ac-devd-afc peptide substrate Search Results


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  • 99
    Millipore fluorogenic substrates ac devd afc
    ODE activates apoptosis in CRC cells A panel of established CRC cell lines (HCT-116, Lovo, HT-29 and DLD-1) and three primary human CRC cell lines were treated with or without ODE at applied concentrations, cells were further cultured, cell apoptosis was analyzed by listed assay A - D , G and H . HCT-116 cells were pretreated with <t>Ac-DEVD-CHO</t> (“DVED”), Ac-LEHD-CHO (“LEHD”) or Ac-VAD-CHO (“VAD”) (40 μM each) for 1 h, following by ODE (50 μg/mL) treatment, cell viability E . and cell death F . were tested. “DMSO” stands for 0.1% DMSO. <t>Cleaved-PARP/cleaved-caspase-3</t> expression (vs. Tubulin) was quantified. Data in this figure were repeated four times, and similar results were obtained. * p
    Fluorogenic Substrates Ac Devd Afc, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    BioVision fluorogenic peptide substrate ac devd afc
    ODE activates apoptosis in CRC cells A panel of established CRC cell lines (HCT-116, Lovo, HT-29 and DLD-1) and three primary human CRC cell lines were treated with or without ODE at applied concentrations, cells were further cultured, cell apoptosis was analyzed by listed assay A - D , G and H . HCT-116 cells were pretreated with <t>Ac-DEVD-CHO</t> (“DVED”), Ac-LEHD-CHO (“LEHD”) or Ac-VAD-CHO (“VAD”) (40 μM each) for 1 h, following by ODE (50 μg/mL) treatment, cell viability E . and cell death F . were tested. “DMSO” stands for 0.1% DMSO. <t>Cleaved-PARP/cleaved-caspase-3</t> expression (vs. Tubulin) was quantified. Data in this figure were repeated four times, and similar results were obtained. * p
    Fluorogenic Peptide Substrate Ac Devd Afc, supplied by BioVision, used in various techniques. Bioz Stars score: 79/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biomol GmbH fluorescence peptide substrate ac devd afc
    ODE activates apoptosis in CRC cells A panel of established CRC cell lines (HCT-116, Lovo, HT-29 and DLD-1) and three primary human CRC cell lines were treated with or without ODE at applied concentrations, cells were further cultured, cell apoptosis was analyzed by listed assay A - D , G and H . HCT-116 cells were pretreated with <t>Ac-DEVD-CHO</t> (“DVED”), Ac-LEHD-CHO (“LEHD”) or Ac-VAD-CHO (“VAD”) (40 μM each) for 1 h, following by ODE (50 μg/mL) treatment, cell viability E . and cell death F . were tested. “DMSO” stands for 0.1% DMSO. <t>Cleaved-PARP/cleaved-caspase-3</t> expression (vs. Tubulin) was quantified. Data in this figure were repeated four times, and similar results were obtained. * p
    Fluorescence Peptide Substrate Ac Devd Afc, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 79/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biomol GmbH ac devd afc peptide substrate
    ODE activates apoptosis in CRC cells A panel of established CRC cell lines (HCT-116, Lovo, HT-29 and DLD-1) and three primary human CRC cell lines were treated with or without ODE at applied concentrations, cells were further cultured, cell apoptosis was analyzed by listed assay A - D , G and H . HCT-116 cells were pretreated with <t>Ac-DEVD-CHO</t> (“DVED”), Ac-LEHD-CHO (“LEHD”) or Ac-VAD-CHO (“VAD”) (40 μM each) for 1 h, following by ODE (50 μg/mL) treatment, cell viability E . and cell death F . were tested. “DMSO” stands for 0.1% DMSO. <t>Cleaved-PARP/cleaved-caspase-3</t> expression (vs. Tubulin) was quantified. Data in this figure were repeated four times, and similar results were obtained. * p
    Ac Devd Afc Peptide Substrate, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 79/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bachem ac devd afc peptide substrate
    zVADfmk inhibits amidinopiperidine-based compounds induced apoptosis. (A) The determination of Annexin V and 7-AAD positive Ramos cells treated with compounds 15 or 16 for 24 h. The data present the percentage of gated cells. (B) Caspase 3/7 activity was determined in cell lysates of Ramos cells treated for 4 h, 8 h, 16 h and 24 h with either 50 µM inhibitor or 10 µM TPCK, used as a positive control. Cleavage of <t>Ac-DEVD-AFC</t> in whole cell lysates was determined spectrofluorometrically. The results are presented as changes in fluorescence as a function of time. (C) Western blot analysis of the caspase-3 processing. Cells were treated for indicated time periods in the presence of zVADfmk (50 µM) and/or compound 16 (50 µM). (D) Analysis of Annexin V/7-AAD positive cells after 16 h treatment with compound 16 in the absence or presence of zVADfmk. NT, non-treated cells.
    Ac Devd Afc Peptide Substrate, supplied by Bachem, used in various techniques. Bioz Stars score: 87/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biomol GmbH fluorogenic peptide substrate acetyl devd afc
    zVADfmk inhibits amidinopiperidine-based compounds induced apoptosis. (A) The determination of Annexin V and 7-AAD positive Ramos cells treated with compounds 15 or 16 for 24 h. The data present the percentage of gated cells. (B) Caspase 3/7 activity was determined in cell lysates of Ramos cells treated for 4 h, 8 h, 16 h and 24 h with either 50 µM inhibitor or 10 µM TPCK, used as a positive control. Cleavage of <t>Ac-DEVD-AFC</t> in whole cell lysates was determined spectrofluorometrically. The results are presented as changes in fluorescence as a function of time. (C) Western blot analysis of the caspase-3 processing. Cells were treated for indicated time periods in the presence of zVADfmk (50 µM) and/or compound 16 (50 µM). (D) Analysis of Annexin V/7-AAD positive cells after 16 h treatment with compound 16 in the absence or presence of zVADfmk. NT, non-treated cells.
    Fluorogenic Peptide Substrate Acetyl Devd Afc, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 84/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore caspase 3 specific substrate ac devd afc
    (A) Addition reaction between <t>caspase-3</t> and monomer leading to activity loss. (B) Strategy to protect caspase-3 activity using a cysteinyl-2-pyridyl disulfide (CPD) protecting group (PG) prior to nanogel formulation.
    Caspase 3 Specific Substrate Ac Devd Afc, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 419 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    AnaSpec sensolyte homogeneous afc caspase 3 7 assay kit
    (A) Addition reaction between <t>caspase-3</t> and monomer leading to activity loss. (B) Strategy to protect caspase-3 activity using a cysteinyl-2-pyridyl disulfide (CPD) protecting group (PG) prior to nanogel formulation.
    Sensolyte Homogeneous Afc Caspase 3 7 Assay Kit, supplied by AnaSpec, used in various techniques. Bioz Stars score: 94/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore caspase substrates
    (A) Addition reaction between <t>caspase-3</t> and monomer leading to activity loss. (B) Strategy to protect caspase-3 activity using a cysteinyl-2-pyridyl disulfide (CPD) protecting group (PG) prior to nanogel formulation.
    Caspase Substrates, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    ODE activates apoptosis in CRC cells A panel of established CRC cell lines (HCT-116, Lovo, HT-29 and DLD-1) and three primary human CRC cell lines were treated with or without ODE at applied concentrations, cells were further cultured, cell apoptosis was analyzed by listed assay A - D , G and H . HCT-116 cells were pretreated with Ac-DEVD-CHO (“DVED”), Ac-LEHD-CHO (“LEHD”) or Ac-VAD-CHO (“VAD”) (40 μM each) for 1 h, following by ODE (50 μg/mL) treatment, cell viability E . and cell death F . were tested. “DMSO” stands for 0.1% DMSO. Cleaved-PARP/cleaved-caspase-3 expression (vs. Tubulin) was quantified. Data in this figure were repeated four times, and similar results were obtained. * p

