parp Stressgen Inc Search Results


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  • 90
    Millipore rabbit anti parp antibodies
    Rabbit Anti Parp Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Cell Signaling Technology Inc anti parp1
    Pharmacodynamic studies of compound 12 in the MDA-MB-231 xenograft tumors in mice. SCID mice bearing MDA-MB-231 xenograft tumors were treated with compound 12 at 5 mg/kg intravenously. Mice were sacrificed at indicated time-points and tumor tissue lysates were examined by western blot analysis with specific antibodies against cIAP1, <t>XIAP,</t> caspase-3 (C3), <t>PARP</t> and cleaved PARP. GAPDH was used as the loading control.
    Anti Parp1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 674 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    parp  (Abcam)
    90
    Abcam parp
    Effect of <t>MMP19</t> and ASNS knockdown on cisplatin-induced DNA damage and apoptosis S16 cells were transiently transfected with siRNAs against ASNS and MMP19 or scrambled control siRNA followed by treatment with cisplatin at different doses and analysis of DNA damage by detection of γ-H2AX and apoptosis by detection of cleaved <t>PARP</t> on Western blot (A), by staining of disintegrated nuclei (C), or by determination of cell death using ELISA (B). Actin was used as a loading control for Western blot analysis. The apoptosis assay and detection of γ-H2AX and cleaved PARP (cPARP) for ASNS knockdown cells were performed in the condition with supplementation of 0.4 mM Asn.
    Parp, supplied by Abcam, used in various techniques. Bioz Stars score: 90/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    GeneTex anti parp1
    Effect of <t>MMP19</t> and ASNS knockdown on cisplatin-induced DNA damage and apoptosis S16 cells were transiently transfected with siRNAs against ASNS and MMP19 or scrambled control siRNA followed by treatment with cisplatin at different doses and analysis of DNA damage by detection of γ-H2AX and apoptosis by detection of cleaved <t>PARP</t> on Western blot (A), by staining of disintegrated nuclei (C), or by determination of cell death using ELISA (B). Actin was used as a loading control for Western blot analysis. The apoptosis assay and detection of γ-H2AX and cleaved PARP (cPARP) for ASNS knockdown cells were performed in the condition with supplementation of 0.4 mM Asn.
    Anti Parp1, supplied by GeneTex, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc parp
    Impact of AIF expression on the cytotoxicity of menadione A. After 3h treatment with (+) or without (−) 50μM menadione, the subcellular localization of AIF in U2OS cells was checked by immunoblot in the indicated fractions, using antibodies directed against proteins localized in mitochondria (HSP60, VDAC and cytochrome c ), cytosol (caspase-3) or nuclei <t>(PARP).</t> B. Extracts of U2OS cells (duplicates) subjected to the transfection with AIF-specific (AIF.1 and AIF.2) or control (Co.1 and Co.2) siRNA were analyzed by immunoblot for the abundance of AIF. Actin was used as a loading control. C. D. U2OS cells transfected with two distinct control siRNAs (Co.1 and Co.2) or two distinct, non-overlapping siRNAs targeting AIF (siRNA AIF.1 and AIF.2) were treated with 50μM menadione or the solvent (Control) for 3h and drug-induced cell death was quantified by flow cytometric assessment (pictograms shown in C; histograms shown in D) of DAPI uptake (DAPI positivity) and forward light scatter (FSC) analysis that allows for the identification of apoptotic cells according to their reduced size (low FSC). Data are expressed as mean values ± SEM.
    Parp, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 325 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Biomol GmbH anti parp1 c2 10 antibodies
    Impact of AIF expression on the cytotoxicity of menadione A. After 3h treatment with (+) or without (−) 50μM menadione, the subcellular localization of AIF in U2OS cells was checked by immunoblot in the indicated fractions, using antibodies directed against proteins localized in mitochondria (HSP60, VDAC and cytochrome c ), cytosol (caspase-3) or nuclei <t>(PARP).</t> B. Extracts of U2OS cells (duplicates) subjected to the transfection with AIF-specific (AIF.1 and AIF.2) or control (Co.1 and Co.2) siRNA were analyzed by immunoblot for the abundance of AIF. Actin was used as a loading control. C. D. U2OS cells transfected with two distinct control siRNAs (Co.1 and Co.2) or two distinct, non-overlapping siRNAs targeting AIF (siRNA AIF.1 and AIF.2) were treated with 50μM menadione or the solvent (Control) for 3h and drug-induced cell death was quantified by flow cytometric assessment (pictograms shown in C; histograms shown in D) of DAPI uptake (DAPI positivity) and forward light scatter (FSC) analysis that allows for the identification of apoptotic cells according to their reduced size (low FSC). Data are expressed as mean values ± SEM.
    Anti Parp1 C2 10 Antibodies, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Promega parp degradation fragments
    Effect of ischemic conditioning on mitochondrial cytochrome C (Mcytc) and cytosolic cytochrome C (Ccytc) (A), autophagy- (B), apoptosis- (C), and antioxidant-related (D) proteins in the rat kidney subjected to ischemia/reperfusion injury . I30 × 2 decreased Ccytc release when compared to I15 × 4 and I60 kidneys. In the autophagy-related protein expression, the expression in LC3 and Beclin-1 protein is implicated in an order of I30 × 2 > I15 × 4 > I60 > CN. In the proapoptotic mechanisms, increased Bax/Bcl-2 ratio, active <t>CPP32</t> and <t>PARP</t> degradation expression are displayed in an order of I30 × 2 > I15 × 4 > I60 > CN. In the antioxidant protein expression, the expression in MnSOD, CuZnSOD amd catalase is demonstrated in an order of I30 × 2 > I15 × 4 > I60 > control (CN). *, P
    Parp Degradation Fragments, supplied by Promega, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Santa Cruz Biotechnology parp
    Knockdown of <t>GRP78</t> sensitizes cancer cells to HDAC inhibitors-mediated apoptosis A , MDA-MB-435 cells were transfected with siRNA against GRP78 (siGrp78) or a random control (siCtrl), and 48 h later, were either non-treated (-) or treated (+) with TSA for 24 h. The upper panel shows GRP78 levels in the transfected cells with β-actin as loading control. Lower panel shows the percent of apoptotic cells under each condition as determined by mitochondrial membrane potential staining using the JC-1 assay. B , HCT116 cells were subjected to the same conditions as ( A ) and the cell lysates were assayed for <t>PARP</t> cleavage by Western blot. The normal length (116 kDa) and apoptotic, cleaved forms (85 kDa) of PARP are indicated. GAPDH was used as a control.
    Parp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 99/100, based on 85 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Santa Cruz Biotechnology human parp
    Knockdown of <t>GRP78</t> sensitizes cancer cells to HDAC inhibitors-mediated apoptosis A , MDA-MB-435 cells were transfected with siRNA against GRP78 (siGrp78) or a random control (siCtrl), and 48 h later, were either non-treated (-) or treated (+) with TSA for 24 h. The upper panel shows GRP78 levels in the transfected cells with β-actin as loading control. Lower panel shows the percent of apoptotic cells under each condition as determined by mitochondrial membrane potential staining using the JC-1 assay. B , HCT116 cells were subjected to the same conditions as ( A ) and the cell lysates were assayed for <t>PARP</t> cleavage by Western blot. The normal length (116 kDa) and apoptotic, cleaved forms (85 kDa) of PARP are indicated. GAPDH was used as a control.
    Human Parp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 80/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Becton Dickinson cleaved parp
    Knockdown of <t>GRP78</t> sensitizes cancer cells to HDAC inhibitors-mediated apoptosis A , MDA-MB-435 cells were transfected with siRNA against GRP78 (siGrp78) or a random control (siCtrl), and 48 h later, were either non-treated (-) or treated (+) with TSA for 24 h. The upper panel shows GRP78 levels in the transfected cells with β-actin as loading control. Lower panel shows the percent of apoptotic cells under each condition as determined by mitochondrial membrane potential staining using the JC-1 assay. B , HCT116 cells were subjected to the same conditions as ( A ) and the cell lysates were assayed for <t>PARP</t> cleavage by Western blot. The normal length (116 kDa) and apoptotic, cleaved forms (85 kDa) of PARP are indicated. GAPDH was used as a control.
    Cleaved Parp, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 99/100, based on 198 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Cell Signaling Technology Inc cleaved parp
    GLN’s intestinal protection is inhibited by G RGD SP. A) IEC-6 cells were treated for 1 h with either media, G RGD SP or G RGE SP before the cells were treated with 0, 2, 10 or 20 mM GLN. Cell survival, following lethal HS (44°C), was measured via MTS assay. All groups were normalized to their non-HS controls to account for differences in cell growth. Assays were carried out in triplicate, experiments were performed 4 times and shown as mean±SEM. B) IEC-6 cells were treated as described in Fig. 2A , but they underwent non-lethal HS (43°C). After 3 hours recovery at 37°C, <t>Bax</t> and Bcl-2 levels were measured by Western blot. Bax was ratioed to anti-apoptotic marker Bcl-2 and shown in fold change±SEM (n = 4). C) Representative Western blot of <t>PARP</t> and cleaved PARP and densitometric analysis of cleaved PARP ratioed to HS 0 mM GLN are displayed. Cleaved PARP levels are presented as fold change±SEM (n = 4).
