cleaved caspase 3 rabbit 9664s ab 10831820 cst  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc cleaved caspase 3 rabbit 9664s ab 10831820 cst
    Cleaved Caspase 3 Rabbit 9664s Ab 10831820 Cst, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cleaved caspase 3 rabbit 9664s ab 10831820 cst/product/Cell Signaling Technology Inc
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    rabbit anti human cleaved caspase 3 asp175 5a1e  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti human cleaved caspase 3 asp175 5a1e
    Western blot analysis was employed to assess the expression levels of (A) BAX, Bcl-2, and cleaved <t>caspase-3</t> in LNCaP cells after exposure to the different concentrations of EADR. The graph represents the relative intensity of (B) BAX, Bcl-2, and cleaved caspase-3 proteins in relation to EADR concentration. The data are presented as mean ± SD of results obtained from three independent experiments. Statistical significance was assigned to p -values less than 0.05 (*), indicating a significant difference compared to the control group.
    Rabbit Anti Human Cleaved Caspase 3 Asp175 5a1e, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti human cleaved caspase 3 asp175 5a1e/product/Cell Signaling Technology Inc
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    Images

    1) Product Images from "Diospyros rhodocalyx Kurz induces mitochondrial-mediated apoptosis via BAX, Bcl-2, and caspase-3 pathways in LNCaP human prostate cancer cell line"

    Article Title: Diospyros rhodocalyx Kurz induces mitochondrial-mediated apoptosis via BAX, Bcl-2, and caspase-3 pathways in LNCaP human prostate cancer cell line

    Journal: PeerJ

    doi: 10.7717/peerj.17637

    Western blot analysis was employed to assess the expression levels of (A) BAX, Bcl-2, and cleaved caspase-3 in LNCaP cells after exposure to the different concentrations of EADR. The graph represents the relative intensity of (B) BAX, Bcl-2, and cleaved caspase-3 proteins in relation to EADR concentration. The data are presented as mean ± SD of results obtained from three independent experiments. Statistical significance was assigned to p -values less than 0.05 (*), indicating a significant difference compared to the control group.
    Figure Legend Snippet: Western blot analysis was employed to assess the expression levels of (A) BAX, Bcl-2, and cleaved caspase-3 in LNCaP cells after exposure to the different concentrations of EADR. The graph represents the relative intensity of (B) BAX, Bcl-2, and cleaved caspase-3 proteins in relation to EADR concentration. The data are presented as mean ± SD of results obtained from three independent experiments. Statistical significance was assigned to p -values less than 0.05 (*), indicating a significant difference compared to the control group.

    Techniques Used: Western Blot, Expressing, Concentration Assay, Control

    alexa fluor 647 cleaved caspase 3 rabbit mab asp175  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc alexa fluor 647 cleaved caspase 3 rabbit mab asp175
    Alexa Fluor 647 Cleaved Caspase 3 Rabbit Mab Asp175, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alexa fluor 647 cleaved caspase 3 rabbit mab asp175/product/Cell Signaling Technology Inc
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    alexa fluor 647 cleaved caspase 3 rabbit mab asp175 - by Bioz Stars, 2024-07
    86/100 stars

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    rabbit anti cleaved active caspase 3 monoclonal antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti cleaved active caspase 3 monoclonal antibody
    Deficiency of DNAJC6 activates mitochondria-mediated pro-apoptotic pathway in dopaminergic neurons. ( A ) Cytochrome c was predominantly located within mitochondrial fractions of control and SC shRNA-transfected dopaminergic neurons. Three-day transfection of shRNAs targeting DNAJC6 significantly decreased mitochondrial cytochrome c and elevated cytosolic cytochrome c in dopaminergic neurons. Transfecting dopaminergic neurons with shRNAs of DNAJC6 significantly upregulated cytosolic active caspase-9 and <t>active</t> <t>caspase-3.</t> ( B ) DNAJC6 paucity induced by 4-day transfection of shRNAs targeting DNAJC6 significantly upregulated the percentage of TUNEL-positive apoptotic dopaminergic neurons. Each bar represents the mean ± S.E. value of 6 experiments. *** p < 0.001 compared with control dopaminergic neurons.
    Rabbit Anti Cleaved Active Caspase 3 Monoclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti cleaved active caspase 3 monoclonal antibody/product/Cell Signaling Technology Inc
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    rabbit anti cleaved active caspase 3 monoclonal antibody - by Bioz Stars, 2024-07
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    1) Product Images from "Downregulation of Protease Cathepsin D and Upregulation of Pathologic α-Synuclein Mediate Paucity of DNAJC6-Induced Degeneration of Dopaminergic Neurons"