    Journal: Oncotarget

    Article Title: Aqueous Oldenlandia diffusa extracts inhibits colorectal cancer cells via activating AMP-activated protein kinase signalings

    doi: 10.18632/oncotarget.9969

    Figure Lengend Snippet: ODE activates apoptosis in CRC cells A panel of established CRC cell lines (HCT-116, Lovo, HT-29 and DLD-1) and three primary human CRC cell lines were treated with or without ODE at applied concentrations, cells were further cultured, cell apoptosis was analyzed by listed assay A - D , G and H . HCT-116 cells were pretreated with Ac-DEVD-CHO (“DVED”), Ac-LEHD-CHO (“LEHD”) or Ac-VAD-CHO (“VAD”) (40 μM each) for 1 h, following by ODE (50 μg/mL) treatment, cell viability E . and cell death F . were tested. “DMSO” stands for 0.1% DMSO. Cleaved-PARP/cleaved-caspase-3 expression (vs. Tubulin) was quantified. Data in this figure were repeated four times, and similar results were obtained. * p

    Article Snippet: Assay of caspase-3 activity As described [ ], to test caspase-3 activity, 20 μg of cytosolic protein extracts per sample were mixed with the caspase assay buffer [ ] and the caspase-3 substrate Ac-DEVD-AFC (15 μg/mL) (Calbiochem).

    Techniques: Cell Culture, Expressing

    UV-induced degradation of p21 protein in AR-positive 104-R cells. (A) 104-R cells were treated with or without a synthetic androgen, R1881 (2 nM) for 2 h followed by UV irradiation (100 J/m 2 ). The p21 protein levels were analyzed by immunobloting with anti-p21 antibody. (B and C) 104-R cells were treated with or without proteasome inhibitor MG-132 (10 μM) for 2 h. The p21 protein levels were analyzed by immunoblotting (B), as described in (A). Caspase activity was measured using fluorogenic substrate Ac-DEVD-AFC (C). * p

    Journal: Biochemical and biophysical research communications

    Article Title: Androgen receptor primes prostate cancer cells to apoptosis through down-regulation of basal p21 expression

    doi: 10.1016/j.bbrc.2012.10.135

    Figure Lengend Snippet: UV-induced degradation of p21 protein in AR-positive 104-R cells. (A) 104-R cells were treated with or without a synthetic androgen, R1881 (2 nM) for 2 h followed by UV irradiation (100 J/m 2 ). The p21 protein levels were analyzed by immunobloting with anti-p21 antibody. (B and C) 104-R cells were treated with or without proteasome inhibitor MG-132 (10 μM) for 2 h. The p21 protein levels were analyzed by immunoblotting (B), as described in (A). Caspase activity was measured using fluorogenic substrate Ac-DEVD-AFC (C). * p

    Article Snippet: The fluorogenic caspase-3 substrate DEVD-AFC (carbobenzoxy-Asp-Glu-Val-Asp-7-amino-4- trifluoromethyl coumarin), protein synthesis inhibitor cycloheximide (CHX), and proteasomal inhibitor MG-132 were from Calbiochem (La Jolla, CA).

