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  • 95
    Millipore α 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
    α Bax, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α bax/product/Millipore
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    92
    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: 92/100, based on 762 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bax/product/Millipore
    Average 92 stars, based on 762 article reviews
    Price from $9.99 to $1999.99
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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 175 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bax/product/ABclonal
    Average 95 stars, based on 175 article reviews
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    99
    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: 99/100, based on 10008 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bax/product/Cell Signaling Technology Inc
    Average 99 stars, based on 10008 article reviews
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    bax - by Bioz Stars, 2020-05
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    bax  (Abcam)
    95
    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: 95/100, based on 3796 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bax/product/Abcam
    Average 95 stars, based on 3796 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 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/total bax/product/Cell Signaling Technology Inc
    Average 99 stars, based on 28 article reviews
    Price from $9.99 to $1999.99
    total bax - by Bioz Stars, 2020-05
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    91
    BioLegend 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.
    Bax, supplied by BioLegend, used in various techniques. Bioz Stars score: 91/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bax/product/BioLegend
    Average 91 stars, based on 27 article reviews
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    88
    Novoprotein bax a
    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.
    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
    Average 88 stars, based on 7 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

    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

    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

    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

    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

    Protein expression of Bax, BCL2, cleaved caspase-8, cleaved caspase-9, cleaved PARP, NF-κB p65 in A375 cell line is detected by western blot analysis. β-actin was used as an internal control. Significance levels between distinct groups were determined using one-way analysis of variance. **P≤0.01 vs. the control. PARP, poly (ADP-ribose) polymerase; BCL2, B-cell lymphoma-2.

    Journal: Oncology Letters

    Article Title: Cardamonin as a potential treatment for melanoma induces human melanoma cell apoptosis

    doi: 10.3892/ol.2019.11242

    Figure Lengend Snippet: Protein expression of Bax, BCL2, cleaved caspase-8, cleaved caspase-9, cleaved PARP, NF-κB p65 in A375 cell line is detected by western blot analysis. β-actin was used as an internal control. Significance levels between distinct groups were determined using one-way analysis of variance. **P≤0.01 vs. the control. PARP, poly (ADP-ribose) polymerase; BCL2, B-cell lymphoma-2.

    Article Snippet: The membranes were then blocked in 5% non-fat milk in TBST (0.05%Tween20) for 1 h at room temperature and incubated with homologous primary antibodies (all 1:1,000) overnight at 4°C [β-actin, cat. no. AC026; P65, cat. no. A2547; BCL2, cat. no. A2212; BAX, cat. no. A7626 (all ABclonal Biotech Co., Ltd.); Cleaved Caspase-8, cat. no. 9496; Cleaved Caspase-9, cat. no. 20750; Cleaved PARP, cat. no. 5625 (all Cell Signaling Technology, Inc.)].

    Techniques: Expressing, Western Blot

    Protein expression of Bax, BCL2, cleaved caspase-8, cleaved caspase-9, cleaved PARP, nuclear factor-κB p65 in M14 cell line detected by western blot analysis. β-actin was used as an internal control. The levels of different proteins were quantified and normalized to β-actin and are shown in a histogram. Significance levels between distinct groups were determined using one-way analysis of variance. **P≤0.01 vs. the control. PARP, poly (ADP-ribose) polymerase; BCL2, B-cell lymphoma-2.

    Journal: Oncology Letters

    Article Title: Cardamonin as a potential treatment for melanoma induces human melanoma cell apoptosis

    doi: 10.3892/ol.2019.11242

    Figure Lengend Snippet: Protein expression of Bax, BCL2, cleaved caspase-8, cleaved caspase-9, cleaved PARP, nuclear factor-κB p65 in M14 cell line detected by western blot analysis. β-actin was used as an internal control. The levels of different proteins were quantified and normalized to β-actin and are shown in a histogram. Significance levels between distinct groups were determined using one-way analysis of variance. **P≤0.01 vs. the control. PARP, poly (ADP-ribose) polymerase; BCL2, B-cell lymphoma-2.

    Article Snippet: The membranes were then blocked in 5% non-fat milk in TBST (0.05%Tween20) for 1 h at room temperature and incubated with homologous primary antibodies (all 1:1,000) overnight at 4°C [β-actin, cat. no. AC026; P65, cat. no. A2547; BCL2, cat. no. A2212; BAX, cat. no. A7626 (all ABclonal Biotech Co., Ltd.); Cleaved Caspase-8, cat. no. 9496; Cleaved Caspase-9, cat. no. 20750; Cleaved PARP, cat. no. 5625 (all Cell Signaling Technology, Inc.)].

    Techniques: Expressing, Western Blot

    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

    OXA treatment reduces protein synthesis and concentration within TA muscle. (A) OXA treatment showed a trend to reduce total protein concentration, and reduced (B) total p70S6K and (C) total rpS6 when compared to VEH suggesting a suppression of protein synthesis. (D) Apoptosis initiation marker total Bax was also supressed in TA muscle. Contrastingly no change in (E) total ubiquitin-proteasome marker MuRF1 or (F) autophagy marker p62 expression was noted. (G) Western blot representative images are digitally cut together to remove blots of other chemotherapies not presented in this manuscript, no other alteration was performed. Significance: * p