    Article Title: Downregulation of Protease Cathepsin D and Upregulation of Pathologic α-Synuclein Mediate Paucity of DNAJC6-Induced Degeneration of Dopaminergic Neurons

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms25126711

    Deficiency of DNAJC6 activates mitochondria-mediated pro-apoptotic pathway in dopaminergic neurons. ( A ) Cytochrome c was predominantly located within mitochondrial fractions of control and SC shRNA-transfected dopaminergic neurons. Three-day transfection of shRNAs targeting DNAJC6 significantly decreased mitochondrial cytochrome c and elevated cytosolic cytochrome c in dopaminergic neurons. Transfecting dopaminergic neurons with shRNAs of DNAJC6 significantly upregulated cytosolic active caspase-9 and active caspase-3. ( B ) DNAJC6 paucity induced by 4-day transfection of shRNAs targeting DNAJC6 significantly upregulated the percentage of TUNEL-positive apoptotic dopaminergic neurons. Each bar represents the mean ± S.E. value of 6 experiments. *** p < 0.001 compared with control dopaminergic neurons.
    Figure Legend Snippet: Deficiency of DNAJC6 activates mitochondria-mediated pro-apoptotic pathway in dopaminergic neurons. ( A ) Cytochrome c was predominantly located within mitochondrial fractions of control and SC shRNA-transfected dopaminergic neurons. Three-day transfection of shRNAs targeting DNAJC6 significantly decreased mitochondrial cytochrome c and elevated cytosolic cytochrome c in dopaminergic neurons. Transfecting dopaminergic neurons with shRNAs of DNAJC6 significantly upregulated cytosolic active caspase-9 and active caspase-3. ( B ) DNAJC6 paucity induced by 4-day transfection of shRNAs targeting DNAJC6 significantly upregulated the percentage of TUNEL-positive apoptotic dopaminergic neurons. Each bar represents the mean ± S.E. value of 6 experiments. *** p < 0.001 compared with control dopaminergic neurons.