    Techniques: Irradiation, Western Blot, Activity Assay

    (A) Light-induced expression of Plk3. HeLa cells were transfected with the T 3 -caged EGFP-Plk3 plasmid followed by irradiation of the caged construct (365 nm, 5 min, 25 W) and incubated for 48 h. The cells were then fixed and stained with DAPI (nuclei) and rhodamine phalloidin (actin filaments) prior to imaging (63× magnification). White arrows indicate binucleated cells, and scale bars indicate 50 μm. (B) Light-induced activation of caspase-3. HeLa cells were transfected with the T mut negative control, T 0 -noncaged, and T 3 -caged EGFP-Plk3 plasmids. The cells were either irradiated (365 nm, 5 min, 25 W) or kept in the dark and lysed after 48 h. The lysate was assayed with a fluorogenic caspase-3 substrate (Calbiochem). Fluorescence units were normalized to the noncaged control, and standard deviations were calculated from three individual experiments. ns = not significant ( P > 0.05), *** = highly significant ( P

    Journal: Journal of the American Chemical Society

    Article Title: Site-Specific Promoter Caging Enables Optochemical Gene Activation in Cells and Animals

    doi: 10.1021/ja500327g

    Figure Lengend Snippet: (A) Light-induced expression of Plk3. HeLa cells were transfected with the T 3 -caged EGFP-Plk3 plasmid followed by irradiation of the caged construct (365 nm, 5 min, 25 W) and incubated for 48 h. The cells were then fixed and stained with DAPI (nuclei) and rhodamine phalloidin (actin filaments) prior to imaging (63× magnification). White arrows indicate binucleated cells, and scale bars indicate 50 μm. (B) Light-induced activation of caspase-3. HeLa cells were transfected with the T mut negative control, T 0 -noncaged, and T 3 -caged EGFP-Plk3 plasmids. The cells were either irradiated (365 nm, 5 min, 25 W) or kept in the dark and lysed after 48 h. The lysate was assayed with a fluorogenic caspase-3 substrate (Calbiochem). Fluorescence units were normalized to the noncaged control, and standard deviations were calculated from three individual experiments. ns = not significant ( P > 0.05), *** = highly significant ( P

    Article Snippet: HeLa cell protein extract (100 μg) was incubated with 50 μM Caspase-3 substrate (Ac-DEVD-AFC, Calbiochem) in activity buffer (50 mM HEPES, 150 mM NaCl, 50 mM MgCl2 , 250 μM EDTA, 10% sucrose, 0.1% CHAPS, pH 7.2) at 37 °C for 20 h. The fluorescence was measured on a BioTek Synergy 4 plate reader (400/505 nm).

    Techniques: Expressing, Transfection, Plasmid Preparation, Irradiation, Construct, Incubation, Staining, Imaging, Activation Assay, Negative Control, Fluorescence

    zVADfmk inhibits amidinopiperidine-based compounds induced apoptosis. (A) The determination of Annexin V and 7-AAD positive Ramos cells treated with compounds 15 or 16 for 24 h. The data present the percentage of gated cells. (B) Caspase 3/7 activity was determined in cell lysates of Ramos cells treated for 4 h, 8 h, 16 h and 24 h with either 50 µM inhibitor or 10 µM TPCK, used as a positive control. Cleavage of Ac-DEVD-AFC in whole cell lysates was determined spectrofluorometrically. The results are presented as changes in fluorescence as a function of time. (C) Western blot analysis of the caspase-3 processing. Cells were treated for indicated time periods in the presence of zVADfmk (50 µM) and/or compound 16 (50 µM). (D) Analysis of Annexin V/7-AAD positive cells after 16 h treatment with compound 16 in the absence or presence of zVADfmk. NT, non-treated cells.

    Journal: PLoS ONE

    Article Title: Selective Cytotoxicity of Amidinopiperidine Based Compounds Towards Burkitt's Lymphoma Cells Involves Proteasome Inhibition

    doi: 10.1371/journal.pone.0041961

    Figure Lengend Snippet: zVADfmk inhibits amidinopiperidine-based compounds induced apoptosis. (A) The determination of Annexin V and 7-AAD positive Ramos cells treated with compounds 15 or 16 for 24 h. The data present the percentage of gated cells. (B) Caspase 3/7 activity was determined in cell lysates of Ramos cells treated for 4 h, 8 h, 16 h and 24 h with either 50 µM inhibitor or 10 µM TPCK, used as a positive control. Cleavage of Ac-DEVD-AFC in whole cell lysates was determined spectrofluorometrically. The results are presented as changes in fluorescence as a function of time. (C) Western blot analysis of the caspase-3 processing. Cells were treated for indicated time periods in the presence of zVADfmk (50 µM) and/or compound 16 (50 µM). (D) Analysis of Annexin V/7-AAD positive cells after 16 h treatment with compound 16 in the absence or presence of zVADfmk. NT, non-treated cells.