    Cleaved Parp, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 5938 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Millipore monoclonal anti parp
    GLN’s intestinal protection is inhibited by G RGD SP. A) IEC-6 cells were treated for 1 h with either media, G RGD SP or G RGE SP before the cells were treated with 0, 2, 10 or 20 mM GLN. Cell survival, following lethal HS (44°C), was measured via MTS assay. All groups were normalized to their non-HS controls to account for differences in cell growth. Assays were carried out in triplicate, experiments were performed 4 times and shown as mean±SEM. B) IEC-6 cells were treated as described in Fig. 2A , but they underwent non-lethal HS (43°C). After 3 hours recovery at 37°C, <t>Bax</t> and Bcl-2 levels were measured by Western blot. Bax was ratioed to anti-apoptotic marker Bcl-2 and shown in fold change±SEM (n = 4). C) Representative Western blot of <t>PARP</t> and cleaved PARP and densitometric analysis of cleaved PARP ratioed to HS 0 mM GLN are displayed. Cleaved PARP levels are presented as fold change±SEM (n = 4).
    Monoclonal Anti Parp, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Cell Signaling Technology Inc anti cleaved parp
    Effects of 3-nitropropionic acid (3NP) and geldanamycin (GA) on apoptosis. Striatal cells were treated with GA, 3NP and GA+3NP. (Aa) After 24 h of treatment, cells were collected and protein extracts prepared from each samples were analyzed by immunoblotting using indicated antibodies. GA suppressed 3NP-induced <t>caspase-3</t> activation and level of cleaved <t>PARP.</t> β-actin was used as a loading control. (Ab and c) Quantitative analysis was obtained from three individual experiments (n=3). The nuclear morphological changes are shown by 3NP-treated striatal cells. (Ba) The abrogation of nuclear damage by GA was measured using DAPI staining and (Bb) quantitative analysis of apoptotic cells. The more apoptotic cells were observed in only 3NP treated striatal cells compared to GA+3NP-treated striatal cells. Apoptotic cells were quantitatively counted using a microscope. In only 3NP-170-treated striatal cells, ~42% of cells showed DNA fragmentation whereas ~21% of cells included fragmentation in GA+3NP-treated striatal cells. Approximately 100 DAPI-positive cells were counted in each experiment. Quantitative analysis was obtained from three individual experiments (n=3). * P
    Anti Cleaved Parp, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1283 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Pharmingen anti parp mab
    Fig. 4. Cell-stress-associated EndoG and <t>AIF</t> release is prevented by zVAD-fmk, unlike cytochrome c , Smac/Diablo and HtrA2/Omi. ( A ) Percentages of cells with apoptotic nuclei (percentage of apoptotic nuclei) in HeLa cells treated for 7 and 9 h with staurosporine (STS, 2 µM) or actinomycin D (ActD, 20 µM) in the absence or presence of zVAD-fmk (100 µM). ( B ) Cells were treated as in (A). Total cell extracts were analyzed by western blotting for caspase-9 and caspase-3 processing and <t>PARP</t> cleavage. ( C ) HeLa cells were treated as in (A). Cytosolic fraction and heavy membrane fraction were analyzed by western blotting for the presence of cytochrome c , Smac/Diablo, HtrA2/Omi, EndoG and AIF. As control for loading, actin was used in the cytosolic fraction and Cox IV in the heavy membrane fraction. ( D ) HeLa cells were treated as in (A) and then ΔΨm was assessed by flow cytometry using DiOC 6 (50 nM). Top: % indicates percentage of ΔΨm loss. Bottom: histogram showing the percentage of ΔΨm loss in three independent experiments. The asterisks indicate additional non-specific bands.
    Anti Parp Mab, supplied by Pharmingen, used in various techniques. Bioz Stars score: 80/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc rabbit anti parp
    Fig. 4. Cell-stress-associated EndoG and <t>AIF</t> release is prevented by zVAD-fmk, unlike cytochrome c , Smac/Diablo and HtrA2/Omi. ( A ) Percentages of cells with apoptotic nuclei (percentage of apoptotic nuclei) in HeLa cells treated for 7 and 9 h with staurosporine (STS, 2 µM) or actinomycin D (ActD, 20 µM) in the absence or presence of zVAD-fmk (100 µM). ( B ) Cells were treated as in (A). Total cell extracts were analyzed by western blotting for caspase-9 and caspase-3 processing and <t>PARP</t> cleavage. ( C ) HeLa cells were treated as in (A). Cytosolic fraction and heavy membrane fraction were analyzed by western blotting for the presence of cytochrome c , Smac/Diablo, HtrA2/Omi, EndoG and AIF. As control for loading, actin was used in the cytosolic fraction and Cox IV in the heavy membrane fraction. ( D ) HeLa cells were treated as in (A) and then ΔΨm was assessed by flow cytometry using DiOC 6 (50 nM). Top: % indicates percentage of ΔΨm loss. Bottom: histogram showing the percentage of ΔΨm loss in three independent experiments. The asterisks indicate additional non-specific bands.
    Rabbit Anti Parp, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 607 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Promega anti parp p85 fragment pab
    Fig. 4. Cell-stress-associated EndoG and <t>AIF</t> release is prevented by zVAD-fmk, unlike cytochrome c , Smac/Diablo and HtrA2/Omi. ( A ) Percentages of cells with apoptotic nuclei (percentage of apoptotic nuclei) in HeLa cells treated for 7 and 9 h with staurosporine (STS, 2 µM) or actinomycin D (ActD, 20 µM) in the absence or presence of zVAD-fmk (100 µM). ( B ) Cells were treated as in (A). Total cell extracts were analyzed by western blotting for caspase-9 and caspase-3 processing and <t>PARP</t> cleavage. ( C ) HeLa cells were treated as in (A). Cytosolic fraction and heavy membrane fraction were analyzed by western blotting for the presence of cytochrome c , Smac/Diablo, HtrA2/Omi, EndoG and AIF. As control for loading, actin was used in the cytosolic fraction and Cox IV in the heavy membrane fraction. ( D ) HeLa cells were treated as in (A) and then ΔΨm was assessed by flow cytometry using DiOC 6 (50 nM). Top: % indicates percentage of ΔΨm loss. Bottom: histogram showing the percentage of ΔΨm loss in three independent experiments. The asterisks indicate additional non-specific bands.
    Anti Parp P85 Fragment Pab, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 178 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Biomol GmbH anti parp
    Fig. 4. Cell-stress-associated EndoG and <t>AIF</t> release is prevented by zVAD-fmk, unlike cytochrome c , Smac/Diablo and HtrA2/Omi. ( A ) Percentages of cells with apoptotic nuclei (percentage of apoptotic nuclei) in HeLa cells treated for 7 and 9 h with staurosporine (STS, 2 µM) or actinomycin D (ActD, 20 µM) in the absence or presence of zVAD-fmk (100 µM). ( B ) Cells were treated as in (A). Total cell extracts were analyzed by western blotting for caspase-9 and caspase-3 processing and <t>PARP</t> cleavage. ( C ) HeLa cells were treated as in (A). Cytosolic fraction and heavy membrane fraction were analyzed by western blotting for the presence of cytochrome c , Smac/Diablo, HtrA2/Omi, EndoG and AIF. As control for loading, actin was used in the cytosolic fraction and Cox IV in the heavy membrane fraction. ( D ) HeLa cells were treated as in (A) and then ΔΨm was assessed by flow cytometry using DiOC 6 (50 nM). Top: % indicates percentage of ΔΨm loss. Bottom: histogram showing the percentage of ΔΨm loss in three independent experiments. The asterisks indicate additional non-specific bands.
    Anti Parp, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 96/100, based on 74 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Promega polyclonal anti cleaved parp
    Fig. 4. Cell-stress-associated EndoG and <t>AIF</t> release is prevented by zVAD-fmk, unlike cytochrome c , Smac/Diablo and HtrA2/Omi. ( A ) Percentages of cells with apoptotic nuclei (percentage of apoptotic nuclei) in HeLa cells treated for 7 and 9 h with staurosporine (STS, 2 µM) or actinomycin D (ActD, 20 µM) in the absence or presence of zVAD-fmk (100 µM). ( B ) Cells were treated as in (A). Total cell extracts were analyzed by western blotting for caspase-9 and caspase-3 processing and <t>PARP</t> cleavage. ( C ) HeLa cells were treated as in (A). Cytosolic fraction and heavy membrane fraction were analyzed by western blotting for the presence of cytochrome c , Smac/Diablo, HtrA2/Omi, EndoG and AIF. As control for loading, actin was used in the cytosolic fraction and Cox IV in the heavy membrane fraction. ( D ) HeLa cells were treated as in (A) and then ΔΨm was assessed by flow cytometry using DiOC 6 (50 nM). Top: % indicates percentage of ΔΨm loss. Bottom: histogram showing the percentage of ΔΨm loss in three independent experiments. The asterisks indicate additional non-specific bands.
    Polyclonal Anti Cleaved Parp, supplied by Promega, used in various techniques. Bioz Stars score: 77/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Cell Signaling Technology Inc rabbit anti cleaved parp