    Techniques Used: Control, shRNA, Transfection, TUNEL Assay

    PARK19 DNAJC6 mutants fail to inhibit tunicamycin- or rotenone-evoked neurotoxicity, α-synuclein upregulation and apoptotic signaling in dopaminergic neurons. ( A ) FLAG-tagged human WT, Q789X or R927G DNAJC6 was transiently expressed in SH-SY5Y dopaminergic neurons. ( B ) Three-day incubation of 1 μM tunicamycin (TCM) or 0.5 μM rotenone (RTN) induced the neurodegeneration of dopaminergic cells. WT DNAJC6 significantly inhibited tunicamycin- or rotenone-evoked degeneration of dopaminergic neurons. On the contrary, PARK19 DNAJC6 mutants (Q789X or R927G) failed to prevent tunicamycin- or rotenone-triggered neurodegeneration. Each bar shows the mean ± S.E. value of 7 experiments. ( C ) Tunicamycin (TCM; 1 μM) upregulated the cytosolic expressions of active caspase-12, PERK, CHOP, IRE1α, Grp78 and α-synuclein. WT DNAJC6 significantly prevented the tunicamycin-evoked upregulation of cytosolic active caspase-12, PERK, CHOP, IRE1α, Grp78 and α-synuclein. PARK19 DNAJC6 mutants (Q789X or R927G) did not affect the upregulation of cytosolic active caspase-12, PERK, CHOP, IRE1α, Grp78 or α-synuclein caused by tunicamycin. ( D ) Rotenone (RTN; 0.5 μM) upregulated the cytosolic levels of α-synuclein, active caspase-3, active caspase-9 and cytochrome c. WT DNAJC6 inhibited the rotenone-evoked upregulation of cytosolic α-synuclein, active caspase-3, active caspase-9 and cytochrome c. PARK19 DNAJC6 mutants (Q789X or R927G) failed to reverse the upregulation of cytosolic α-synuclein, active caspase-3, active caspase-9 and cytochrome c caused by rotenone. Each bar represents the mean ± S.E. value of 6 experiments. ** p < 0.01 or *** p < 0.001 compared with control dopaminergic neurons. # p < 0.01 compared with tunicamycin- or rotenone-treated dopaminergic neurons.
    Figure Legend Snippet: PARK19 DNAJC6 mutants fail to inhibit tunicamycin- or rotenone-evoked neurotoxicity, α-synuclein upregulation and apoptotic signaling in dopaminergic neurons. ( A ) FLAG-tagged human WT, Q789X or R927G DNAJC6 was transiently expressed in SH-SY5Y dopaminergic neurons. ( B ) Three-day incubation of 1 μM tunicamycin (TCM) or 0.5 μM rotenone (RTN) induced the neurodegeneration of dopaminergic cells. WT DNAJC6 significantly inhibited tunicamycin- or rotenone-evoked degeneration of dopaminergic neurons. On the contrary, PARK19 DNAJC6 mutants (Q789X or R927G) failed to prevent tunicamycin- or rotenone-triggered neurodegeneration. Each bar shows the mean ± S.E. value of 7 experiments. ( C ) Tunicamycin (TCM; 1 μM) upregulated the cytosolic expressions of active caspase-12, PERK, CHOP, IRE1α, Grp78 and α-synuclein. WT DNAJC6 significantly prevented the tunicamycin-evoked upregulation of cytosolic active caspase-12, PERK, CHOP, IRE1α, Grp78 and α-synuclein. PARK19 DNAJC6 mutants (Q789X or R927G) did not affect the upregulation of cytosolic active caspase-12, PERK, CHOP, IRE1α, Grp78 or α-synuclein caused by tunicamycin. ( D ) Rotenone (RTN; 0.5 μM) upregulated the cytosolic levels of α-synuclein, active caspase-3, active caspase-9 and cytochrome c. WT DNAJC6 inhibited the rotenone-evoked upregulation of cytosolic α-synuclein, active caspase-3, active caspase-9 and cytochrome c. PARK19 DNAJC6 mutants (Q789X or R927G) failed to reverse the upregulation of cytosolic α-synuclein, active caspase-3, active caspase-9 and cytochrome c caused by rotenone. Each bar represents the mean ± S.E. value of 6 experiments. ** p < 0.01 or *** p < 0.001 compared with control dopaminergic neurons. # p < 0.01 compared with tunicamycin- or rotenone-treated dopaminergic neurons.

