 high erythroblasts. (B) Defective survival of EpoR-HM CD71 high Kit neg erythroblasts and rescue of survival potential by PY343 in EpoR-H. Kit pos progenitor cells were prepared from wt-EpoR, EpoR-HM, and EpoR-H bone marrow and were expanded in SP34-EX media. At day 3 of culture, CD71 and Ter119 marker expression was assayed and cells were costained with annexin-V. Relative frequencies of annexin-V–positive cells among CD71 pos subpopulations of EpoR-HM, EpoR-H, and wt-EpoR erythroblasts are graphed. Expanded cells also were shifted to differentiation medium, and frequencies of annexin-V and Ter119–copositive cells were analyzed. (C) Elevated DAPK-2 expression in EpoR-HM erythroblasts. Death-associated protein kinase-2 (DAPK-2) expression in wt-EpoR, EpoR-HM, and EpoR-H erythroblasts was assayed by Western blotting (and digital densitometry). Note the several fold increase in DAPK-2 levels in EpoR-HM erythroblasts (representative of 3 independent experiments). For Bcl-xl, plotted quantitation values are mean values plus or minus SE; n = 3 wt-EpoR, EpoR-HM, and EpoR-H mice per group, x = 2 experiments. For annexin-V staining, plotted values are mean values plus or minus SE; n = 3 wt-EpoR, EpoR-HM, and EpoR-H mice per group, x = 4 experiments.

    Article Snippet: Blocked membranes (0.05% Tween-20, 3% fat-free milk, 1% BSA, 0.15 M NaCl, 20 mM Tris, pH 7.4) were incubated with antibodies to Akt (no. sc-1618; SantaCruz Biotechnology, Santa Cruz, CA), p60Src (no. sc-8056; SantaCruz Biotechnology), p38 MAPK (no. 535; SantaCruz Biotechnology), Bax (no. AB2915; Chemicon, Temecula, CA), DAPK-2 (no. 3606; Chemicon), Bcl-x (no. 610211; BD Biosciences), and the following antibodies from Cell Signaling (Beverly, MA): Stat5 (no. 9352), PY-Stat5 (no. 9351), PS-Akt (no. 9271), PY-p60Src (no. 2101), PY/T-p38MAPK (no. 9211), ERK1,2 (no. 9102), PY/T-ERK1,2 (no. 4375), SAPK/JNK (no. 9252), PY/T-SAPK/JNK (no. 9251), PT/S p70S6-kinase (no. 9204), and p70S6-kinase (no. 9202).

    Techniques: Expressing, Western Blot, Marker, Quantitation Assay, Mouse Assay, Staining

    Genistein reduce the protein expression of Notch-1 and induce the expression of Bax/Bcl-2, Caspase-8. Western blot analysis were carried out to demonstrated the of expression of Notch-1, Bax, Bcl-2 and Caspase-8 in HT-29 cells treated by genistein (200 μmol/L) and TNF-α (10 ng/ml) respectively for 48 h. Density of the bands were quantified by a densitometry analysis. Data are presented after normalization by β-actin. The data shown are representative of three independent experiments. (* p

    Journal: BMC Cancer

    Article Title: Genistein induces apoptosis of colon cancer cells by reversal of epithelial-to-mesenchymal via a Notch1/NF-κB/slug/E-cadherin pathway

    doi: 10.1186/s12885-017-3829-9

    Figure Lengend Snippet: Genistein reduce the protein expression of Notch-1 and induce the expression of Bax/Bcl-2, Caspase-8. Western blot analysis were carried out to demonstrated the of expression of Notch-1, Bax, Bcl-2 and Caspase-8 in HT-29 cells treated by genistein (200 μmol/L) and TNF-α (10 ng/ml) respectively for 48 h. Density of the bands were quantified by a densitometry analysis. Data are presented after normalization by β-actin. The data shown are representative of three independent experiments. (* p

    Article Snippet: After blocking, specific antibodies such as Bax, caspase-3, caspase-8, Bcl-2, PI3K, Notch1, p-NF-κB, NF-κB, E-cadherin, N-cadherin and β-actin from AB clonal Biotechnology Co., Ltd. (Wuhan, China) were used to perform detection.