    Article Snippet: Cell lysates (20 µg of protein) were incubated for 30 min at 37°C in caspase reaction buffer (20 mM PIPES, pH 7.2, 10% sucrose, 0.1% CHAPS, 1 mM EDTA, 100 mM NaCl), after which 100 µM Ac-DEVD-AFC peptide substrate (Bachem, Bubendorf, Switzerland) was added.

    Techniques: Activity Assay, Positive Control, Fluorescence, Western Blot

    (A) Addition reaction between caspase-3 and monomer leading to activity loss. (B) Strategy to protect caspase-3 activity using a cysteinyl-2-pyridyl disulfide (CPD) protecting group (PG) prior to nanogel formulation.

    Journal: Molecular pharmaceutics

    Article Title: Utilizing Inverse Emulsion Polymerization to Generate Responsive Nanogels for Cytosolic Protein Delivery

    doi: 10.1021/acs.molpharmaceut.7b00643

    Figure Lengend Snippet: (A) Addition reaction between caspase-3 and monomer leading to activity loss. (B) Strategy to protect caspase-3 activity using a cysteinyl-2-pyridyl disulfide (CPD) protecting group (PG) prior to nanogel formulation.

    Article Snippet: Although treatment of caspase-3 with the CPD protecting group can prevent acrylamide induced protein activity loss, there are also other factors that can affect protein activity in the IEP process.

    Techniques: Activity Assay

    Protein release from redox-responsive nanogels. (A) Coomassie-stained SDS-PAGE demonstrating caspase-3 release. (B) Western blot analysis demonstrating DTT- (100 mM) or GSH- (10 mM) mediated release. For quantification of the concentration of released caspase-3, a dilution series of human caspase-3 was detected using an anti-caspase-3 antibody that recognizes the large subunit. (C) Coomassie-stained SDS-PAGE demonstrating PAK2 release. For quantification 10 μL of the indicated concentration of purified PAK2 was included on the same gel.

    Journal: Molecular pharmaceutics

    Article Title: Utilizing Inverse Emulsion Polymerization to Generate Responsive Nanogels for Cytosolic Protein Delivery

    doi: 10.1021/acs.molpharmaceut.7b00643

    Figure Lengend Snippet: Protein release from redox-responsive nanogels. (A) Coomassie-stained SDS-PAGE demonstrating caspase-3 release. (B) Western blot analysis demonstrating DTT- (100 mM) or GSH- (10 mM) mediated release. For quantification of the concentration of released caspase-3, a dilution series of human caspase-3 was detected using an anti-caspase-3 antibody that recognizes the large subunit. (C) Coomassie-stained SDS-PAGE demonstrating PAK2 release. For quantification 10 μL of the indicated concentration of purified PAK2 was included on the same gel.

    Article Snippet: Although treatment of caspase-3 with the CPD protecting group can prevent acrylamide induced protein activity loss, there are also other factors that can affect protein activity in the IEP process.

    Techniques: Staining, SDS Page, Western Blot, Concentration Assay, Purification

    (A) Cell viability assay upon incubation of caspase-3 encapsulated nanogels (redox-responsive and redox-insensitive control nanogels) and free, un-encapsulated caspase-3. (B) Cellular viability of HeLa cells after incubation with nanogels at different concentrations. (C) Hemolysis assay of red blood cells in presence of nanogels at different concentrations. All error bars correspond to the percent error calculated from the standard deviation of duplicate wells.

    Journal: Molecular pharmaceutics

    Article Title: Utilizing Inverse Emulsion Polymerization to Generate Responsive Nanogels for Cytosolic Protein Delivery

    doi: 10.1021/acs.molpharmaceut.7b00643

    Figure Lengend Snippet: (A) Cell viability assay upon incubation of caspase-3 encapsulated nanogels (redox-responsive and redox-insensitive control nanogels) and free, un-encapsulated caspase-3. (B) Cellular viability of HeLa cells after incubation with nanogels at different concentrations. (C) Hemolysis assay of red blood cells in presence of nanogels at different concentrations. All error bars correspond to the percent error calculated from the standard deviation of duplicate wells.

    Article Snippet: Although treatment of caspase-3 with the CPD protecting group can prevent acrylamide induced protein activity loss, there are also other factors that can affect protein activity in the IEP process.

    Techniques: Viability Assay, Incubation, Hemolysis Assay, Standard Deviation

    Cartoon representation of caspase-3 encapsulated within a redox-responsive nanogel and its resulting disassembly in a reducing environment.