    Journal: Frontiers in Pharmacology

    Article Title: BGP-15 Protects against Oxaliplatin-Induced Skeletal Myopathy and Mitochondrial Reactive Oxygen Species Production in Mice

    doi: 10.3389/fphar.2017.00137

    Figure Lengend Snippet: OXA treatment reduces protein synthesis and concentration within TA muscle. (A) OXA treatment showed a trend to reduce total protein concentration, and reduced (B) total p70S6K and (C) total rpS6 when compared to VEH suggesting a suppression of protein synthesis. (D) Apoptosis initiation marker total Bax was also supressed in TA muscle. Contrastingly no change in (E) total ubiquitin-proteasome marker MuRF1 or (F) autophagy marker p62 expression was noted. (G) Western blot representative images are digitally cut together to remove blots of other chemotherapies not presented in this manuscript, no other alteration was performed. Significance: * p

    Article Snippet: Probes used: Bax total (CST #2772), MuRF1 total (ECM #MP3401), PAR total (Enzo #ALX-804-220), PARP-1 total (Santa Cruz SC-8007), PARP-2 total (Santa Cruz SC-393310), p70S6K total (CST #2708), rp-S6 total (C ST #2217), SQSTM1/p62 total (CST #5114).

    Techniques: Concentration Assay, Protein Concentration, Marker, Expressing, 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

    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

    H460 cells were incubated with various concentrations of SFP for 48 h. Bax and Bcl-2 protein expression levels were detected via western blotting using β-actin as internal control. ** P

    Journal: Acta Pharmacologica Sinica

    Article Title: Silk fibroin peptide suppresses proliferation and induces apoptosis and cell cycle arrest in human lung cancer cells

    doi: 10.1038/s41401-018-0048-0

    Figure Lengend Snippet: H460 cells were incubated with various concentrations of SFP for 48 h. Bax and Bcl-2 protein expression levels were detected via western blotting using β-actin as internal control. ** P

    Article Snippet: The primary antibodies were as follows: anti-Bcl-2 (1:1000 dilution, rabbit monoclonal antibody, Cell Signaling Technology, Beverly, USA), anti-β-actin (1:1000 dilution, mouse monoclonal antibody, Cell Signaling Technology, Beverly, USA), and anti-Bax (1:1000 dilution, rabbit monoclonal antibody, Cell Signaling Technology, Beverly, USA).

    Techniques: Incubation, Expressing, Western Blot

    Loss of PKR stabilizes Bcl-2/Bax binding and inhibits Bax insertion to OMM . ( a ) REH or ( b ) K562 cells were exposed to H 2 O 2 for 6 h, lysed and co-immunoprecipitation of Bcl-2 and Bax performed. ( c ) REH cells were treated with H 2 O 2 for 6 h. Mitochondria were isolated and treated with alkaline buffer. Mitochondrial debris was then collected by ultracentrifugation and subject to western blot for evaluating BAX level. ( d ) K562 cells were treated with H 2 O 2 for 6 h. Bax insertion was evaluated as described previously. Total cellular levels of Bax and Bcl-2 after 6-h exposure to H 2 O 2 were evaluated by western blot.

    Journal: Blood Cancer Journal

    Article Title: PKR negatively regulates leukemia progression in association with PP2A activation, Bcl-2 inhibition and increased apoptosis

    doi: 10.1038/bcj.2013.42

    Figure Lengend Snippet: Loss of PKR stabilizes Bcl-2/Bax binding and inhibits Bax insertion to OMM . ( a ) REH or ( b ) K562 cells were exposed to H 2 O 2 for 6 h, lysed and co-immunoprecipitation of Bcl-2 and Bax performed. ( c ) REH cells were treated with H 2 O 2 for 6 h. Mitochondria were isolated and treated with alkaline buffer. Mitochondrial debris was then collected by ultracentrifugation and subject to western blot for evaluating BAX level. ( d ) K562 cells were treated with H 2 O 2 for 6 h. Bax insertion was evaluated as described previously. Total cellular levels of Bax and Bcl-2 after 6-h exposure to H 2 O 2 were evaluated by western blot.

    Article Snippet: Phospho-serine 51-specific eIF2α, eIF2α, phosphor-serine 70-specific Bcl-2, BAX antibodies were from Cell Signaling Technology (Beverly, MA, USA).

    Techniques: Binding Assay, Immunoprecipitation, Isolation, Western Blot

    Effect of HCS on the levels of apoptosis-related molecules in T24 and EJ cell lines. The active (cleaved) forms of Caspase 3,8,9 and cleaved PARP were increased in a dose-dependent manner in HCS-treated T24 and EJ cells. the expression level of Bax was also elevated,whereas, the anti-apoptosis proteins such as Bcl-2 and XIAP were down regulated after HCS treatment.

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Huachansu suppresses human bladder cancer cell growth through the Fas/Fasl and TNF- alpha/TNFR1 pathway in vitro and in vivo

    doi: 10.1186/s13046-015-0134-9

    Figure Lengend Snippet: Effect of HCS on the levels of apoptosis-related molecules in T24 and EJ cell lines. The active (cleaved) forms of Caspase 3,8,9 and cleaved PARP were increased in a dose-dependent manner in HCS-treated T24 and EJ cells. the expression level of Bax was also elevated,whereas, the anti-apoptosis proteins such as Bcl-2 and XIAP were down regulated after HCS treatment.

    Article Snippet: Blots were probed with the following antibodies Bax, Bcl-2, XIAP, cleaved Caspase-3,-8,-9, cleaved PARP, p65, p-p65, iκB-α (Cell Signaling Technology, USA), Fas, Fasl, (epitomics,USA) and TNFR1 (Proteintech group,USA ) overnight at 4°C.

    Techniques: 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