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rabbit polyclonal anti active caspase 3 antibody  (Novus Biologicals)


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    Structured Review

    Novus Biologicals rabbit polyclonal anti active caspase 3 antibody
    Rabbit Polyclonal Anti Active Caspase 3 Antibody, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 95/100, based on 181 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/polyclonal+rabbit+anti+caspase+3/Caspase-3+Antibody+-+(active%2Fcleaved)/pm42858657-125-38-43
    Average 95 stars, based on 181 article reviews
    rabbit polyclonal anti active caspase 3 antibody - by Bioz Stars, 2026-11
    95/100 stars

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    Related Articles

    Immunodetection:

    Article Title: Translocation of the proto-oncogene Bcl-6 in human glioblastoma multiforme.
    Article Snippet: .. For p53 and caspase 3 immunodetection, sections were pretreated with sodium citrate pH 6.1 (Dako Corporation, Milan, Italy) solution for 30 min at 98 C, for Bcl-6 with EDTA pH8 at the same time and temperature conditions, all in DAKO PT Link for antigen retrieval, and then incubated with monoclonal mouse anti-Bcl-6 (Dako), monoclonal mouse anti-p53 (Dako, Clone DO7), polyclonal rabbit anti-caspase 3 (Novus Biologicals), diluted 1:10, 1:50, 1:100, respectively. ..

    Incubation:

    Article Title: Translocation of the proto-oncogene Bcl-6 in human glioblastoma multiforme.
    Article Snippet: .. For p53 and caspase 3 immunodetection, sections were pretreated with sodium citrate pH 6.1 (Dako Corporation, Milan, Italy) solution for 30 min at 98 C, for Bcl-6 with EDTA pH8 at the same time and temperature conditions, all in DAKO PT Link for antigen retrieval, and then incubated with monoclonal mouse anti-Bcl-6 (Dako), monoclonal mouse anti-p53 (Dako, Clone DO7), polyclonal rabbit anti-caspase 3 (Novus Biologicals), diluted 1:10, 1:50, 1:100, respectively. ..