    Journal: Molecular pharmaceutics

    Article Title: Utilizing Inverse Emulsion Polymerization to Generate Responsive Nanogels for Cytosolic Protein Delivery

    doi: 10.1021/acs.molpharmaceut.7b00643

    Figure Lengend Snippet: Cartoon representation of caspase-3 encapsulated within a redox-responsive nanogel and its resulting disassembly in a reducing environment.

    Article Snippet: Although treatment of caspase-3 with the CPD protecting group can prevent acrylamide induced protein activity loss, there are also other factors that can affect protein activity in the IEP process.

    Techniques:

    Increased caspase-3 activity is indicative of increased myocellular apoptosis and may be a mechanism contributing to cardiac dilatation in male HCM mice consuming the soy diet. Caspase-3 activity is significantly attenuated in HCM males consuming the casein diet. n = 5–13 in each group. * P

    Journal: Journal of Clinical Investigation

    Article Title: Soy diet worsens heart disease in mice

    doi: 10.1172/JCI24676

    Figure Lengend Snippet: Increased caspase-3 activity is indicative of increased myocellular apoptosis and may be a mechanism contributing to cardiac dilatation in male HCM mice consuming the soy diet. Caspase-3 activity is significantly attenuated in HCM males consuming the casein diet. n = 5–13 in each group. * P

    Article Snippet: Caspase-3 activity was determined by monitoring the rate of cleavage of a fluorogenic caspase-3 specific substrate (Acetyl-AspGluValAsp-AMC; Calbiochem).

    Techniques: Activity Assay, Mouse Assay

    Spleen CD4+ T cells from WT or TIM-3Tg mice cultured with ConA (2μg/ml or 4μg/ml) −/+ rGal-9 (1μg/ml) were assessed at 24h for: (A) IFN-γ (ELISA); and (B) caspase 3/7 (FACS). n=6/group.

    Journal: Journal of hepatology

    Article Title: Recipient T-Cell TIM-3 and Hepatocyte Galectin-9 Signaling Protects Mouse Liver Transplants Against Ischemia-Reperfusion Injury

    doi: 10.1016/j.jhep.2014.10.034

    Figure Lengend Snippet: Spleen CD4+ T cells from WT or TIM-3Tg mice cultured with ConA (2μg/ml or 4μg/ml) −/+ rGal-9 (1μg/ml) were assessed at 24h for: (A) IFN-γ (ELISA); and (B) caspase 3/7 (FACS). n=6/group.

    Article Snippet: Liver tissue samples as well as spleen and hepatic CD4+ T cells (separated by magnetic cell sorting; StemCell Technologies) were assessed for caspase-3 activity (Calbiochem) according to the manufacturer’s instruction [ ].

    Techniques: Mouse Assay, Cell Culture, Enzyme-linked Immunosorbent Assay, FACS

    Butyrate and SAHA induced apoptosis, caspase-3 activation, and cytochrome c release in HeLa cells. HeLa cells were harvested after 2 days of treatment with indicated concentrations of butyrate or SAHA. ( A ) Cell death was measured by Hoechst dye 33342

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Apoptotic and autophagic cell death induced by histone deacetylase inhibitors

    doi: 10.1073/pnas.0408345102

    Figure Lengend Snippet: Butyrate and SAHA induced apoptosis, caspase-3 activation, and cytochrome c release in HeLa cells. HeLa cells were harvested after 2 days of treatment with indicated concentrations of butyrate or SAHA. ( A ) Cell death was measured by Hoechst dye 33342

    Article Snippet: N -benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD-FMK) and caspase-3 fluorogenic substrate were from Calbiochem.

    Techniques: Activation Assay

    Apaf-1 is required for butyrate and SAHA-induced caspase-3 activation but not cell death. Apaf-1 wild-type (WT, filled bars) and knockout (KO, open bars) MEFs were harvested after the treatment with butyrate ( A ) or SAHA ( B ) for 2 days or 3 days, and caspase-3

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Apoptotic and autophagic cell death induced by histone deacetylase inhibitors

    doi: 10.1073/pnas.0408345102

    Figure Lengend Snippet: Apaf-1 is required for butyrate and SAHA-induced caspase-3 activation but not cell death. Apaf-1 wild-type (WT, filled bars) and knockout (KO, open bars) MEFs were harvested after the treatment with butyrate ( A ) or SAHA ( B ) for 2 days or 3 days, and caspase-3

    Article Snippet: N -benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD-FMK) and caspase-3 fluorogenic substrate were from Calbiochem.

    Techniques: Activation Assay, Knock-Out

    Overexpression of Bcl-XL blocked butyrate- and SAHA-induced cytochrome c release and caspase-3 activation, but not cell death. HeLa cell lines stably transfected with Bcl-XL (HeLa-Bcl-XL) or vector alone (HeLa) were treated for 2 days with various concentrations

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Apoptotic and autophagic cell death induced by histone deacetylase inhibitors

    doi: 10.1073/pnas.0408345102

    Figure Lengend Snippet: Overexpression of Bcl-XL blocked butyrate- and SAHA-induced cytochrome c release and caspase-3 activation, but not cell death. HeLa cell lines stably transfected with Bcl-XL (HeLa-Bcl-XL) or vector alone (HeLa) were treated for 2 days with various concentrations

    Article Snippet: N -benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD-FMK) and caspase-3 fluorogenic substrate were from Calbiochem.