    Downregulation of Wnt-11 leads to apoptosis in prostate cancer cells . (a) Extracts from control shRNA and WNT11 shRNA LNCaP cells grown in androgen-depleted medium for 7 days were probed by western blotting for cleaved <t>PARP,</t> cleaved <t>caspase-9</t> and HSP60. (b) Caspase assays from control shRNA and WNT11 shRNA LNCaP cells grown in androgen-depleted medium for 4 days. Caspase activity was significantly higher in WNT11 shRNA cells (shaded bars) compared to in control shRNA cells (n = 6; p
    Rabbit Anti Cleaved Parp, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 391 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc mouse anti parp
    JNJ-26481585 and Doxorubicin cooperate to induce <t>caspase</t> activation and caspase-dependent apoptosis A. , Cells were treated with 15 nM JNJ-26481585 and/or 0.25 μg/ml Doxorubicin for indicated times. Cleavage of caspase-9, -8, -3 and <t>PARP</t> was assessed by Western blotting, GAPDH served as loading control. B. , Cells were treated for indicated times with 15 nM JNJ-26481585 and/or 0.25 μg/ml Doxorubicin. Apoptosis was determined by analysis of DNA fragmentation of PI-stained nuclei using flow cytometry. Mean and SEM of at least three independent experiments carried out in triplicate are shown; ** P
    Mouse Anti Parp, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc anti parp rabbit polyclonal antibody
    JNJ-26481585 and Doxorubicin cooperate to induce <t>caspase</t> activation and caspase-dependent apoptosis A. , Cells were treated with 15 nM JNJ-26481585 and/or 0.25 μg/ml Doxorubicin for indicated times. Cleavage of caspase-9, -8, -3 and <t>PARP</t> was assessed by Western blotting, GAPDH served as loading control. B. , Cells were treated for indicated times with 15 nM JNJ-26481585 and/or 0.25 μg/ml Doxorubicin. Apoptosis was determined by analysis of DNA fragmentation of PI-stained nuclei using flow cytometry. Mean and SEM of at least three independent experiments carried out in triplicate are shown; ** P
    Anti Parp Rabbit Polyclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc poly adp ribose polymerase parp
    Expression of proapoptotic proteins in the ischemic territory: <t>poly-ADP</t> ribose polymerase <t>(PARP;</t> A ) and cleaved PARP ( P = 0.1) ( B ); Bcl 2/adenovirus E1B 19-kDa interacting protein (BNip-3) ( P = 0.3; C ); apoptosis inducing factor (AIF;
    Poly Adp Ribose Polymerase Parp, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 388 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Santa Cruz Biotechnology anti parp polyclonal antibody
    Expression of proapoptotic proteins in the ischemic territory: <t>poly-ADP</t> ribose polymerase <t>(PARP;</t> A ) and cleaved PARP ( P = 0.1) ( B ); Bcl 2/adenovirus E1B 19-kDa interacting protein (BNip-3) ( P = 0.3; C ); apoptosis inducing factor (AIF;
    Anti Parp Polyclonal Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 89/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Expression of proapoptotic proteins in the ischemic territory: <t>poly-ADP</t> ribose polymerase <t>(PARP;</t> A ) and cleaved PARP ( P = 0.1) ( B ); Bcl 2/adenovirus E1B 19-kDa interacting protein (BNip-3) ( P = 0.3; C ); apoptosis inducing factor (AIF;
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    Comparison of phosphorylation of H2AX and <t>PAR</t> accumulation in response to low and high-input-power damage in two NIR systems. ( A ) Time course analysis of <t>γH2AX</t> following 60 mW and 100 mW damage in the Mira-900 system. PtK2 cells were fixed at specific time points p.i. as indicated at the top. Scale bar = 10 μm. ( B ) Similar analysis as in ( A ) with 15% and 25% input laser using the Meta system. Scale bar = 10 μm. ( C ) Localization of GFP-NTH1 DNA glycosylase and γH2AX response to laser damage with the indicated input power (15% and 25%) in the Meta system. Left: live cell image of GFP-NTH1 at 3 min p.i. Right: γH2AX immunostaining of the same cells fixed at 10 min p.i. Scale bar = 10 μm. ( D ) Left: Immunofluorescent staining of PAR at low (60 mW) and high (100 mW) input power in the Mira-900 system at 1 min p.i. Right: time course analysis of PAR response at low (15%) and high (25%) input power in the Meta system. Time points p.i. are indicated at the top. Scale bar = 10 μm. ( E ) Immunofluorescent staining of PAR and PARP1 at low and high input power at 3 min p.i. Mira-900 system (left) and Meta system (right) with and without PARP inhibitor NU1025. Scale bar = 10 μm.
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    Comparison of phosphorylation of H2AX and <t>PAR</t> accumulation in response to low and high-input-power damage in two NIR systems. ( A ) Time course analysis of <t>γH2AX</t> following 60 mW and 100 mW damage in the Mira-900 system. PtK2 cells were fixed at specific time points p.i. as indicated at the top. Scale bar = 10 μm. ( B ) Similar analysis as in ( A ) with 15% and 25% input laser using the Meta system. Scale bar = 10 μm. ( C ) Localization of GFP-NTH1 DNA glycosylase and γH2AX response to laser damage with the indicated input power (15% and 25%) in the Meta system. Left: live cell image of GFP-NTH1 at 3 min p.i. Right: γH2AX immunostaining of the same cells fixed at 10 min p.i. Scale bar = 10 μm. ( D ) Left: Immunofluorescent staining of PAR at low (60 mW) and high (100 mW) input power in the Mira-900 system at 1 min p.i. Right: time course analysis of PAR response at low (15%) and high (25%) input power in the Meta system. Time points p.i. are indicated at the top. Scale bar = 10 μm. ( E ) Immunofluorescent staining of PAR and PARP1 at low and high input power at 3 min p.i. Mira-900 system (left) and Meta system (right) with and without PARP inhibitor NU1025. Scale bar = 10 μm.
    Stressgen, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 95 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Protein expression analysis in a panel of human breast cancer cell lines and effect of NVP-AUY922 on the HSP90-p23 complex in BT-474 cells. (a) The expression of HSP90 and specific proteins affected by HSP90 inhibition (Her3 [EGFR3], Her2 [ErbB2, EGFR2], phospho Her2 [pHer2], EGFR, AKT [PKB], phospho-AKT [pAkt], estrogen receptor-alpha [ERa], PI3K [p110α], PDK1, <t>HSP70,</t> Hsc70, Rb, pMEK1/2, pERK, Bax, Bcl-2, Bad, and Bcl-XL) was analyzed in seven human breast cancer cell lines (BT20, BT-474, MDA-MB-157 [MB-157], MDA-MB-231 [MB-231], MDA-MB-468 [MB-468], SKBr3, and MCF-7) by Western blot analysis. (b) The ERBB2-overexpressing and estrogen receptor-positive cell line BT-474 was chosen for studies of the kinetics and concentration-dependent dissociation of HSP90-p23 complexes and client proteins in the presence of NVP-AUY922 or tanespimycin (17-AAG). The amount of p23 associated with HSP90 was determined by immunoprecipitating p23 followed by immunoblotting for HSP90. The levels of ERBB2, AKT, phosphorylated AKT and β-tubulin were determined by immunoblotting. DMSO, dimethyl sulfoxide; HSP90, heat shock protein 90.
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    Protein expression analysis in a panel of human breast cancer cell lines and effect of NVP-AUY922 on the HSP90-p23 complex in BT-474 cells. (a) The expression of HSP90 and specific proteins affected by HSP90 inhibition (Her3 [EGFR3], Her2 [ErbB2, EGFR2], phospho Her2 [pHer2], EGFR, AKT [PKB], phospho-AKT [pAkt], estrogen receptor-alpha [ERa], PI3K [p110α], PDK1, <t>HSP70,</t> Hsc70, Rb, pMEK1/2, pERK, Bax, Bcl-2, Bad, and Bcl-XL) was analyzed in seven human breast cancer cell lines (BT20, BT-474, MDA-MB-157 [MB-157], MDA-MB-231 [MB-231], MDA-MB-468 [MB-468], SKBr3, and MCF-7) by Western blot analysis. (b) The ERBB2-overexpressing and estrogen receptor-positive cell line BT-474 was chosen for studies of the kinetics and concentration-dependent dissociation of HSP90-p23 complexes and client proteins in the presence of NVP-AUY922 or tanespimycin (17-AAG). The amount of p23 associated with HSP90 was determined by immunoprecipitating p23 followed by immunoblotting for HSP90. The levels of ERBB2, AKT, phosphorylated AKT and β-tubulin were determined by immunoblotting. DMSO, dimethyl sulfoxide; HSP90, heat shock protein 90.
    Mpo Fluorometric Detection Kit, supplied by Assay Designs Inc, used in various techniques. Bioz Stars score: 78/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Protein expression analysis in a panel of human breast cancer cell lines and effect of NVP-AUY922 on the HSP90-p23 complex in BT-474 cells. (a) The expression of HSP90 and specific proteins affected by HSP90 inhibition (Her3 [EGFR3], Her2 [ErbB2, EGFR2], phospho Her2 [pHer2], EGFR, AKT [PKB], phospho-AKT [pAkt], estrogen receptor-alpha [ERa], PI3K [p110α], PDK1, <t>HSP70,</t> Hsc70, Rb, pMEK1/2, pERK, Bax, Bcl-2, Bad, and Bcl-XL) was analyzed in seven human breast cancer cell lines (BT20, BT-474, MDA-MB-157 [MB-157], MDA-MB-231 [MB-231], MDA-MB-468 [MB-468], SKBr3, and MCF-7) by Western blot analysis. (b) The ERBB2-overexpressing and estrogen receptor-positive cell line BT-474 was chosen for studies of the kinetics and concentration-dependent dissociation of HSP90-p23 complexes and client proteins in the presence of NVP-AUY922 or tanespimycin (17-AAG). The amount of p23 associated with HSP90 was determined by immunoprecipitating p23 followed by immunoblotting for HSP90. The levels of ERBB2, AKT, phosphorylated AKT and β-tubulin were determined by immunoblotting. DMSO, dimethyl sulfoxide; HSP90, heat shock protein 90.
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    Image Search Results