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    (A–B) Annexin V, CF450 staining (0.25 µg/ml) in NSCLC cells with QPRT knockdown cultured in 2D (A) and 3D conditions with representative spheroid images (B) (n = 4). (C) Quantification of cell viability using PI staining for PC9, H2009 and H2030, and SYTOX Green for H1581 cells with QPRT silencing upon Z-VAD-FMK (50 µM for PC9, H2009 and H2030, and 100 µM for H1581) treatment (n = 4). (D) Immunoblots for co-IP experiments of V5-QPRT and its interaction with pro-caspase 3 in PC9, H2009 and H2030 cells. (E) <t>Caspase-3/7</t> activity level in NSCLC cells with QPRT knockdown (n = 4). (F) Ribbon representation of QPRT (PDB: 5AYY) in complex with quinolinic acid with active site residues shown as sticks. Residues are colored according to ConSurf conservation scores . (G) Measurement of QPRT enzymatic activity over time of wild-type and catalytically inactive QPRT mutants purified form bacterial cells (n = 3). (H) Immunoblots for caspase-3 co-immunoprecipitated with catalytically inactive QPRT K139A versus wild-type QPRT. Data are represented as the mean ± SEM with statistical significance measured by one-way ANOVA followed by Dunnett’s post hoc test for panels A, B, and E, and followed by Tukey’s post hoc test for panel E. For the graph in panel G statistical significance was measured by two-way repeated measures ANOVA followed by Dunnett’s post hoc test and p value for the last time point is shown on the graphs. Scale bars in B indicate 400 µm.
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    (A–B) Annexin V, CF450 staining (0.25 µg/ml) in NSCLC cells with QPRT knockdown cultured in 2D (A) and 3D conditions with representative spheroid images (B) (n = 4). (C) Quantification of cell viability using PI staining for PC9, H2009 and H2030, and SYTOX Green for H1581 cells with QPRT silencing upon Z-VAD-FMK (50 µM for PC9, H2009 and H2030, and 100 µM for H1581) treatment (n = 4). (D) Immunoblots for co-IP experiments of V5-QPRT and its interaction with pro-caspase 3 in PC9, H2009 and H2030 cells. (E) <t>Caspase-3/7</t> activity level in NSCLC cells with QPRT knockdown (n = 4). (F) Ribbon representation of QPRT (PDB: 5AYY) in complex with quinolinic acid with active site residues shown as sticks. Residues are colored according to ConSurf conservation scores . (G) Measurement of QPRT enzymatic activity over time of wild-type and catalytically inactive QPRT mutants purified form bacterial cells (n = 3). (H) Immunoblots for caspase-3 co-immunoprecipitated with catalytically inactive QPRT K139A versus wild-type QPRT. Data are represented as the mean ± SEM with statistical significance measured by one-way ANOVA followed by Dunnett’s post hoc test for panels A, B, and E, and followed by Tukey’s post hoc test for panel E. For the graph in panel G statistical significance was measured by two-way repeated measures ANOVA followed by Dunnett’s post hoc test and p value for the last time point is shown on the graphs. Scale bars in B indicate 400 µm.
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    (A–B) Annexin V, CF450 staining (0.25 µg/ml) in NSCLC cells with QPRT knockdown cultured in 2D (A) and 3D conditions with representative spheroid images (B) (n = 4). (C) Quantification of cell viability using PI staining for PC9, H2009 and H2030, and SYTOX Green for H1581 cells with QPRT silencing upon Z-VAD-FMK (50 µM for PC9, H2009 and H2030, and 100 µM for H1581) treatment (n = 4). (D) Immunoblots for co-IP experiments of V5-QPRT and its interaction with pro-caspase 3 in PC9, H2009 and H2030 cells. (E) <t>Caspase-3/7</t> activity level in NSCLC cells with QPRT knockdown (n = 4). (F) Ribbon representation of QPRT (PDB: 5AYY) in complex with quinolinic acid with active site residues shown as sticks. Residues are colored according to ConSurf conservation scores . (G) Measurement of QPRT enzymatic activity over time of wild-type and catalytically inactive QPRT mutants purified form bacterial cells (n = 3). (H) Immunoblots for caspase-3 co-immunoprecipitated with catalytically inactive QPRT K139A versus wild-type QPRT. Data are represented as the mean ± SEM with statistical significance measured by one-way ANOVA followed by Dunnett’s post hoc test for panels A, B, and E, and followed by Tukey’s post hoc test for panel E. For the graph in panel G statistical significance was measured by two-way repeated measures ANOVA followed by Dunnett’s post hoc test and p value for the last time point is shown on the graphs. Scale bars in B indicate 400 µm.
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    (A–B) Annexin V, CF450 staining (0.25 µg/ml) in NSCLC cells with QPRT knockdown cultured in 2D (A) and 3D conditions with representative spheroid images (B) (n = 4). (C) Quantification of cell viability using PI staining for PC9, H2009 and H2030, and SYTOX Green for H1581 cells with QPRT silencing upon Z-VAD-FMK (50 µM for PC9, H2009 and H2030, and 100 µM for H1581) treatment (n = 4). (D) Immunoblots for co-IP experiments of V5-QPRT and its interaction with pro-caspase 3 in PC9, H2009 and H2030 cells. (E) <t>Caspase-3/7</t> activity level in NSCLC cells with QPRT knockdown (n = 4). (F) Ribbon representation of QPRT (PDB: 5AYY) in complex with quinolinic acid with active site residues shown as sticks. Residues are colored according to ConSurf conservation scores . (G) Measurement of QPRT enzymatic activity over time of wild-type and catalytically inactive QPRT mutants purified form bacterial cells (n = 3). (H) Immunoblots for caspase-3 co-immunoprecipitated with catalytically inactive QPRT K139A versus wild-type QPRT. Data are represented as the mean ± SEM with statistical significance measured by one-way ANOVA followed by Dunnett’s post hoc test for panels A, B, and E, and followed by Tukey’s post hoc test for panel E. For the graph in panel G statistical significance was measured by two-way repeated measures ANOVA followed by Dunnett’s post hoc test and p value for the last time point is shown on the graphs. Scale bars in B indicate 400 µm.
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    Cell Signaling Technology Inc anti active caspase 3 rabbit polyclonal antibody
    (A–B) Annexin V, CF450 staining (0.25 µg/ml) in NSCLC cells with QPRT knockdown cultured in 2D (A) and 3D conditions with representative spheroid images (B) (n = 4). (C) Quantification of cell viability using PI staining for PC9, H2009 and H2030, and SYTOX Green for H1581 cells with QPRT silencing upon Z-VAD-FMK (50 µM for PC9, H2009 and H2030, and 100 µM for H1581) treatment (n = 4). (D) Immunoblots for co-IP experiments of V5-QPRT and its interaction with pro-caspase 3 in PC9, H2009 and H2030 cells. (E) <t>Caspase-3/7</t> activity level in NSCLC cells with QPRT knockdown (n = 4). (F) Ribbon representation of QPRT (PDB: 5AYY) in complex with quinolinic acid with active site residues shown as sticks. Residues are colored according to ConSurf conservation scores . (G) Measurement of QPRT enzymatic activity over time of wild-type and catalytically inactive QPRT mutants purified form bacterial cells (n = 3). (H) Immunoblots for caspase-3 co-immunoprecipitated with catalytically inactive QPRT K139A versus wild-type QPRT. Data are represented as the mean ± SEM with statistical significance measured by one-way ANOVA followed by Dunnett’s post hoc test for panels A, B, and E, and followed by Tukey’s post hoc test for panel E. For the graph in panel G statistical significance was measured by two-way repeated measures ANOVA followed by Dunnett’s post hoc test and p value for the last time point is shown on the graphs. Scale bars in B indicate 400 µm.
    Anti Active Caspase 3 Rabbit Polyclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/polyclonal+rabbit+anti+caspase+3/Caspase-3+Antibody/pm41820376-316-24-30
    Average 99 stars, based on 1 article reviews
    anti active caspase 3 rabbit polyclonal antibody - by Bioz Stars, 2026-11
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      Buy from Supplier