    Techniques: Over Expression, Activation Assay, Stable Transfection, Transfection, Plasmid Preparation

    Induction of apoptosis following depletion of SREBP in cancer cells is restricted to lipoprotein deplete conditions.  ( A ) RPE-myrAkt-ER cells were transfected with 25 nM siRNA oligonucleotides targeting SREBP1, SREBP2 or a combination of both. After 48 hours, cells were placed in medium containing 10% FCS or 1% LPDS for a further 48 hours in the presence of 100 nM 4-OHT or solvent (ethanol). Cell viability was determined by measuring caspase 3/7 activity (Apoptosis) normalized to total protein content (SRB). Graph shows mean ± SEM of three independent experiments. ( B ) The effect of SREBP depletion on cell viability in breast cancer cells. Cells were treated and analyzed as in A. Graphs show mean ± SEM of three independent experiments. Cell lines carry different mutations in components of the PI3-kinase pathway: MCF7 (PIK3CA E545K), T47D (PIK3CA L194F), HCC1954 (PIK3CA H1047R), BT549 (PTEN null ), MDA-MB-468 (PTEN null ), MDA-MB-231 (KRAS G13D) and SKBR3 (HER2 amplification). Information on cancer gene mutations was obtained from the Wellcome Trust Sanger Institute Cancer Genome Project ( http://www.sanger.ac.uk/genetics/CGP ). ( C ) Effect of depletion of SREBP1 or SREBP2 on viability of U87 glioblastoma cells. Graph shows mean ± SEM of three independent experiments. * P

    Journal: Cancer & Metabolism

    Article Title: Sterol regulatory element binding protein-dependent regulation of lipid synthesis supports cell survival and tumor growth

    doi: 10.1186/2049-3002-1-3

    Figure Lengend Snippet: Induction of apoptosis following depletion of SREBP in cancer cells is restricted to lipoprotein deplete conditions. ( A ) RPE-myrAkt-ER cells were transfected with 25 nM siRNA oligonucleotides targeting SREBP1, SREBP2 or a combination of both. After 48 hours, cells were placed in medium containing 10% FCS or 1% LPDS for a further 48 hours in the presence of 100 nM 4-OHT or solvent (ethanol). Cell viability was determined by measuring caspase 3/7 activity (Apoptosis) normalized to total protein content (SRB). Graph shows mean ± SEM of three independent experiments. ( B ) The effect of SREBP depletion on cell viability in breast cancer cells. Cells were treated and analyzed as in A. Graphs show mean ± SEM of three independent experiments. Cell lines carry different mutations in components of the PI3-kinase pathway: MCF7 (PIK3CA E545K), T47D (PIK3CA L194F), HCC1954 (PIK3CA H1047R), BT549 (PTEN null ), MDA-MB-468 (PTEN null ), MDA-MB-231 (KRAS G13D) and SKBR3 (HER2 amplification). Information on cancer gene mutations was obtained from the Wellcome Trust Sanger Institute Cancer Genome Project ( http://www.sanger.ac.uk/genetics/CGP ). ( C ) Effect of depletion of SREBP1 or SREBP2 on viability of U87 glioblastoma cells. Graph shows mean ± SEM of three independent experiments. * P

    Article Snippet: Thapsigargin and caspase 3/7 substrate were from Calbiochem.

    Techniques: Transfection, Activity Assay, Sulforhodamine B Assay, Multiple Displacement Amplification, Amplification

    miR-579-3p induces melanoma cells apoptosis and inhibit cell cycle progression. ( A ) The indicated cells were transfected with miR-579-3p or scrambled miR for 48 h and apoptosis induction was evaluated by FACS analysis. WM266 transfected as described above were subjected to Western blot analysis ( B ) and to FACS analysis to evaluate cell cycle progression and caspase 3/7 activation ( C  and  D ). ( E ) miR-579-3p was transfected in the same cells in presence or not of p21Si to evaluate cell cycle progression through FACS analysis. Error bars, ±SD,  P

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: miR-579-3p controls melanoma progression and resistance to target therapy

    doi: 10.1073/pnas.1607753113

    Figure Lengend Snippet: miR-579-3p induces melanoma cells apoptosis and inhibit cell cycle progression. ( A ) The indicated cells were transfected with miR-579-3p or scrambled miR for 48 h and apoptosis induction was evaluated by FACS analysis. WM266 transfected as described above were subjected to Western blot analysis ( B ) and to FACS analysis to evaluate cell cycle progression and caspase 3/7 activation ( C and D ). ( E ) miR-579-3p was transfected in the same cells in presence or not of p21Si to evaluate cell cycle progression through FACS analysis. Error bars, ±SD, P

    Article Snippet: Flow cytometric analysis to determine caspase 3/7 activity was performed according to the manufacturer’s instructions (Millipore).