    Pharmacodynamic studies of compound 12 in the MDA-MB-231 xenograft tumors in mice. SCID mice bearing MDA-MB-231 xenograft tumors were treated with compound 12 at 5 mg/kg intravenously. Mice were sacrificed at indicated time-points and tumor tissue lysates were examined by western blot analysis with specific antibodies against cIAP1, XIAP, caspase-3 (C3), PARP and cleaved PARP. GAPDH was used as the loading control.

    Journal: Journal of medicinal chemistry

    Article Title: A Potent Bivalent Smac Mimetic (SM-1200) Achieving Rapid, Complete and Durable Tumor Regression in Mice

    doi: 10.1021/jm400216d

    Figure Lengend Snippet: Pharmacodynamic studies of compound 12 in the MDA-MB-231 xenograft tumors in mice. SCID mice bearing MDA-MB-231 xenograft tumors were treated with compound 12 at 5 mg/kg intravenously. Mice were sacrificed at indicated time-points and tumor tissue lysates were examined by western blot analysis with specific antibodies against cIAP1, XIAP, caspase-3 (C3), PARP and cleaved PARP. GAPDH was used as the loading control.

    Article Snippet: Primary antibody against cleaved caspase 3 was purchased from Stressgen Biotechnologies; Primary antibodies against cIAP1 and cIAP2 were purchased from R & D systems; Primary antibody against XIAP was purchased from BD Biosciences; and Primary antibodies against PARP and β-actin from Cell Signaling Technology.

    Techniques: Multiple Displacement Amplification, Mouse Assay, Western Blot

    PARP-1 cleavage upon treating with UV-C

    Journal: Molecular cancer research : MCR

    Article Title: Hsp27 Protects Adenocarcinoma Cells from UV-induced Apoptosis by Akt and p21 Dependent Pathway of Survival

    doi: 10.1158/1541-7786.MCR-10-0181

    Figure Lengend Snippet: PARP-1 cleavage upon treating with UV-C

    Article Snippet: Western blot analyses were performed using primary antibodies for Hsp27 (stressgen), p-Hsp 27, Bax, Bcl-2, p21, p-p21, p53, p15, PARP-1, GAPDH, Akt, p-p38MAPK and p-MAPKAP-2 (Cell Signaling, Beverly, MA) and enhanced chemiluminescence reagent (Pierce Protein Research Products, Rockford, IL).

    Techniques:

    Activation of PARP, caspases and other apoptosis mediators during HSP27-dependent gemcitabine-induced apoptosis. (A and B) Immunoblotting showing cleavage of PARP, CASPASE 3, CASPASE 8 and CASPASE 9 upon gemcitabine treatment in HSP27-overexpressing PL5/hu18 but not parental control cells in a dose-dependent (A) and time-dependent (B) manner. (C) Proliferation assays displaying abrogation of HSP27-dependent gemcitabine sensitivity through pre-incubation with the pan-caspase inhibitor Z-VAD-FMK at 20 μM for 3 hrs. Error bars represent SEM of at least three independent experiments. (D) Immunoblotting assessing expression changes of the indicated pro- or anti-apoptotic molecules in parental PL5 and PL5/hu18 cells upon treatment with gemcitabine at 25 nM at the indicated time-points. ß-ACTIN served as loading control. (E) Immunoblotting displaying time-dependent BIM expression changes in PL5/hu18 cells treated with gemcitabine at 25 nM. (F) Immunoblotting assessing expression changes of CHOP and GRP78 in parental PL5 and PL5/hu18 cells upon treatment with gemcitabine at 25 nM at the indicated time-points. ß-ACTIN served as loading control. Confirmatory HSP27 overexpression in PL5/hu18 cells is additionally depicted.

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Overexpression of heat shock protein 27 (HSP27) increases gemcitabine sensitivity in pancreatic cancer cells through S-phase arrest and apoptosis

    doi: 10.1111/jcmm.12444

    Figure Lengend Snippet: Activation of PARP, caspases and other apoptosis mediators during HSP27-dependent gemcitabine-induced apoptosis. (A and B) Immunoblotting showing cleavage of PARP, CASPASE 3, CASPASE 8 and CASPASE 9 upon gemcitabine treatment in HSP27-overexpressing PL5/hu18 but not parental control cells in a dose-dependent (A) and time-dependent (B) manner. (C) Proliferation assays displaying abrogation of HSP27-dependent gemcitabine sensitivity through pre-incubation with the pan-caspase inhibitor Z-VAD-FMK at 20 μM for 3 hrs. Error bars represent SEM of at least three independent experiments. (D) Immunoblotting assessing expression changes of the indicated pro- or anti-apoptotic molecules in parental PL5 and PL5/hu18 cells upon treatment with gemcitabine at 25 nM at the indicated time-points. ß-ACTIN served as loading control. (E) Immunoblotting displaying time-dependent BIM expression changes in PL5/hu18 cells treated with gemcitabine at 25 nM. (F) Immunoblotting assessing expression changes of CHOP and GRP78 in parental PL5 and PL5/hu18 cells upon treatment with gemcitabine at 25 nM at the indicated time-points. ß-ACTIN served as loading control. Confirmatory HSP27 overexpression in PL5/hu18 cells is additionally depicted.