    Techniques: Expressing, Western Blot

    Pathways involved in apoptotic and EMT effect by genistein in HT-29 cells. Genistein reverse the EMT by promoting E-cadherin expression and inhibiting N-cadherin expression; combine with the regulations of EMT makers, Snail2/slug, ZEB1, and TWIST1. Genistein promotes Bax/Bcl-2 and caspase-8 activity by inhibiting notch-1. The notch-1 reduction leads to the inhibition of both p-NF-κB and NF-κB expression results in a reduction of EMT

    Journal: BMC Cancer

    Article Title: Genistein induces apoptosis of colon cancer cells by reversal of epithelial-to-mesenchymal via a Notch1/NF-κB/slug/E-cadherin pathway

    doi: 10.1186/s12885-017-3829-9

    Figure Lengend Snippet: Pathways involved in apoptotic and EMT effect by genistein in HT-29 cells. Genistein reverse the EMT by promoting E-cadherin expression and inhibiting N-cadherin expression; combine with the regulations of EMT makers, Snail2/slug, ZEB1, and TWIST1. Genistein promotes Bax/Bcl-2 and caspase-8 activity by inhibiting notch-1. The notch-1 reduction leads to the inhibition of both p-NF-κB and NF-κB expression results in a reduction of EMT

    Article Snippet: After blocking, specific antibodies such as Bax, caspase-3, caspase-8, Bcl-2, PI3K, Notch1, p-NF-κB, NF-κB, E-cadherin, N-cadherin and β-actin from AB clonal Biotechnology Co., Ltd. (Wuhan, China) were used to perform detection.

    Techniques: Expressing, Activity Assay, Inhibition

    HgCl 2 induced apoptosis is reduced in KO mice a) TUNEL nuclear staining in renal cortex, 24h after HgCl 2 treatment and b) quantitation which shows reduced TUNEL positive nuclei in KO group. c) Cleaved caspase 3 and activated Bax levels are lower by Western blot in KO kidney compared to WT (d e). **, P

    Journal: Kidney international

    Article Title: Specific deletion of glycogen synthase kinase-3? in the renal proximal tubule protects against acute nephrotoxic injury in mice

    doi: 10.1038/ki.2012.239

    Figure Lengend Snippet: HgCl 2 induced apoptosis is reduced in KO mice a) TUNEL nuclear staining in renal cortex, 24h after HgCl 2 treatment and b) quantitation which shows reduced TUNEL positive nuclei in KO group. c) Cleaved caspase 3 and activated Bax levels are lower by Western blot in KO kidney compared to WT (d e). **, P

    Article Snippet: Monoclonal antibody for GSK3β (BD-Transduction Laboratories, San Jose, CA) and polyclonal antibodies for pGSK3β, β-actin, cleaved caspase 3, Bax (Cell Signaling, Danvers, MA) and c-myc (Santa Cruz Biotechnology, CA) were used.

    Techniques: Mouse Assay, TUNEL Assay, Staining, Quantitation Assay, Western Blot

    rHMGB1 exerted no effect on protein expression of Bax and Bcl2 in neonatal rat cardiomyocytes. (A) Western blot analysis of cytosolic Bax (cyto-Bax) in the presence of rHMGB1. (B)Total cellular protein expression of Bax. (C) Total cellular protein expression of Bcl2. β-actin served as a loading control. Results are means ± SEM. Each experiment was repeated three times.

    Journal: PLoS ONE

    Article Title: HMGB1-RAGE Axis Makes No Contribution to Cardiac Remodeling Induced by Pressure-Overload

    doi: 10.1371/journal.pone.0158514

    Figure Lengend Snippet: rHMGB1 exerted no effect on protein expression of Bax and Bcl2 in neonatal rat cardiomyocytes. (A) Western blot analysis of cytosolic Bax (cyto-Bax) in the presence of rHMGB1. (B)Total cellular protein expression of Bax. (C) Total cellular protein expression of Bcl2. β-actin served as a loading control. Results are means ± SEM. Each experiment was repeated three times.

    Article Snippet: Immunoblotting was performed using antibodies against HMGB1 (Cell Signaling Technology), cytosolic Bax (cyto-Bax), total-Bax, Erk and phosphor-Erk (Cell Signaling Technology) and Bcl2 (Santa Cruz Biotechnology).