    Techniques: Transfection, FACS, Western Blot, Activation Assay

    Lower levels of activated caspase 3 activity correlate with better discrimination learning. a ) Parallel relationship between cognitive scores (errors in reversal learning) and abundance of cells expressing activated caspase 3 in each animal  b ) Caspase 3 expression is directly correlated with errors in reversal learning. Pearson analysis r = 0.76, p

    Journal: PLoS ONE

    Article Title: Dietary and Behavioral Interventions Protect against Age Related Activation of Caspase Cascades in the Canine Brain

    doi: 10.1371/journal.pone.0024652

    Figure Lengend Snippet: Lower levels of activated caspase 3 activity correlate with better discrimination learning. a ) Parallel relationship between cognitive scores (errors in reversal learning) and abundance of cells expressing activated caspase 3 in each animal b ) Caspase 3 expression is directly correlated with errors in reversal learning. Pearson analysis r = 0.76, p

    Article Snippet: Specifically, wells were coated with 1 µl of active caspase-3 protease (Chemicon) and incubated with frontal cortex homogenates (1 µl, 4 ug/ul) from 4 aged beagles at 37°C for 1 hour.

    Techniques: Activity Assay, Expressing

    Double labeling with caspase 3 and neuronal or glial markers. a ) Double labeling of activated caspase 3 with the neuronal marker NeuN and b ) the glial marker GFAP revealed that the majority of cells positive for activated caspase-3 were also NeuN positive.

    Journal: PLoS ONE

    Article Title: Dietary and Behavioral Interventions Protect against Age Related Activation of Caspase Cascades in the Canine Brain

    doi: 10.1371/journal.pone.0024652

    Figure Lengend Snippet: Double labeling with caspase 3 and neuronal or glial markers. a ) Double labeling of activated caspase 3 with the neuronal marker NeuN and b ) the glial marker GFAP revealed that the majority of cells positive for activated caspase-3 were also NeuN positive.

    Article Snippet: Specifically, wells were coated with 1 µl of active caspase-3 protease (Chemicon) and incubated with frontal cortex homogenates (1 µl, 4 ug/ul) from 4 aged beagles at 37°C for 1 hour.

    Techniques: Labeling, Marker

    Activation of caspase 3 is associated with increased levels of caspase-3 cleavage products. a ) Fractin immunohistochemical staining in frontal cortices of aged dogs treated with AOX and/or ENR interventions showed significant reduction in expression of active caspase 3 in the E/A group *p

    Journal: PLoS ONE

    Article Title: Dietary and Behavioral Interventions Protect against Age Related Activation of Caspase Cascades in the Canine Brain

    doi: 10.1371/journal.pone.0024652

    Figure Lengend Snippet: Activation of caspase 3 is associated with increased levels of caspase-3 cleavage products. a ) Fractin immunohistochemical staining in frontal cortices of aged dogs treated with AOX and/or ENR interventions showed significant reduction in expression of active caspase 3 in the E/A group *p

    Article Snippet: Specifically, wells were coated with 1 µl of active caspase-3 protease (Chemicon) and incubated with frontal cortex homogenates (1 µl, 4 ug/ul) from 4 aged beagles at 37°C for 1 hour.

    Techniques: Activation Assay, Immunohistochemistry, Staining, Expressing

    Immunohistochemical staining for caspase 3 in aged canine brains. a ) Caspase 3 immunohistochemical staining in frontal cortices of aged dogs treated with AOX and/or ENR interventions showed significant reduction in expression of active caspase 3. **p

    Journal: PLoS ONE

    Article Title: Dietary and Behavioral Interventions Protect against Age Related Activation of Caspase Cascades in the Canine Brain

    doi: 10.1371/journal.pone.0024652

    Figure Lengend Snippet: Immunohistochemical staining for caspase 3 in aged canine brains. a ) Caspase 3 immunohistochemical staining in frontal cortices of aged dogs treated with AOX and/or ENR interventions showed significant reduction in expression of active caspase 3. **p

    Article Snippet: Specifically, wells were coated with 1 µl of active caspase-3 protease (Chemicon) and incubated with frontal cortex homogenates (1 µl, 4 ug/ul) from 4 aged beagles at 37°C for 1 hour.

    Techniques: Immunohistochemistry, Staining, Expressing

    Double-labeling detected by immunofluorescence revealed colocalization of fractin and active caspase 3 in several cells in the frontal cortex.

    Journal: PLoS ONE

    Article Title: Dietary and Behavioral Interventions Protect against Age Related Activation of Caspase Cascades in the Canine Brain

    doi: 10.1371/journal.pone.0024652

    Figure Lengend Snippet: Double-labeling detected by immunofluorescence revealed colocalization of fractin and active caspase 3 in several cells in the frontal cortex.

    Article Snippet: Specifically, wells were coated with 1 µl of active caspase-3 protease (Chemicon) and incubated with frontal cortex homogenates (1 µl, 4 ug/ul) from 4 aged beagles at 37°C for 1 hour.