    Article Snippet: The following first antibodies were used: anti-HSP27 (SPA-803; Stressgen/Enzo, Lörrach, Germany); anti-CASPASE 3, anti-CASPASE 8, anti-CASPASE 9, anti-PARP, anti-BCL-2, anti-BCL-xL, anti-BID, anti-BAX, anti-MCL-1 (all Cell Signaling Technology/New England Biolabs GmbH, Frankfurt am Main, Germany); anti-BAK, anti-BIM (BD Biosciences); anti-CHOP, anti-GRP78 (both Santa Cruz Biotechnology, Heidelberg, Germany).

    Techniques: Activation Assay, Incubation, Expressing, Over Expression

    α-Lipoic acid (α-LA) induces caspase 3 activation and poly ADP-ribose polymerase (PARP) degradation. A549 cells were treated with various concentrations of α-LA for 18 hours. Equal amounts of cell lysates were subjected to electrophoresis and expression of PARP and caspase 3 was evaluated by western blot analysis. Heat shock cognate protein 70 (Hsc 70) was used as a loading control.

    Journal: The Korean Journal of Thoracic and Cardiovascular Surgery

    Article Title: Induction of ER Stress-Mediated Apoptosis by ?-Lipoic Acid in A549 Cell Lines

    doi: 10.5090/kjtcs.2012.45.1.1

    Figure Lengend Snippet: α-Lipoic acid (α-LA) induces caspase 3 activation and poly ADP-ribose polymerase (PARP) degradation. A549 cells were treated with various concentrations of α-LA for 18 hours. Equal amounts of cell lysates were subjected to electrophoresis and expression of PARP and caspase 3 was evaluated by western blot analysis. Heat shock cognate protein 70 (Hsc 70) was used as a loading control.

    Article Snippet: X-linked inhibitor of apoptosis protein (XIAP) and Bcl2-associated X protein (BAX) antibodies were purchased from BD Biosciences Inc. (Franklin Lakes, NJ, USA), extracellular signal-regulated kinase (ERK) antibodies were obtained from Transduction Laboratory Inc. (Lexington, KY, USA), and poly (ADP-ribose) polymerase (PARP) antibodies were obtained from Cell Signaling Inc. (Beverly, MA, USA).

    Techniques: Activation Assay, Electrophoresis, Expressing, Western Blot

    Effect of MMP19 and ASNS knockdown on cisplatin-induced DNA damage and apoptosis S16 cells were transiently transfected with siRNAs against ASNS and MMP19 or scrambled control siRNA followed by treatment with cisplatin at different doses and analysis of DNA damage by detection of γ-H2AX and apoptosis by detection of cleaved PARP on Western blot (A), by staining of disintegrated nuclei (C), or by determination of cell death using ELISA (B). Actin was used as a loading control for Western blot analysis. The apoptosis assay and detection of γ-H2AX and cleaved PARP (cPARP) for ASNS knockdown cells were performed in the condition with supplementation of 0.4 mM Asn.

    Journal: Molecular cancer therapeutics

    Article Title: Over-expression of asparagine synthetase and matrix metalloproteinase 19 confers cisplatin sensitivity in nasopharyngeal carcinoma cells

    doi: 10.1158/1535-7163.MCT-12-1190

    Figure Lengend Snippet: Effect of MMP19 and ASNS knockdown on cisplatin-induced DNA damage and apoptosis S16 cells were transiently transfected with siRNAs against ASNS and MMP19 or scrambled control siRNA followed by treatment with cisplatin at different doses and analysis of DNA damage by detection of γ-H2AX and apoptosis by detection of cleaved PARP on Western blot (A), by staining of disintegrated nuclei (C), or by determination of cell death using ELISA (B). Actin was used as a loading control for Western blot analysis. The apoptosis assay and detection of γ-H2AX and cleaved PARP (cPARP) for ASNS knockdown cells were performed in the condition with supplementation of 0.4 mM Asn.

    Article Snippet: Anti-MMP19 (ab53146), ASNS (H00000440-B01), CGA (sc18224 or sc57185), p-H2AX (KAM-CC255), and cleaved PARP (19F4, #9546) antibodies were from Abcam (Cambridge, MA USA), ABNOVA (Taipei, Taiwan, China), Santa Cruz biotechnology Inc. (Santa Cruz, CA), Stressgen (Brussels, Belgium), and Cell Signaling Technology, Inc. (Danvers, MA), respectively.

    Techniques: Transfection, Western Blot, Staining, Enzyme-linked Immunosorbent Assay, Apoptosis Assay

    Impact of AIF expression on the cytotoxicity of menadione A. After 3h treatment with (+) or without (−) 50μM menadione, the subcellular localization of AIF in U2OS cells was checked by immunoblot in the indicated fractions, using antibodies directed against proteins localized in mitochondria (HSP60, VDAC and cytochrome c ), cytosol (caspase-3) or nuclei (PARP). B. Extracts of U2OS cells (duplicates) subjected to the transfection with AIF-specific (AIF.1 and AIF.2) or control (Co.1 and Co.2) siRNA were analyzed by immunoblot for the abundance of AIF. Actin was used as a loading control. C. D. U2OS cells transfected with two distinct control siRNAs (Co.1 and Co.2) or two distinct, non-overlapping siRNAs targeting AIF (siRNA AIF.1 and AIF.2) were treated with 50μM menadione or the solvent (Control) for 3h and drug-induced cell death was quantified by flow cytometric assessment (pictograms shown in C; histograms shown in D) of DAPI uptake (DAPI positivity) and forward light scatter (FSC) analysis that allows for the identification of apoptotic cells according to their reduced size (low FSC). Data are expressed as mean values ± SEM.

    Journal: Oncotarget

    Article Title: Apoptosis inducing factor (AIF) mediates lethal redox stress induced by menadione

    doi: 10.18632/oncotarget.12562

    Figure Lengend Snippet: Impact of AIF expression on the cytotoxicity of menadione A. After 3h treatment with (+) or without (−) 50μM menadione, the subcellular localization of AIF in U2OS cells was checked by immunoblot in the indicated fractions, using antibodies directed against proteins localized in mitochondria (HSP60, VDAC and cytochrome c ), cytosol (caspase-3) or nuclei (PARP). B. Extracts of U2OS cells (duplicates) subjected to the transfection with AIF-specific (AIF.1 and AIF.2) or control (Co.1 and Co.2) siRNA were analyzed by immunoblot for the abundance of AIF. Actin was used as a loading control. C. D. U2OS cells transfected with two distinct control siRNAs (Co.1 and Co.2) or two distinct, non-overlapping siRNAs targeting AIF (siRNA AIF.1 and AIF.2) were treated with 50μM menadione or the solvent (Control) for 3h and drug-induced cell death was quantified by flow cytometric assessment (pictograms shown in C; histograms shown in D) of DAPI uptake (DAPI positivity) and forward light scatter (FSC) analysis that allows for the identification of apoptotic cells according to their reduced size (low FSC). Data are expressed as mean values ± SEM.

    Article Snippet: Antibodies against the following proteins were used: actin (mouse mAb; CHEMICON); AIF (mouse mAB; Santa Cruz; rabbit pAB; Cell Signaling); Hsp60 (mouse mAb; Stressgen); caspase 3 (rabbit pAB; Cell Signaling); PARP (rabbit pAB; Cell Signaling); VDAC (rabbit pAB; Cell Signaling); Cytochrome C (mAB BD Bioscience).