    Techniques: Expressing, Western Blot

    Release of cytochrome c from mitochondria was required for HMGA2-induced WI38 cell apoptosis ( A ) The decrease of Bcl-2 levels with a concomitant increase in Bax and cleaved caspase 9, as measured by immunoblotting in apoptotic WI38 cells induced by HMGA2 at indicated time point. ( B ) Immunofluorescence images showing the release of mitochondrial cytochrome c in HMGA2-expressing cells at day 5 (enlarged areas in frames). Scale bar: 50 μm. ( C ) Mitochondrial-cytosolic extracts were prepared from cells expressing GFP or HMGA2-GFP at day 5 and analysed for the cytochrome c by Western blotting, showing the release of cytochrome c from mitochondria in response to HMGA2 overexpression. VDAC as a mitochondrial marker and tubulin as a cytosolic marker were detected. ( D ) Verification of the silencing efficiency of shApaf1 by qPCR in WI38 cells. ( E ) Apaf1 deficient WI38 cells partially escape from HMGA2 induced cell death as calculated in relative survival percentage using MTT assay at day 8. ( F ) Attenuated levels of cleaved caspase 9 and -3 were detected in cells treated as in ( E ).

    Journal: Bioscience Reports

    Article Title: A novel anti-proliferative role of HMGA2 in induction of apoptosis through caspase 2 in primary human fibroblast cells

    doi: 10.1042/BSR20140112

    Figure Lengend Snippet: Release of cytochrome c from mitochondria was required for HMGA2-induced WI38 cell apoptosis ( A ) The decrease of Bcl-2 levels with a concomitant increase in Bax and cleaved caspase 9, as measured by immunoblotting in apoptotic WI38 cells induced by HMGA2 at indicated time point. ( B ) Immunofluorescence images showing the release of mitochondrial cytochrome c in HMGA2-expressing cells at day 5 (enlarged areas in frames). Scale bar: 50 μm. ( C ) Mitochondrial-cytosolic extracts were prepared from cells expressing GFP or HMGA2-GFP at day 5 and analysed for the cytochrome c by Western blotting, showing the release of cytochrome c from mitochondria in response to HMGA2 overexpression. VDAC as a mitochondrial marker and tubulin as a cytosolic marker were detected. ( D ) Verification of the silencing efficiency of shApaf1 by qPCR in WI38 cells. ( E ) Apaf1 deficient WI38 cells partially escape from HMGA2 induced cell death as calculated in relative survival percentage using MTT assay at day 8. ( F ) Attenuated levels of cleaved caspase 9 and -3 were detected in cells treated as in ( E ).

    Article Snippet: The primary antibodies used were: anti-pp53 (1:1,000, CST), anti-p53 (1:1000, CST), anti-p21 (1:500, Santa Cruz), anti-p16 (Santa Cruz, sc-468), anti-caspase 3 (1:1000, CST), anti-PARP [poly(ADP ribose) polymerase] 1 (1:3000, ECTOMICS), anti-HMGA2 (1:5000, ECTOMICS), anti-caspase 9 (1:1000, Bioworld), anti-Bax and anti-Bcl2 (1:1000, CST), anti-caspase 2 (1:1000, KeyGEN), anti-γH2A (1:2000, Millipore) and anti-β-actin (1:10 000, Sungene).

    Techniques: Immunofluorescence, Expressing, Western Blot, Over Expression, Marker, Real-time Polymerase Chain Reaction, MTT Assay

    Effects of glycyrrhizic acid on expression of Bax and caspase-3 were evaluated by western blotting. Total proteins were extracted from the livers of rats in the different treatment groups. GAPDH and tubulin were used to confirm the same sample loading in each lane. Data are shown as mean ± SD. a P

    Journal: World Journal of Gastroenterology : WJG

    Article Title: Glycyrrhizic acid inhibits apoptosis and fibrosis in carbon-tetrachloride-induced rat liver injury

    doi: 10.3748/wjg.v21.i17.5271

    Figure Lengend Snippet: Effects of glycyrrhizic acid on expression of Bax and caspase-3 were evaluated by western blotting. Total proteins were extracted from the livers of rats in the different treatment groups. GAPDH and tubulin were used to confirm the same sample loading in each lane. Data are shown as mean ± SD. a P

    Article Snippet: MMP2 and MMP9 antibodies were bought from Abcam (Cambridge, MA, United States), CTGF antibody was bought from Santa Cruz Biotechnology (Santa Cruz, CA, United States), caspase-3 and Bax antibodies were purchased from Cell Signaling Technology (Beverly, MA, United States).