    Techniques Used: Incubation, Control

    anti rabbit cleaved caspase 3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti rabbit cleaved caspase 3
    Anti Rabbit Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti rabbit cleaved caspase 3/product/Cell Signaling Technology Inc
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    rabbit cleaved caspase 3 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit cleaved caspase 3 antibody
    Rabbit Cleaved Caspase 3 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit cleaved caspase 3 antibody/product/Cell Signaling Technology Inc
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    anti rabbit cleaved caspase 3  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti rabbit cleaved caspase 3
    ERp57 protects against mutant TDP-43 induced cell death in neuronal cell lines A Neuro-2a cells were co-expressed with wild-type TDP-43 (TDP-WT) or TDP-43 M337V (M337V, green) and V5 tagged ERp57 (red), examined by confocal microscopy at 72 h post transfection. Nuclei are shown by Hoechst stain (blue). Arrow represents condensed or fragmented nuclei, indicating apoptosis is underway. Few cells expressing TDP-WT (panel 1) or TDP-WT co-expressing ERp57 (panel 2) contained fragmented nuclei and hence were apoptotic (< 1%) but more cells expressing TDP-43 M337V (panel 3) displayed Hoechst-stained condensed nuclei, indicating apoptosis, indicated by white arrows (middle panel). However, fewer cells co-expressing TDP-43 M337V with ERp57 (panel 3) were undergoing apoptosis compared to those transfected with empty vector, scale bar = 5 µm. B Quantification of apoptotic nuclei in cells in 5A expressing TDP-43 and ERp57. Results are expressed as mean ± SD, n = 3. A significant difference in apoptosis was observed between wild-type TDP-43 and TDP-43 M337V cells (****p < 0.0001). Over-expression of ERp57 with TDP-43 M337V resulted in significantly fewer cells undergoing apoptosis compared to cells transfected with empty vector only (***p < 0.001). C <t>Activated</t> <t>caspase-3</t> immunoreactivity, confirming induction of apoptosis, in cells expressing TDP-43 M337V and ERp57. Neuro-2a cells were co-expressed with either wild-type TDP-43 or TDP-43 M337V (green) and ERp57 for 72 h, followed by immunocytochemistry using anti-activated caspase-3 antibodies (red), visualized using confocal microscopy. Nuclei are shown by Hoechst stain (blue). White arrow represents caspase-3 activation, indicating apoptosis is underway. As expected, fewer cells expressing wild-type TDP-43 (row 1) displayed caspase-3 activation, compared to cells expressing TDP-43 M337V (row 3). However, fewer cells expressing TDP-43 M337V with ERp57 (row 4) displayed caspase-3 activation, compared to those TDP-43 M337V cells transfected with empty vector. D Quantification of transfected cells visualized in 6C, immunostained using anti-activated caspase-3 antibodies. Results are expressed as mean ± SD, n = 3. Over-expression of ERp57 with TDP-43 M337V significantly decreased the proportion of cells with activated caspase-3, indicating apoptotic cell death is underway, compared to cells expressing empty vector only (**p < 0.01, ***p<0.001 )
    Anti Rabbit Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti rabbit cleaved caspase 3/product/Cell Signaling Technology Inc
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    1) Product Images from "Protein Disulfide Isomerase Endoplasmic Reticulum Protein 57 (ERp57) is Protective Against ALS-Associated Mutant TDP-43 in Neuronal Cells"

    Article Title: Protein Disulfide Isomerase Endoplasmic Reticulum Protein 57 (ERp57) is Protective Against ALS-Associated Mutant TDP-43 in Neuronal Cells