    Techniques: Expressing, Transfection, Flow Cytometry

    Effect of ischemic conditioning on mitochondrial cytochrome C (Mcytc) and cytosolic cytochrome C (Ccytc) (A), autophagy- (B), apoptosis- (C), and antioxidant-related (D) proteins in the rat kidney subjected to ischemia/reperfusion injury . I30 × 2 decreased Ccytc release when compared to I15 × 4 and I60 kidneys. In the autophagy-related protein expression, the expression in LC3 and Beclin-1 protein is implicated in an order of I30 × 2 > I15 × 4 > I60 > CN. In the proapoptotic mechanisms, increased Bax/Bcl-2 ratio, active CPP32 and PARP degradation expression are displayed in an order of I30 × 2 > I15 × 4 > I60 > CN. In the antioxidant protein expression, the expression in MnSOD, CuZnSOD amd catalase is demonstrated in an order of I30 × 2 > I15 × 4 > I60 > control (CN). *, P

    Journal: Journal of Biomedical Science

    Article Title: Ischemic conditioning by short periods of reperfusion attenuates renal ischemia/reperfusion induced apoptosis and autophagy in the rat

    doi: 10.1186/1423-0127-16-19

    Figure Lengend Snippet: Effect of ischemic conditioning on mitochondrial cytochrome C (Mcytc) and cytosolic cytochrome C (Ccytc) (A), autophagy- (B), apoptosis- (C), and antioxidant-related (D) proteins in the rat kidney subjected to ischemia/reperfusion injury . I30 × 2 decreased Ccytc release when compared to I15 × 4 and I60 kidneys. In the autophagy-related protein expression, the expression in LC3 and Beclin-1 protein is implicated in an order of I30 × 2 > I15 × 4 > I60 > CN. In the proapoptotic mechanisms, increased Bax/Bcl-2 ratio, active CPP32 and PARP degradation expression are displayed in an order of I30 × 2 > I15 × 4 > I60 > CN. In the antioxidant protein expression, the expression in MnSOD, CuZnSOD amd catalase is demonstrated in an order of I30 × 2 > I15 × 4 > I60 > control (CN). *, P

    Article Snippet: Antibodies raised against polyclonal anti-Mn SOD (Stressgen Bioreagents Limited, Victoria, Canada), polyclonal rabbit anti-human CuZn SOD (Stress Marq Biosciences Inc., Victoria, Canada), catalase (Chemicon International Inc., Temecular, CA), Bax (Chemicon, Temecula, CA), Bcl-2 (Transduction, Bluegrass-Lexington, KY), the activation fragments of caspase 3 (CPP32/Yama/Apopain, Upstate Biotechnology, Lake Placid, NY), PARP degradation fragments (Promega, Madison, WI), LC3 (MLB), Beclin-1 (AnaSpec, Inc., San Jose, CA) and β-actin (Sigma, Saint Louis, MI) were used.

    Techniques: Expressing

    Knockdown of GRP78 sensitizes cancer cells to HDAC inhibitors-mediated apoptosis A , MDA-MB-435 cells were transfected with siRNA against GRP78 (siGrp78) or a random control (siCtrl), and 48 h later, were either non-treated (-) or treated (+) with TSA for 24 h. The upper panel shows GRP78 levels in the transfected cells with β-actin as loading control. Lower panel shows the percent of apoptotic cells under each condition as determined by mitochondrial membrane potential staining using the JC-1 assay. B , HCT116 cells were subjected to the same conditions as ( A ) and the cell lysates were assayed for PARP cleavage by Western blot. The normal length (116 kDa) and apoptotic, cleaved forms (85 kDa) of PARP are indicated. GAPDH was used as a control.

    Journal: Molecular cancer therapeutics

    Article Title: Transcriptional induction of GRP78/BiP by histone deacetylase inhibitors and resistance to histone deacetylase inhibitor-induced apoptosis

    doi: 10.1158/1535-7163.MCT-08-1166

    Figure Lengend Snippet: Knockdown of GRP78 sensitizes cancer cells to HDAC inhibitors-mediated apoptosis A , MDA-MB-435 cells were transfected with siRNA against GRP78 (siGrp78) or a random control (siCtrl), and 48 h later, were either non-treated (-) or treated (+) with TSA for 24 h. The upper panel shows GRP78 levels in the transfected cells with β-actin as loading control. Lower panel shows the percent of apoptotic cells under each condition as determined by mitochondrial membrane potential staining using the JC-1 assay. B , HCT116 cells were subjected to the same conditions as ( A ) and the cell lysates were assayed for PARP cleavage by Western blot. The normal length (116 kDa) and apoptotic, cleaved forms (85 kDa) of PARP are indicated. GAPDH was used as a control.

    Article Snippet: The antibodies against GRP78, CHOP, β-actin, GAPDH, HSP70, His, PDI, PARP (Santa Cruz Biotechnology, Inc.), caspase-7 (BD PharMingen), GRP94 (Stressgen) and FLAG (Sigma) were used per manufacturer’s recommendations.

    Techniques: Multiple Displacement Amplification, Transfection, Staining, Western Blot

    GLN’s intestinal protection is inhibited by G RGD SP. A) IEC-6 cells were treated for 1 h with either media, G RGD SP or G RGE SP before the cells were treated with 0, 2, 10 or 20 mM GLN. Cell survival, following lethal HS (44°C), was measured via MTS assay. All groups were normalized to their non-HS controls to account for differences in cell growth. Assays were carried out in triplicate, experiments were performed 4 times and shown as mean±SEM. B) IEC-6 cells were treated as described in Fig. 2A , but they underwent non-lethal HS (43°C). After 3 hours recovery at 37°C, Bax and Bcl-2 levels were measured by Western blot. Bax was ratioed to anti-apoptotic marker Bcl-2 and shown in fold change±SEM (n = 4). C) Representative Western blot of PARP and cleaved PARP and densitometric analysis of cleaved PARP ratioed to HS 0 mM GLN are displayed. Cleaved PARP levels are presented as fold change±SEM (n = 4).

    Journal: PLoS ONE

    Article Title: Fibronectin-Integrin Signaling Is Required for L-Glutamine's Protection against Gut Injury

    doi: 10.1371/journal.pone.0050185

    Figure Lengend Snippet: GLN’s intestinal protection is inhibited by G RGD SP. A) IEC-6 cells were treated for 1 h with either media, G RGD SP or G RGE SP before the cells were treated with 0, 2, 10 or 20 mM GLN. Cell survival, following lethal HS (44°C), was measured via MTS assay. All groups were normalized to their non-HS controls to account for differences in cell growth. Assays were carried out in triplicate, experiments were performed 4 times and shown as mean±SEM. B) IEC-6 cells were treated as described in Fig. 2A , but they underwent non-lethal HS (43°C). After 3 hours recovery at 37°C, Bax and Bcl-2 levels were measured by Western blot. Bax was ratioed to anti-apoptotic marker Bcl-2 and shown in fold change±SEM (n = 4). C) Representative Western blot of PARP and cleaved PARP and densitometric analysis of cleaved PARP ratioed to HS 0 mM GLN are displayed. Cleaved PARP levels are presented as fold change±SEM (n = 4).

    Article Snippet: Primary antibodies against HSP32 and HSP70 (1∶10,000 dilution) (StressGen, Victoria, BC, Canada) and FN (1∶10,000), or against total ERK1/2, [T(P)202 /Y(P)204 ]ERK1/2, total HSF-1, [S(P)303 ]HSF-1, cleaved caspase-3, cleaved PARP, bax, and bcl-2 (1∶1,000) (Cell signaling, Danvers, MA) were used.

    Techniques: MTS Assay, Western Blot, Marker

    Effects of 3-nitropropionic acid (3NP) and geldanamycin (GA) on apoptosis. Striatal cells were treated with GA, 3NP and GA+3NP. (Aa) After 24 h of treatment, cells were collected and protein extracts prepared from each samples were analyzed by immunoblotting using indicated antibodies. GA suppressed 3NP-induced caspase-3 activation and level of cleaved PARP. β-actin was used as a loading control. (Ab and c) Quantitative analysis was obtained from three individual experiments (n=3). The nuclear morphological changes are shown by 3NP-treated striatal cells. (Ba) The abrogation of nuclear damage by GA was measured using DAPI staining and (Bb) quantitative analysis of apoptotic cells. The more apoptotic cells were observed in only 3NP treated striatal cells compared to GA+3NP-treated striatal cells. Apoptotic cells were quantitatively counted using a microscope. In only 3NP-170-treated striatal cells, ~42% of cells showed DNA fragmentation whereas ~21% of cells included fragmentation in GA+3NP-treated striatal cells. Approximately 100 DAPI-positive cells were counted in each experiment. Quantitative analysis was obtained from three individual experiments (n=3). * P