    Techniques: Expressing, Western Blot

    Western blot results: ( A ). Expression Analysis of PP2B, Interleukin-6 and iNos (NOS2) upon treatment of Forskolin Compound. Treatments in HeLa (2 µM, 5 µM, and 10 µM) Cell lysates were subjected to Western blot analysis with PP2B, IL-6, and NOS2 antibody followed by sequential re probing against Actin. ( B ) Bar graph below indicates densitometric analysis of bands in immunoblot. ( C ) Expression Analysis of Caspase-3, Bcl2 and Bax upon treatment of Forskolin Compound HeLa and Forskolin-Treatments in HeLa (2 µM, 5 µM, and 10 µM) Cell lysates were subjected to Western blot analysis with Caspase-3, Bcl2 and Bax antibody followed by sequential re probing against Actin. ( D ) Densitometric analysis of the bands in Western blot, (**** denotes p

    Journal: Journal of Clinical Medicine

    Article Title: Natural Compound Modulates the Cervical Cancer Microenvironment—A Pharmacophore Guided Molecular Modelling Approaches

    doi: 10.3390/jcm7120551

    Figure Lengend Snippet: Western blot results: ( A ). Expression Analysis of PP2B, Interleukin-6 and iNos (NOS2) upon treatment of Forskolin Compound. Treatments in HeLa (2 µM, 5 µM, and 10 µM) Cell lysates were subjected to Western blot analysis with PP2B, IL-6, and NOS2 antibody followed by sequential re probing against Actin. ( B ) Bar graph below indicates densitometric analysis of bands in immunoblot. ( C ) Expression Analysis of Caspase-3, Bcl2 and Bax upon treatment of Forskolin Compound HeLa and Forskolin-Treatments in HeLa (2 µM, 5 µM, and 10 µM) Cell lysates were subjected to Western blot analysis with Caspase-3, Bcl2 and Bax antibody followed by sequential re probing against Actin. ( D ) Densitometric analysis of the bands in Western blot, (**** denotes p

    Article Snippet: The antibodies Bax, Bcl2, Caspase-3 were sourced from Cell Signalling Technologies, PP2B, IL-6 and NOS2 primary antibodies are purchased from Santa Cruz biotechnologies (Dallas, TX, USA).

    Techniques: Western Blot, Expressing

    Effects of human 3K3A-APC on activation of caspases-9 and -3, p53 levels and Bax and Bcl-2 expression and requirements for EPCR and PAR1 in hypoxic human BECs. (a) Western blots for p53 in nuclear extracts, and Bax and Bcl-2 in whole-cell extracts from

    Journal:

    Article Title: Neuroprotective activities of activated protein C mutant with reduced anticoagulant activity

    doi: 10.1111/j.1460-9568.2009.06664.x

    Figure Lengend Snippet: Effects of human 3K3A-APC on activation of caspases-9 and -3, p53 levels and Bax and Bcl-2 expression and requirements for EPCR and PAR1 in hypoxic human BECs. (a) Western blots for p53 in nuclear extracts, and Bax and Bcl-2 in whole-cell extracts from

    Article Snippet: For western blot analysis the following antibodies were used: polyclonal rabbit antibody against human p53 (1 : 1000, Cell Signaling, Beverly, MA, USA), human Bcl-2 (1 : 1000, Cell Signaling) and human Bax (1 : 1000, Cell Signaling), which cross-react with the corresponding mouse proteins.

    Techniques: Activation Assay, Expressing, Western Blot

    Effects of murine recombinant 3K3A-APC on activation of caspases-9 and -3, p53 levels and Bax and Bcl-2 expression in NMDA-treated mouse neurons. Caspase-9 (a) and caspase-3 (b) activities in neurons treated with NMDA in the absence or presence of caspase-9

    Journal:

    Article Title: Neuroprotective activities of activated protein C mutant with reduced anticoagulant activity

    doi: 10.1111/j.1460-9568.2009.06664.x

    Figure Lengend Snippet: Effects of murine recombinant 3K3A-APC on activation of caspases-9 and -3, p53 levels and Bax and Bcl-2 expression in NMDA-treated mouse neurons. Caspase-9 (a) and caspase-3 (b) activities in neurons treated with NMDA in the absence or presence of caspase-9

    Article Snippet: For western blot analysis the following antibodies were used: polyclonal rabbit antibody against human p53 (1 : 1000, Cell Signaling, Beverly, MA, USA), human Bcl-2 (1 : 1000, Cell Signaling) and human Bax (1 : 1000, Cell Signaling), which cross-react with the corresponding mouse proteins.