    Journal: Neuromolecular Medicine

    doi: 10.1007/s12017-024-08787-0

    ERp57 protects against mutant TDP-43 induced cell death in neuronal cell lines A Neuro-2a cells were co-expressed with wild-type TDP-43 (TDP-WT) or TDP-43 M337V (M337V, green) and V5 tagged ERp57 (red), examined by confocal microscopy at 72 h post transfection. Nuclei are shown by Hoechst stain (blue). Arrow represents condensed or fragmented nuclei, indicating apoptosis is underway. Few cells expressing TDP-WT (panel 1) or TDP-WT co-expressing ERp57 (panel 2) contained fragmented nuclei and hence were apoptotic (< 1%) but more cells expressing TDP-43 M337V (panel 3) displayed Hoechst-stained condensed nuclei, indicating apoptosis, indicated by white arrows (middle panel). However, fewer cells co-expressing TDP-43 M337V with ERp57 (panel 3) were undergoing apoptosis compared to those transfected with empty vector, scale bar = 5 µm. B Quantification of apoptotic nuclei in cells in 5A expressing TDP-43 and ERp57. Results are expressed as mean ± SD, n = 3. A significant difference in apoptosis was observed between wild-type TDP-43 and TDP-43 M337V cells (****p < 0.0001). Over-expression of ERp57 with TDP-43 M337V resulted in significantly fewer cells undergoing apoptosis compared to cells transfected with empty vector only (***p < 0.001). C Activated caspase-3 immunoreactivity, confirming induction of apoptosis, in cells expressing TDP-43 M337V and ERp57. Neuro-2a cells were co-expressed with either wild-type TDP-43 or TDP-43 M337V (green) and ERp57 for 72 h, followed by immunocytochemistry using anti-activated caspase-3 antibodies (red), visualized using confocal microscopy. Nuclei are shown by Hoechst stain (blue). White arrow represents caspase-3 activation, indicating apoptosis is underway. As expected, fewer cells expressing wild-type TDP-43 (row 1) displayed caspase-3 activation, compared to cells expressing TDP-43 M337V (row 3). However, fewer cells expressing TDP-43 M337V with ERp57 (row 4) displayed caspase-3 activation, compared to those TDP-43 M337V cells transfected with empty vector. D Quantification of transfected cells visualized in 6C, immunostained using anti-activated caspase-3 antibodies. Results are expressed as mean ± SD, n = 3. Over-expression of ERp57 with TDP-43 M337V significantly decreased the proportion of cells with activated caspase-3, indicating apoptotic cell death is underway, compared to cells expressing empty vector only (**p < 0.01, ***p<0.001 )
    Figure Legend Snippet: ERp57 protects against mutant TDP-43 induced cell death in neuronal cell lines A Neuro-2a cells were co-expressed with wild-type TDP-43 (TDP-WT) or TDP-43 M337V (M337V, green) and V5 tagged ERp57 (red), examined by confocal microscopy at 72 h post transfection. Nuclei are shown by Hoechst stain (blue). Arrow represents condensed or fragmented nuclei, indicating apoptosis is underway. Few cells expressing TDP-WT (panel 1) or TDP-WT co-expressing ERp57 (panel 2) contained fragmented nuclei and hence were apoptotic (< 1%) but more cells expressing TDP-43 M337V (panel 3) displayed Hoechst-stained condensed nuclei, indicating apoptosis, indicated by white arrows (middle panel). However, fewer cells co-expressing TDP-43 M337V with ERp57 (panel 3) were undergoing apoptosis compared to those transfected with empty vector, scale bar = 5 µm. B Quantification of apoptotic nuclei in cells in 5A expressing TDP-43 and ERp57. Results are expressed as mean ± SD, n = 3. A significant difference in apoptosis was observed between wild-type TDP-43 and TDP-43 M337V cells (****p < 0.0001). Over-expression of ERp57 with TDP-43 M337V resulted in significantly fewer cells undergoing apoptosis compared to cells transfected with empty vector only (***p < 0.001). C Activated caspase-3 immunoreactivity, confirming induction of apoptosis, in cells expressing TDP-43 M337V and ERp57. Neuro-2a cells were co-expressed with either wild-type TDP-43 or TDP-43 M337V (green) and ERp57 for 72 h, followed by immunocytochemistry using anti-activated caspase-3 antibodies (red), visualized using confocal microscopy. Nuclei are shown by Hoechst stain (blue). White arrow represents caspase-3 activation, indicating apoptosis is underway. As expected, fewer cells expressing wild-type TDP-43 (row 1) displayed caspase-3 activation, compared to cells expressing TDP-43 M337V (row 3). However, fewer cells expressing TDP-43 M337V with ERp57 (row 4) displayed caspase-3 activation, compared to those TDP-43 M337V cells transfected with empty vector. D Quantification of transfected cells visualized in 6C, immunostained using anti-activated caspase-3 antibodies. Results are expressed as mean ± SD, n = 3. Over-expression of ERp57 with TDP-43 M337V significantly decreased the proportion of cells with activated caspase-3, indicating apoptotic cell death is underway, compared to cells expressing empty vector only (**p < 0.01, ***p<0.001 )

    Techniques Used: Mutagenesis, Confocal Microscopy, Transfection, Staining, Expressing, Plasmid Preparation, Over Expression, Immunocytochemistry, Activation Assay

    alexa fluor 647 cleaved caspase 3 rabbit mab asp175  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc alexa fluor 647 cleaved caspase 3 rabbit mab asp175
    Neuro-2A cultures were infected with dLAT2903, McKrae, and ΔsncRNA1&2 viruses (10 pfu/cell for 24 hr) or mock infected. ( A) Detection of cleaved <t>caspase-3</t> in infected cells . At 24 hr PI, cells were harvested and reacted with anti-cleaved capase-3 antibody and FACS analysis was performed for expression of caspase-3 (see ). Experiments were repeated twice; and ( B) Quantification of FACS analysis from A . Percent of cleaved capase-3 positive cells for each infected or mock infected cells were counted. Each bar represents the mean ± SEM of cleaved capase-3-positive cells (N = 6).
    Alexa Fluor 647 Cleaved Caspase 3 Rabbit Mab Asp175, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alexa fluor 647 cleaved caspase 3 rabbit mab asp175/product/Cell Signaling Technology Inc
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    1) Product Images from "The anti-apoptotic function of HSV-1 LAT in neuronal cell cultures but not its function during reactivation correlates with expression of two small non-coding RNAs, sncRNA1&2"