    Journal: International Journal of Molecular Medicine

    Article Title: Geldanamycin attenuates 3-nitropropionic acid-induced apoptosis and JNK activation through the expression of HSP 70 in striatal cells

    doi: 10.3892/ijmm.2014.1747

    Figure Lengend Snippet: Effects of 3-nitropropionic acid (3NP) and geldanamycin (GA) on apoptosis. Striatal cells were treated with GA, 3NP and GA+3NP. (Aa) After 24 h of treatment, cells were collected and protein extracts prepared from each samples were analyzed by immunoblotting using indicated antibodies. GA suppressed 3NP-induced caspase-3 activation and level of cleaved PARP. β-actin was used as a loading control. (Ab and c) Quantitative analysis was obtained from three individual experiments (n=3). The nuclear morphological changes are shown by 3NP-treated striatal cells. (Ba) The abrogation of nuclear damage by GA was measured using DAPI staining and (Bb) quantitative analysis of apoptotic cells. The more apoptotic cells were observed in only 3NP treated striatal cells compared to GA+3NP-treated striatal cells. Apoptotic cells were quantitatively counted using a microscope. In only 3NP-170-treated striatal cells, ~42% of cells showed DNA fragmentation whereas ~21% of cells included fragmentation in GA+3NP-treated striatal cells. Approximately 100 DAPI-positive cells were counted in each experiment. Quantitative analysis was obtained from three individual experiments (n=3). * P

    Article Snippet: The membranes were blocked in 5% skim milk in TBST (20 mM Tris-HCl, pH 7.6, 137 mM NaCl, 0.05% Tween-20) for 30 min at room temperature and sequentially incubated with an appropriate antibody; anti-HSP 90 monoclonal antibody (1:1,000), anti-HSP 70 monoclonal antibody (1:1,000) (both from Stressgen Biotechnologies, Victoria, BC, Canada), anti-cleaved caspase-3 and total caspase-3 polyconal antibody (1:1,000), anti-Cleaved PARP and total PARP polyconal antibody (1:1,000) (Cell Signaling Technology, Inc., Danvers, MA, USA), anti-IκB-α monoclonal antibody (Santa Cruz Biotechnology Inc., Santa Cruz, CA, USA), total JNK and P-JNK polyconal antibody (1:1,000), anti-c-Jun and P-c-Jun polyconal antibody (1:1,000) (both from Cell Signaling Technology, Inc.) and β-actin monoclonal antibody (1:2,500; Sigma-Aldrich) in the same buffer overnight at 4°C.

    Techniques: Activation Assay, Staining, Microscopy

    PQ triggers cleavage of caspase substrates. N27 cells were treated with PQ (500 µM) for the indicated times. Cell extracts (100 µg of protein) were prepared as described in the section “Experimental Methods” and analyzed by Western blot analysis. Membranes were probed with anti-PARP antibody, rat specific anticleaved PARP antibody, or anti-p23 antibody. The PARP blot was probed with antiserum specific for cleaved PARP. Blots were reprobed with GAPDH antiserum to assess equality of loading. Each blot is representative of four independent experiments. Positions of molecular mass markers (in kDa) are indicated at left. The band density (integrated density value) is expressed graphically as a percentage ratio of densitometric optical density of cleaved PARP to that of GAPDH. Data (mean ± SD) are from four independent experiments. * P

    Journal: Neuromolecular medicine

    Article Title: Coupling Endoplasmic Reticulum Stress to the Cell Death Program in Dopaminergic Cells: Effect of Paraquat

    doi: 10.1007/s12017-008-8047-9

    Figure Lengend Snippet: PQ triggers cleavage of caspase substrates. N27 cells were treated with PQ (500 µM) for the indicated times. Cell extracts (100 µg of protein) were prepared as described in the section “Experimental Methods” and analyzed by Western blot analysis. Membranes were probed with anti-PARP antibody, rat specific anticleaved PARP antibody, or anti-p23 antibody. The PARP blot was probed with antiserum specific for cleaved PARP. Blots were reprobed with GAPDH antiserum to assess equality of loading. Each blot is representative of four independent experiments. Positions of molecular mass markers (in kDa) are indicated at left. The band density (integrated density value) is expressed graphically as a percentage ratio of densitometric optical density of cleaved PARP to that of GAPDH. Data (mean ± SD) are from four independent experiments. * P

    Article Snippet: Membranes were probed with either a 1:500 dilution of anti-KDEL monoclonal antibody (Stressgen), 1:500 dilution of anti-phospho-eIF2α rabbit monoclonal antibody, anti-eIF2α mouse monoclonal antibody, rat-specific anti-cleaved PARP, anti-caspase-7, or anti-caspase-3 antibodies (all from Cell Signaling Laboratories), a 1:1000 dilution of anti-p23 monoclonal antibody (BD Biosciences), a 1:500 dilution of anti-GADD153 antibody (Santa Cruz), or a 1:50,000 dilution of anti-GAPDH rabbit polyclonal anti-body (Research Diagnostics Inc).

    Techniques: Western Blot

    Fig. 4. Cell-stress-associated EndoG and AIF release is prevented by zVAD-fmk, unlike cytochrome c , Smac/Diablo and HtrA2/Omi. ( A ) Percentages of cells with apoptotic nuclei (percentage of apoptotic nuclei) in HeLa cells treated for 7 and 9 h with staurosporine (STS, 2 µM) or actinomycin D (ActD, 20 µM) in the absence or presence of zVAD-fmk (100 µM). ( B ) Cells were treated as in (A). Total cell extracts were analyzed by western blotting for caspase-9 and caspase-3 processing and PARP cleavage. ( C ) HeLa cells were treated as in (A). Cytosolic fraction and heavy membrane fraction were analyzed by western blotting for the presence of cytochrome c , Smac/Diablo, HtrA2/Omi, EndoG and AIF. As control for loading, actin was used in the cytosolic fraction and Cox IV in the heavy membrane fraction. ( D ) HeLa cells were treated as in (A) and then ΔΨm was assessed by flow cytometry using DiOC 6 (50 nM). Top: % indicates percentage of ΔΨm loss. Bottom: histogram showing the percentage of ΔΨm loss in three independent experiments. The asterisks indicate additional non-specific bands.

    Journal: The EMBO Journal

    Article Title: Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization

    doi: 10.1093/emboj/cdg423

    Figure Lengend Snippet: Fig. 4. Cell-stress-associated EndoG and AIF release is prevented by zVAD-fmk, unlike cytochrome c , Smac/Diablo and HtrA2/Omi. ( A ) Percentages of cells with apoptotic nuclei (percentage of apoptotic nuclei) in HeLa cells treated for 7 and 9 h with staurosporine (STS, 2 µM) or actinomycin D (ActD, 20 µM) in the absence or presence of zVAD-fmk (100 µM). ( B ) Cells were treated as in (A). Total cell extracts were analyzed by western blotting for caspase-9 and caspase-3 processing and PARP cleavage. ( C ) HeLa cells were treated as in (A). Cytosolic fraction and heavy membrane fraction were analyzed by western blotting for the presence of cytochrome c , Smac/Diablo, HtrA2/Omi, EndoG and AIF. As control for loading, actin was used in the cytosolic fraction and Cox IV in the heavy membrane fraction. ( D ) HeLa cells were treated as in (A) and then ΔΨm was assessed by flow cytometry using DiOC 6 (50 nM). Top: % indicates percentage of ΔΨm loss. Bottom: histogram showing the percentage of ΔΨm loss in three independent experiments. The asterisks indicate additional non-specific bands.

    Article Snippet: Antibodies used in immunoblotting were as follows: anti-cytochrome c mAb (clone 7H8.2C12, Pharmingen) (1/2000), rabbit polyclonal anti-Endo G (Pro-Sci Inc.) (1/1000), rabbit polyclonal anti-Smac/Diablo (Pro-Sci Inc.) (1/1000), a purified rabbit polyclonal anti-HtrA2/Omi antibody that we obtained from a rabbit immunized against a mixture of two different human HtrA2/Omi peptides (amino acids 65–80 and 203–220) (1/1000), anti-AIF mAb (clone E1, Santa Cruz) (1/2000), anti-PARP mAb (clone C2-10, Pharmingen) (1/2000), anti-VDAC mAb (clone Ab4, Calbiochem) (1/6000), anti-Cox IV mAb (clone 10G8, Molecular Probe) (1/1000), anti-actin mAb (Sigma) (1/5000) and rabbit polyclonal antibodies specific for caspase-9 (Cayman Chemicals) (1/1000) or caspase-3 (Stressgen) (1/2000).