    Techniques: Recombinant, Activation Assay, Expressing

    Effect of total flavonoids from Flos Puerariae (TFF) on Bax and Bcl-2 expression in retinas of the diabetic mice. A : The photomicrographs were representatives the retina sections immunohistochemistry stained with Bax and Bcl-2 antibody. n=4 per group. (Magnification: 400×). Bax and Bcl-2 expression were localized in the cytosol of cells mainly in ganglion cell layer (GCL) and inner nuclear layer (INL). B : The photographs were representatives the western blot of Bax and Bcl-2 protein. Five western blots per group were experimented. C : Relative intensities of Bax protein (fold to β-actin). D : Relative intensities of Bcl-2 protein (fold to β-actin). E : Ratio of the relative intensities of Bcl-2 to Bax (Bcl-2 / Bax). Data are expressed as mean ±standard deviation. *p

    Journal: Molecular Vision

    Article Title: Protective effects of total flavonoids from Flos Puerariae on retinal neuronal damage in diabetic mice

    doi:

    Figure Lengend Snippet: Effect of total flavonoids from Flos Puerariae (TFF) on Bax and Bcl-2 expression in retinas of the diabetic mice. A : The photomicrographs were representatives the retina sections immunohistochemistry stained with Bax and Bcl-2 antibody. n=4 per group. (Magnification: 400×). Bax and Bcl-2 expression were localized in the cytosol of cells mainly in ganglion cell layer (GCL) and inner nuclear layer (INL). B : The photographs were representatives the western blot of Bax and Bcl-2 protein. Five western blots per group were experimented. C : Relative intensities of Bax protein (fold to β-actin). D : Relative intensities of Bcl-2 protein (fold to β-actin). E : Ratio of the relative intensities of Bcl-2 to Bax (Bcl-2 / Bax). Data are expressed as mean ±standard deviation. *p

    Article Snippet: The membranes were blocked in 5% skim milk for 2 h at room temperature before incubation with an antibody against Bax, Bcl-2 (Cell Signaling Technology, Boston, MA), or β-actin (Santa Cruz Biotechnology, Dallas, TX) overnight at 4 °C.

    Techniques: Expressing, Mouse Assay, Immunohistochemistry, Staining, Western Blot, Standard Deviation

    Bax activity is augmented after SBR and is regulated by p38 MAPK. A : Bax activity was measured in WT and p38-IKO (KO) mice by immunoprecipitating the active form of Bax with an isoform-specific antibody (6A7), followed by Western blotting for total Bax.

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: p38 MAPK regulates Bax activity and apoptosis in enterocytes at baseline and after intestinal resection

    doi: 10.1152/ajpgi.00485.2011

    Figure Lengend Snippet: Bax activity is augmented after SBR and is regulated by p38 MAPK. A : Bax activity was measured in WT and p38-IKO (KO) mice by immunoprecipitating the active form of Bax with an isoform-specific antibody (6A7), followed by Western blotting for total Bax.

    Article Snippet: anti-p38-α MAPK, anti-p38-γ MAPK, anti-total p38 MAPK, anti-total Bax, and anti-actin antibodies are from Cell Signalling (Danvers, MA); anti-cytochrome c and anti-Bax 6A7 antibodies are from BD Pharmingen (San Diego, CA).