    99
    Cell Signaling Technology Inc rabbit polyclonal cleaved caspase 3
    (A–B) Annexin V, CF450 staining (0.25 µg/ml) in NSCLC cells with QPRT knockdown cultured in 2D (A) and 3D conditions with representative spheroid images (B) (n = 4). (C) Quantification of cell viability using PI staining for PC9, H2009 and H2030, and SYTOX Green for H1581 cells with QPRT silencing upon Z-VAD-FMK (50 µM for PC9, H2009 and H2030, and 100 µM for H1581) treatment (n = 4). (D) Immunoblots for co-IP experiments of V5-QPRT and its interaction with pro-caspase 3 in PC9, H2009 and H2030 cells. (E) <t>Caspase-3/7</t> activity level in NSCLC cells with QPRT knockdown (n = 4). (F) Ribbon representation of QPRT (PDB: 5AYY) in complex with quinolinic acid with active site residues shown as sticks. Residues are colored according to ConSurf conservation scores . (G) Measurement of QPRT enzymatic activity over time of wild-type and catalytically inactive QPRT mutants purified form bacterial cells (n = 3). (H) Immunoblots for caspase-3 co-immunoprecipitated with catalytically inactive QPRT K139A versus wild-type QPRT. Data are represented as the mean ± SEM with statistical significance measured by one-way ANOVA followed by Dunnett’s post hoc test for panels A, B, and E, and followed by Tukey’s post hoc test for panel E. For the graph in panel G statistical significance was measured by two-way repeated measures ANOVA followed by Dunnett’s post hoc test and p value for the last time point is shown on the graphs. Scale bars in B indicate 400 µm.
    Rabbit Polyclonal Cleaved Caspase 3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/polyclonal+rabbit+anti+caspase+3/Cleaved+Caspase-3+(Asp175)+Antibody/10__1158_slash_0008___5472__can___25___2166-153-27-31
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    Image Search Results