    Article Title: The anti-apoptotic function of HSV-1 LAT in neuronal cell cultures but not its function during reactivation correlates with expression of two small non-coding RNAs, sncRNA1&2

    Journal: PLOS Pathogens

    doi: 10.1371/journal.ppat.1012307

    Neuro-2A cultures were infected with dLAT2903, McKrae, and ΔsncRNA1&2 viruses (10 pfu/cell for 24 hr) or mock infected. ( A) Detection of cleaved caspase-3 in infected cells . At 24 hr PI, cells were harvested and reacted with anti-cleaved capase-3 antibody and FACS analysis was performed for expression of caspase-3 (see ). Experiments were repeated twice; and ( B) Quantification of FACS analysis from A . Percent of cleaved capase-3 positive cells for each infected or mock infected cells were counted. Each bar represents the mean ± SEM of cleaved capase-3-positive cells (N = 6).
    Figure Legend Snippet: Neuro-2A cultures were infected with dLAT2903, McKrae, and ΔsncRNA1&2 viruses (10 pfu/cell for 24 hr) or mock infected. ( A) Detection of cleaved caspase-3 in infected cells . At 24 hr PI, cells were harvested and reacted with anti-cleaved capase-3 antibody and FACS analysis was performed for expression of caspase-3 (see ). Experiments were repeated twice; and ( B) Quantification of FACS analysis from A . Percent of cleaved capase-3 positive cells for each infected or mock infected cells were counted. Each bar represents the mean ± SEM of cleaved capase-3-positive cells (N = 6).

    Techniques Used: Infection, Expressing

    rabbit anti cleaved caspase 3 antibody  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc rabbit anti cleaved caspase 3 antibody
    Rabbit Anti Cleaved Caspase 3 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti cleaved caspase 3 antibody/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
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    af2305 cleaved caspase 3 rabbit  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc af2305 cleaved caspase 3 rabbit
    Af2305 Cleaved Caspase 3 Rabbit, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc cleaved caspase 3 rabbit 9664s ab 10831820 cst
    Cleaved Caspase 3 Rabbit 9664s Ab 10831820 Cst, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit anti human cleaved caspase 3 asp175 5a1e
    Western blot analysis was employed to assess the expression levels of (A) BAX, Bcl-2, and cleaved <t>caspase-3</t> in LNCaP cells after exposure to the different concentrations of EADR. The graph represents the relative intensity of (B) BAX, Bcl-2, and cleaved caspase-3 proteins in relation to EADR concentration. The data are presented as mean ± SD of results obtained from three independent experiments. Statistical significance was assigned to p -values less than 0.05 (*), indicating a significant difference compared to the control group.
    Rabbit Anti Human Cleaved Caspase 3 Asp175 5a1e, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc alexa fluor 647 cleaved caspase 3 rabbit mab asp175
    Western blot analysis was employed to assess the expression levels of (A) BAX, Bcl-2, and cleaved <t>caspase-3</t> in LNCaP cells after exposure to the different concentrations of EADR. The graph represents the relative intensity of (B) BAX, Bcl-2, and cleaved caspase-3 proteins in relation to EADR concentration. The data are presented as mean ± SD of results obtained from three independent experiments. Statistical significance was assigned to p -values less than 0.05 (*), indicating a significant difference compared to the control group.
    Alexa Fluor 647 Cleaved Caspase 3 Rabbit Mab Asp175, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Western blot analysis was employed to assess the expression levels of (A) BAX, Bcl-2, and cleaved caspase-3 in LNCaP cells after exposure to the different concentrations of EADR. The graph represents the relative intensity of (B) BAX, Bcl-2, and cleaved caspase-3 proteins in relation to EADR concentration. The data are presented as mean ± SD of results obtained from three independent experiments. Statistical significance was assigned to p -values less than 0.05 (*), indicating a significant difference compared to the control group.