    Techniques: Activity Assay, Mouse Assay, Western Blot

    Upper panel- Representative western blotting detection of p65, p53, securin, bax and β-actin in mouse bone marrow (BM), esophagus and stomach cells after exposure with RAN extract with or without lime. For BM, cells were collected after 60, 120 and 180 days, whereas for esophagus and stomach, cells were collected only after 180 days of exposure. β-actin was used as loading control. Lower panel- Quantitative densitometric analysis of the level of proteins of the above mentioned genes in bone marrow, esophagus and stomach cells after 180 days of exposure was shown. The values are the mean ± SD of three independent experiments. The values are normalized to respective β-actin values. * p

    Journal: BMC Cancer

    Article Title: Induction of chromosome instability and stomach cancer by altering the expression pattern of mitotic checkpoint genes in mice exposed to areca-nut

    doi: 10.1186/1471-2407-13-315

    Figure Lengend Snippet: Upper panel- Representative western blotting detection of p65, p53, securin, bax and β-actin in mouse bone marrow (BM), esophagus and stomach cells after exposure with RAN extract with or without lime. For BM, cells were collected after 60, 120 and 180 days, whereas for esophagus and stomach, cells were collected only after 180 days of exposure. β-actin was used as loading control. Lower panel- Quantitative densitometric analysis of the level of proteins of the above mentioned genes in bone marrow, esophagus and stomach cells after 180 days of exposure was shown. The values are the mean ± SD of three independent experiments. The values are normalized to respective β-actin values. * p

    Article Snippet: The membranes were probed with a 1:1000 dilution of a mouse monoclonal antibody against p53 (PAb 240; ab-26; Abcam, USA), Bax (6A7; ab5714; Abcam, USA), Securin (DCS-280; ab3305; Abcam, USA), β-actin (AC-15; ab6276; Abcam, USA) and rabbit polyclonal antibody against NF-κβ P65 (ab31481; bcam, USA).

    Techniques: Western Blot

    lncRNA F11‐AS1/miR‐211‐5p/NR1I3 axis regulates the proliferation, apoptosis, migration and invasion of HepG2.2.15 cells. A, The mRNA expression of Bax, Bcl‐2 and PCNA in HepG2.2.15 cells after transduction determined by RT‐qPCR. B, The protein expression of Bax, Bcl‐2 and PCNA in HepG2.2.15 cells after transduction measured by Western blot analysis. C, The proliferative ability of HepG2.2.15 cells after transduction assessed by CCK‐8 assay. D, the apoptosis rate of HepG2.2.15 cells after transduction evaluated by TUNEL staining. E, The migration ability of HepG2.2.15 cells after transduction assessed by scratch test (×40). F, The invasion ability of HepG2.2.15 cells after transduction determined by Transwell assay (×200). Data were measurement data and expressed by mean ± standard deviation. * P

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Long non‐coding RNA F11‐AS1 inhibits HBV‐related hepatocellular carcinoma progression by regulating NR1I3 via binding to microRNA‐211‐5p, et al. Long non‐coding RNA F11‐AS1 inhibits HBV‐related hepatocellular carcinoma progression by regulating NR1I3 via binding to microRNA‐211‐5p

    doi: 10.1111/jcmm.14881

    Figure Lengend Snippet: lncRNA F11‐AS1/miR‐211‐5p/NR1I3 axis regulates the proliferation, apoptosis, migration and invasion of HepG2.2.15 cells. A, The mRNA expression of Bax, Bcl‐2 and PCNA in HepG2.2.15 cells after transduction determined by RT‐qPCR. B, The protein expression of Bax, Bcl‐2 and PCNA in HepG2.2.15 cells after transduction measured by Western blot analysis. C, The proliferative ability of HepG2.2.15 cells after transduction assessed by CCK‐8 assay. D, the apoptosis rate of HepG2.2.15 cells after transduction evaluated by TUNEL staining. E, The migration ability of HepG2.2.15 cells after transduction assessed by scratch test (×40). F, The invasion ability of HepG2.2.15 cells after transduction determined by Transwell assay (×200). Data were measurement data and expressed by mean ± standard deviation. * P

    Article Snippet: Next, the membrane was probed with primary antibodies including mouse polyclonal antibodies to GAPDH (SAB1405848, 1 μg/mL) and NR1I3 (SAB1406904, 1 μg/mL), rabbit polyclonal antibodies to Bax (SAB4502546, 1:1000) and Bcl‐2 (SAB4500005, 1:1000) from Sigma‐Aldrich, and rabbit monoclonal antibody to proliferating cell nuclear antigen (PCNA; ab92552, 1:1000) from Abcam overnight at 4°C.

    Techniques: Migration, Expressing, Transduction, Quantitative RT-PCR, Western Blot, CCK-8 Assay, TUNEL Assay, Staining, Transwell Assay, Standard Deviation