    (A–B) Annexin V, CF450 staining (0.25 µg/ml) in NSCLC cells with QPRT knockdown cultured in 2D (A) and 3D conditions with representative spheroid images (B) (n = 4). (C) Quantification of cell viability using PI staining for PC9, H2009 and H2030, and SYTOX Green for H1581 cells with QPRT silencing upon Z-VAD-FMK (50 µM for PC9, H2009 and H2030, and 100 µM for H1581) treatment (n = 4). (D) Immunoblots for co-IP experiments of V5-QPRT and its interaction with pro-caspase 3 in PC9, H2009 and H2030 cells. (E) Caspase-3/7 activity level in NSCLC cells with QPRT knockdown (n = 4). (F) Ribbon representation of QPRT (PDB: 5AYY) in complex with quinolinic acid with active site residues shown as sticks. Residues are colored according to ConSurf conservation scores . (G) Measurement of QPRT enzymatic activity over time of wild-type and catalytically inactive QPRT mutants purified form bacterial cells (n = 3). (H) Immunoblots for caspase-3 co-immunoprecipitated with catalytically inactive QPRT K139A versus wild-type QPRT. Data are represented as the mean ± SEM with statistical significance measured by one-way ANOVA followed by Dunnett’s post hoc test for panels A, B, and E, and followed by Tukey’s post hoc test for panel E. For the graph in panel G statistical significance was measured by two-way repeated measures ANOVA followed by Dunnett’s post hoc test and p value for the last time point is shown on the graphs. Scale bars in B indicate 400 µm.

    Journal: bioRxiv

    Article Title: Quinolinic acid phosphoribosyl transferase moonlights as an apoptosis regulator to empower lung cancer progression

    doi: 10.64898/2026.04.01.715697

    Figure Lengend Snippet: (A–B) Annexin V, CF450 staining (0.25 µg/ml) in NSCLC cells with QPRT knockdown cultured in 2D (A) and 3D conditions with representative spheroid images (B) (n = 4). (C) Quantification of cell viability using PI staining for PC9, H2009 and H2030, and SYTOX Green for H1581 cells with QPRT silencing upon Z-VAD-FMK (50 µM for PC9, H2009 and H2030, and 100 µM for H1581) treatment (n = 4). (D) Immunoblots for co-IP experiments of V5-QPRT and its interaction with pro-caspase 3 in PC9, H2009 and H2030 cells. (E) Caspase-3/7 activity level in NSCLC cells with QPRT knockdown (n = 4). (F) Ribbon representation of QPRT (PDB: 5AYY) in complex with quinolinic acid with active site residues shown as sticks. Residues are colored according to ConSurf conservation scores . (G) Measurement of QPRT enzymatic activity over time of wild-type and catalytically inactive QPRT mutants purified form bacterial cells (n = 3). (H) Immunoblots for caspase-3 co-immunoprecipitated with catalytically inactive QPRT K139A versus wild-type QPRT. Data are represented as the mean ± SEM with statistical significance measured by one-way ANOVA followed by Dunnett’s post hoc test for panels A, B, and E, and followed by Tukey’s post hoc test for panel E. For the graph in panel G statistical significance was measured by two-way repeated measures ANOVA followed by Dunnett’s post hoc test and p value for the last time point is shown on the graphs. Scale bars in B indicate 400 µm.

    Article Snippet: For anti-Caspase-3 rabbit polyclonal Ab (Cell Signaling Technology, 9662S) 5% BSA in TBST was used to block the membranes instead of milk.

    Techniques: Staining, Knockdown, Cell Culture, Western Blot, Co-Immunoprecipitation Assay, Activity Assay, Purification, Immunoprecipitation

    In NSCLC cells as diagrammed in de novo NAD + biosynthesis is inactive, and NAD + pools are fueled by the salvage pathways and by the Preiss-Handler pathway. Instead, QPRT functions as an apoptosis inhibitor by interacting with caspase 3 and preventing its activation thereby conferring NSCLC resistance to apoptosis and enabling them to thrive through the stresses of tumor progression (2) .

    Journal: bioRxiv

    Article Title: Quinolinic acid phosphoribosyl transferase moonlights as an apoptosis regulator to empower lung cancer progression

    doi: 10.64898/2026.04.01.715697

    Figure Lengend Snippet: In NSCLC cells as diagrammed in de novo NAD + biosynthesis is inactive, and NAD + pools are fueled by the salvage pathways and by the Preiss-Handler pathway. Instead, QPRT functions as an apoptosis inhibitor by interacting with caspase 3 and preventing its activation thereby conferring NSCLC resistance to apoptosis and enabling them to thrive through the stresses of tumor progression (2) .

    Article Snippet: For anti-Caspase-3 rabbit polyclonal Ab (Cell Signaling Technology, 9662S) 5% BSA in TBST was used to block the membranes instead of milk.

    Techniques: Activation Assay