    Journal: PeerJ

    Article Title: Diospyros rhodocalyx Kurz induces mitochondrial-mediated apoptosis via BAX, Bcl-2, and caspase-3 pathways in LNCaP human prostate cancer cell line

    doi: 10.7717/peerj.17637

    Figure Lengend Snippet: Western blot analysis was employed to assess the expression levels of (A) BAX, Bcl-2, and cleaved caspase-3 in LNCaP cells after exposure to the different concentrations of EADR. The graph represents the relative intensity of (B) BAX, Bcl-2, and cleaved caspase-3 proteins in relation to EADR concentration. The data are presented as mean ± SD of results obtained from three independent experiments. Statistical significance was assigned to p -values less than 0.05 (*), indicating a significant difference compared to the control group.

    Article Snippet: Rabbit anti-human BAX (D2E11) (cat. 5023), rabbit anti-human Bcl-2 (D55G8) (cat. 4223), rabbit anti-human cleaved caspase-3 (ASP175/5A1E) (cat. 9664), rabbit anti-human β-actin (13E5) (cat. 4970), and secondary anti-rabbit IgG horseradish peroxidase (HRP)-linked antibody (cat. 7074) were purchased from Cell Signaling Technology, Danvers, MA.

    Techniques: Western Blot, Expressing, Concentration Assay, Control

    Deficiency of DNAJC6 activates mitochondria-mediated pro-apoptotic pathway in dopaminergic neurons. ( A ) Cytochrome c was predominantly located within mitochondrial fractions of control and SC shRNA-transfected dopaminergic neurons. Three-day transfection of shRNAs targeting DNAJC6 significantly decreased mitochondrial cytochrome c and elevated cytosolic cytochrome c in dopaminergic neurons. Transfecting dopaminergic neurons with shRNAs of DNAJC6 significantly upregulated cytosolic active caspase-9 and active caspase-3. ( B ) DNAJC6 paucity induced by 4-day transfection of shRNAs targeting DNAJC6 significantly upregulated the percentage of TUNEL-positive apoptotic dopaminergic neurons. Each bar represents the mean ± S.E. value of 6 experiments. *** p < 0.001 compared with control dopaminergic neurons.

    Journal: International Journal of Molecular Sciences

    Article Title: Downregulation of Protease Cathepsin D and Upregulation of Pathologic α-Synuclein Mediate Paucity of DNAJC6-Induced Degeneration of Dopaminergic Neurons

    doi: 10.3390/ijms25126711

    Figure Lengend Snippet: Deficiency of DNAJC6 activates mitochondria-mediated pro-apoptotic pathway in dopaminergic neurons. ( A ) Cytochrome c was predominantly located within mitochondrial fractions of control and SC shRNA-transfected dopaminergic neurons. Three-day transfection of shRNAs targeting DNAJC6 significantly decreased mitochondrial cytochrome c and elevated cytosolic cytochrome c in dopaminergic neurons. Transfecting dopaminergic neurons with shRNAs of DNAJC6 significantly upregulated cytosolic active caspase-9 and active caspase-3. ( B ) DNAJC6 paucity induced by 4-day transfection of shRNAs targeting DNAJC6 significantly upregulated the percentage of TUNEL-positive apoptotic dopaminergic neurons. Each bar represents the mean ± S.E. value of 6 experiments. *** p < 0.001 compared with control dopaminergic neurons.

    Article Snippet: PVDF membranes were then incubated with the following primary antibodies: (1) rabbit monoclonal anti-cleaved active caspase 9 antiserum (Cell Signaling Technology); (2) rabbit anti-cleaved active caspase 3 monoclonal antibody (Cell Signaling Technology); (3) mouse anti-cytochrome c monoclonal antibody (Abcam).