    Techniques: Labeling, Immunofluorescence

    Deletion of amino acids 270 to 330 results in the activation of caspase-7 and -8, but not of caspase-9 in HeLa cells. (A) Quantification of caspase-3/7-like activity, expressed as luminescence unit (LMU) in 2 × 10 5 cells, using Caspase-Glo ® 3/7 Assay in Vero E6 cells after transfection with 0.8 µg plasmid DNA at 24 h in 24 well plates. *p

    Journal: Virology

    Article Title: Modulation of Apoptosis and Immune Signaling Pathways by the Hantaan Virus Nucleocapsid Protein

    doi: 10.1016/j.virol.2010.02.018

    Figure Lengend Snippet: Deletion of amino acids 270 to 330 results in the activation of caspase-7 and -8, but not of caspase-9 in HeLa cells. (A) Quantification of caspase-3/7-like activity, expressed as luminescence unit (LMU) in 2 × 10 5 cells, using Caspase-Glo ® 3/7 Assay in Vero E6 cells after transfection with 0.8 µg plasmid DNA at 24 h in 24 well plates. *p

    Article Snippet: Caspase-3/7, -8, and -9 substrates (Sigma, St. Louis, MO) were fluorogenic tetrapeptides; Ac-DEVD-AMC [acetyl-Asp-Glu-Val-Asp-7-(amido-4-methylcoumarin)], Ac-IETD-AMC [acetyl-Ile-Glu-Thr-Asp-7-(amido-4-methylcoumarin)], and Ac-LEHD [acetyl- Leu-Glu-His-Asp-7-(amido-4-trifluoromethylcoumarin)].

    Techniques: Activation Assay, Activity Assay, Caspase-Glo Assay, Transfection, Plasmid Preparation

    Analysis of HTNV N protein interaction with NF-κB, and the examination the cytoplasmic fraction from cells expressing HTNV N protein has on caspase activity. (A) HeLa cells were transfected with 75 µg of plasmid expressing myc-tagged HTNV N protein or empty vector. Immunoprecipitations (IP) were performed with anti-myc antibody bound to magnetic Dynabeads. Immunoprecipitations and whole cell extracts were analyzed by western blot for the levels of HTNV N protein, TRADD, TRAF-2, NF-κB (Rel-A), p-NF-κB (p-Rel-A), or IκB. (B) A modified protocol was used with a longer incubation time of 24 hrs to facilitate immune complex formation. (C) HeLa cells were transfected with 5 µg or 10 µg of plasmid DNA in 6-well plates or T-25 flasks, respectively. Whole cell extracts were made from cells lysed with caspase extract buffer in 6-well plates that were untreated or treated with 5 µM STR and the caspase-3/7 activity was measured. Caspase activity was also measured in the presence of caspase inhibitor (C i ) Z-D(OMe)E(OMe)VD(OMe)–FMK. The cytoplasmic fraction of cells expressing HTNV N protein or mock, untreated or treated with 20 ng/ml of TNF-α for 20 min was extracted and concentrated from cells in T-25 flasks. Caspase activity in cells treated with STR (6-well plates) was measured that were supplemented with 15 µl of cytoplasmic extracts from T-25 flasks. Each value is the mean of three different samples, and the vertical bars represent the standard deviation.

    Journal: Virology

    Article Title: Modulation of Apoptosis and Immune Signaling Pathways by the Hantaan Virus Nucleocapsid Protein

    doi: 10.1016/j.virol.2010.02.018

    Figure Lengend Snippet: Analysis of HTNV N protein interaction with NF-κB, and the examination the cytoplasmic fraction from cells expressing HTNV N protein has on caspase activity. (A) HeLa cells were transfected with 75 µg of plasmid expressing myc-tagged HTNV N protein or empty vector. Immunoprecipitations (IP) were performed with anti-myc antibody bound to magnetic Dynabeads. Immunoprecipitations and whole cell extracts were analyzed by western blot for the levels of HTNV N protein, TRADD, TRAF-2, NF-κB (Rel-A), p-NF-κB (p-Rel-A), or IκB. (B) A modified protocol was used with a longer incubation time of 24 hrs to facilitate immune complex formation. (C) HeLa cells were transfected with 5 µg or 10 µg of plasmid DNA in 6-well plates or T-25 flasks, respectively. Whole cell extracts were made from cells lysed with caspase extract buffer in 6-well plates that were untreated or treated with 5 µM STR and the caspase-3/7 activity was measured. Caspase activity was also measured in the presence of caspase inhibitor (C i ) Z-D(OMe)E(OMe)VD(OMe)–FMK. The cytoplasmic fraction of cells expressing HTNV N protein or mock, untreated or treated with 20 ng/ml of TNF-α for 20 min was extracted and concentrated from cells in T-25 flasks. Caspase activity in cells treated with STR (6-well plates) was measured that were supplemented with 15 µl of cytoplasmic extracts from T-25 flasks. Each value is the mean of three different samples, and the vertical bars represent the standard deviation.

    Article Snippet: Caspase-3/7, -8, and -9 substrates (Sigma, St. Louis, MO) were fluorogenic tetrapeptides; Ac-DEVD-AMC [acetyl-Asp-Glu-Val-Asp-7-(amido-4-methylcoumarin)], Ac-IETD-AMC [acetyl-Ile-Glu-Thr-Asp-7-(amido-4-methylcoumarin)], and Ac-LEHD [acetyl- Leu-Glu-His-Asp-7-(amido-4-trifluoromethylcoumarin)].

    Techniques: Expressing, Activity Assay, Transfection, Plasmid Preparation, Western Blot, Modification, Incubation, Standard Deviation