    Techniques: Control, shRNA, Transfection, TUNEL Assay

    PARK19 DNAJC6 mutants fail to inhibit tunicamycin- or rotenone-evoked neurotoxicity, α-synuclein upregulation and apoptotic signaling in dopaminergic neurons. ( A ) FLAG-tagged human WT, Q789X or R927G DNAJC6 was transiently expressed in SH-SY5Y dopaminergic neurons. ( B ) Three-day incubation of 1 μM tunicamycin (TCM) or 0.5 μM rotenone (RTN) induced the neurodegeneration of dopaminergic cells. WT DNAJC6 significantly inhibited tunicamycin- or rotenone-evoked degeneration of dopaminergic neurons. On the contrary, PARK19 DNAJC6 mutants (Q789X or R927G) failed to prevent tunicamycin- or rotenone-triggered neurodegeneration. Each bar shows the mean ± S.E. value of 7 experiments. ( C ) Tunicamycin (TCM; 1 μM) upregulated the cytosolic expressions of active caspase-12, PERK, CHOP, IRE1α, Grp78 and α-synuclein. WT DNAJC6 significantly prevented the tunicamycin-evoked upregulation of cytosolic active caspase-12, PERK, CHOP, IRE1α, Grp78 and α-synuclein. PARK19 DNAJC6 mutants (Q789X or R927G) did not affect the upregulation of cytosolic active caspase-12, PERK, CHOP, IRE1α, Grp78 or α-synuclein caused by tunicamycin. ( D ) Rotenone (RTN; 0.5 μM) upregulated the cytosolic levels of α-synuclein, active caspase-3, active caspase-9 and cytochrome c. WT DNAJC6 inhibited the rotenone-evoked upregulation of cytosolic α-synuclein, active caspase-3, active caspase-9 and cytochrome c. PARK19 DNAJC6 mutants (Q789X or R927G) failed to reverse the upregulation of cytosolic α-synuclein, active caspase-3, active caspase-9 and cytochrome c caused by rotenone. Each bar represents the mean ± S.E. value of 6 experiments. ** p < 0.01 or *** p < 0.001 compared with control dopaminergic neurons. # p < 0.01 compared with tunicamycin- or rotenone-treated dopaminergic neurons.

    Journal: International Journal of Molecular Sciences

    Article Title: Downregulation of Protease Cathepsin D and Upregulation of Pathologic α-Synuclein Mediate Paucity of DNAJC6-Induced Degeneration of Dopaminergic Neurons

    doi: 10.3390/ijms25126711

    Figure Lengend Snippet: PARK19 DNAJC6 mutants fail to inhibit tunicamycin- or rotenone-evoked neurotoxicity, α-synuclein upregulation and apoptotic signaling in dopaminergic neurons. ( A ) FLAG-tagged human WT, Q789X or R927G DNAJC6 was transiently expressed in SH-SY5Y dopaminergic neurons. ( B ) Three-day incubation of 1 μM tunicamycin (TCM) or 0.5 μM rotenone (RTN) induced the neurodegeneration of dopaminergic cells. WT DNAJC6 significantly inhibited tunicamycin- or rotenone-evoked degeneration of dopaminergic neurons. On the contrary, PARK19 DNAJC6 mutants (Q789X or R927G) failed to prevent tunicamycin- or rotenone-triggered neurodegeneration. Each bar shows the mean ± S.E. value of 7 experiments. ( C ) Tunicamycin (TCM; 1 μM) upregulated the cytosolic expressions of active caspase-12, PERK, CHOP, IRE1α, Grp78 and α-synuclein. WT DNAJC6 significantly prevented the tunicamycin-evoked upregulation of cytosolic active caspase-12, PERK, CHOP, IRE1α, Grp78 and α-synuclein. PARK19 DNAJC6 mutants (Q789X or R927G) did not affect the upregulation of cytosolic active caspase-12, PERK, CHOP, IRE1α, Grp78 or α-synuclein caused by tunicamycin. ( D ) Rotenone (RTN; 0.5 μM) upregulated the cytosolic levels of α-synuclein, active caspase-3, active caspase-9 and cytochrome c. WT DNAJC6 inhibited the rotenone-evoked upregulation of cytosolic α-synuclein, active caspase-3, active caspase-9 and cytochrome c. PARK19 DNAJC6 mutants (Q789X or R927G) failed to reverse the upregulation of cytosolic α-synuclein, active caspase-3, active caspase-9 and cytochrome c caused by rotenone. Each bar represents the mean ± S.E. value of 6 experiments. ** p < 0.01 or *** p < 0.001 compared with control dopaminergic neurons. # p < 0.01 compared with tunicamycin- or rotenone-treated dopaminergic neurons.

    Article Snippet: PVDF membranes were then incubated with the following primary antibodies: (1) rabbit monoclonal anti-cleaved active caspase 9 antiserum (Cell Signaling Technology); (2) rabbit anti-cleaved active caspase 3 monoclonal antibody (Cell Signaling Technology); (3) mouse anti-cytochrome c monoclonal antibody (Abcam).

    Techniques: Incubation, Control