    Techniques: Western Blot, Flow Cytometry, Cytometry

    Downregulation of Wnt-11 leads to apoptosis in prostate cancer cells . (a) Extracts from control shRNA and WNT11 shRNA LNCaP cells grown in androgen-depleted medium for 7 days were probed by western blotting for cleaved PARP, cleaved caspase-9 and HSP60. (b) Caspase assays from control shRNA and WNT11 shRNA LNCaP cells grown in androgen-depleted medium for 4 days. Caspase activity was significantly higher in WNT11 shRNA cells (shaded bars) compared to in control shRNA cells (n = 6; p

    Journal: Molecular Cancer

    Article Title: Wnt-11 promotes neuroendocrine-like differentiation, survival and migration of prostate cancer cells

    doi: 10.1186/1476-4598-9-55

    Figure Lengend Snippet: Downregulation of Wnt-11 leads to apoptosis in prostate cancer cells . (a) Extracts from control shRNA and WNT11 shRNA LNCaP cells grown in androgen-depleted medium for 7 days were probed by western blotting for cleaved PARP, cleaved caspase-9 and HSP60. (b) Caspase assays from control shRNA and WNT11 shRNA LNCaP cells grown in androgen-depleted medium for 4 days. Caspase activity was significantly higher in WNT11 shRNA cells (shaded bars) compared to in control shRNA cells (n = 6; p

    Article Snippet: Antibodies, western blotting and immunostaining The following antibodies were used: mouse anti-NSE (BBS/NC/V1-H14, Dako), rabbit anti-cleaved caspase-9 (Asp330; 9501) and rabbit anti-cleaved PARP (Asp214; 9541) (both from Cell Signalling Technology), rabbit anti-AR (N20; sc-816, Santa Cruz Biotechnology), mouse anti-HSP60 (SPA-806, Stressgen) and goat anti-Wnt-11 (R & D systems, AF2647).

    Techniques: shRNA, Western Blot, Activity Assay

    JNJ-26481585 and Doxorubicin cooperate to induce caspase activation and caspase-dependent apoptosis A. , Cells were treated with 15 nM JNJ-26481585 and/or 0.25 μg/ml Doxorubicin for indicated times. Cleavage of caspase-9, -8, -3 and PARP was assessed by Western blotting, GAPDH served as loading control. B. , Cells were treated for indicated times with 15 nM JNJ-26481585 and/or 0.25 μg/ml Doxorubicin. Apoptosis was determined by analysis of DNA fragmentation of PI-stained nuclei using flow cytometry. Mean and SEM of at least three independent experiments carried out in triplicate are shown; ** P

    Journal: Oncotarget

    Article Title: JNJ-26481585 primes rhabdomyosarcoma cells for chemotherapeutics by engaging the mitochondrial pathway of apoptosis

    doi:

    Figure Lengend Snippet: JNJ-26481585 and Doxorubicin cooperate to induce caspase activation and caspase-dependent apoptosis A. , Cells were treated with 15 nM JNJ-26481585 and/or 0.25 μg/ml Doxorubicin for indicated times. Cleavage of caspase-9, -8, -3 and PARP was assessed by Western blotting, GAPDH served as loading control. B. , Cells were treated for indicated times with 15 nM JNJ-26481585 and/or 0.25 μg/ml Doxorubicin. Apoptosis was determined by analysis of DNA fragmentation of PI-stained nuclei using flow cytometry. Mean and SEM of at least three independent experiments carried out in triplicate are shown; ** P

    Article Snippet: Western blot analysis Western blot analysis was performed as described previously [ ] using the following antibodies: mouse anti-caspase-8, mouse anti-Noxa, rat anti-Bmf (Alexis Biochemicals, Grünberg, Germany), mouse anti-Bcl-2, rabbit anti-Bcl-xL , mouse anti-Bax, rabbit anti-Bak (BD Transduction Laboratories, Heidelberg, Germany), rabbit anti-caspase-3, rabbit anti-caspase-9, rabbit anti-Bim, mouse anti-PARP (Cell Signaling, Beverly, MA), acetylated histone H3 (Upstate Biotechnology, Lake Placid, NY), rabbit anti-Mcl-1 (Stressgene, Victoria, BC), rabbit histone H3 (Abcam, Cambridge, UK).

    Techniques: Activation Assay, Western Blot, Staining, Flow Cytometry, Cytometry

    Expression of proapoptotic proteins in the ischemic territory: poly-ADP ribose polymerase (PARP; A ) and cleaved PARP ( P = 0.1) ( B ); Bcl 2/adenovirus E1B 19-kDa interacting protein (BNip-3) ( P = 0.3; C ); apoptosis inducing factor (AIF;

    Journal: Journal of Applied Physiology

    Article Title: Effect of thrombin fragment (TP508) on myocardial ischemia-reperfusion injury in hypercholesterolemic pigs

    doi: 10.1152/japplphysiol.00071.2009

    Figure Lengend Snippet: Expression of proapoptotic proteins in the ischemic territory: poly-ADP ribose polymerase (PARP; A ) and cleaved PARP ( P = 0.1) ( B ); Bcl 2/adenovirus E1B 19-kDa interacting protein (BNip-3) ( P = 0.3; C ); apoptosis inducing factor (AIF;

    Article Snippet: Levels of B-cell lymphoma 2 (Bcl-2), caspase-3, cleaved caspase-3, phospho-caspase 9, poly-ADP ribose polymerase (PARP), cleaved PARP, Akt, phospho-Akt (Ser473 and Thr308), Bcl-2/adenovirus E1B 19-kDa interacting protein (BNip-3), apoptosis inducing factor (AIF), Bad, phospho-Bad (Ser112), endothelial nitric oxide synthase (eNOS), phospho-eNOS (Ser1177) (Cell Signaling Technology, Beverly, MA), 90-kDa heat shock protein (HSP90), HSP70 (or HSP72), HSC70 (heat shock cognate protein or HSP73), HSP27, and αB-crystallin (Stressgen, Ann Arbor, MI) were assessed.

    Techniques: Expressing

    Comparison of phosphorylation of H2AX and PAR accumulation in response to low and high-input-power damage in two NIR systems. ( A ) Time course analysis of γH2AX following 60 mW and 100 mW damage in the Mira-900 system. PtK2 cells were fixed at specific time points p.i. as indicated at the top. Scale bar = 10 μm. ( B ) Similar analysis as in ( A ) with 15% and 25% input laser using the Meta system. Scale bar = 10 μm. ( C ) Localization of GFP-NTH1 DNA glycosylase and γH2AX response to laser damage with the indicated input power (15% and 25%) in the Meta system. Left: live cell image of GFP-NTH1 at 3 min p.i. Right: γH2AX immunostaining of the same cells fixed at 10 min p.i. Scale bar = 10 μm. ( D ) Left: Immunofluorescent staining of PAR at low (60 mW) and high (100 mW) input power in the Mira-900 system at 1 min p.i. Right: time course analysis of PAR response at low (15%) and high (25%) input power in the Meta system. Time points p.i. are indicated at the top. Scale bar = 10 μm. ( E ) Immunofluorescent staining of PAR and PARP1 at low and high input power at 3 min p.i. Mira-900 system (left) and Meta system (right) with and without PARP inhibitor NU1025. Scale bar = 10 μm.

    Journal: Nucleic Acids Research

    Article Title: Femtosecond near-infrared laser microirradiation reveals a crucial role for PARP signaling on factor assemblies at DNA damage sites

    doi: 10.1093/nar/gkv976

    Figure Lengend Snippet: Comparison of phosphorylation of H2AX and PAR accumulation in response to low and high-input-power damage in two NIR systems. ( A ) Time course analysis of γH2AX following 60 mW and 100 mW damage in the Mira-900 system. PtK2 cells were fixed at specific time points p.i. as indicated at the top. Scale bar = 10 μm. ( B ) Similar analysis as in ( A ) with 15% and 25% input laser using the Meta system. Scale bar = 10 μm. ( C ) Localization of GFP-NTH1 DNA glycosylase and γH2AX response to laser damage with the indicated input power (15% and 25%) in the Meta system. Left: live cell image of GFP-NTH1 at 3 min p.i. Right: γH2AX immunostaining of the same cells fixed at 10 min p.i. Scale bar = 10 μm. ( D ) Left: Immunofluorescent staining of PAR at low (60 mW) and high (100 mW) input power in the Mira-900 system at 1 min p.i. Right: time course analysis of PAR response at low (15%) and high (25%) input power in the Meta system. Time points p.i. are indicated at the top. Scale bar = 10 μm. ( E ) Immunofluorescent staining of PAR and PARP1 at low and high input power at 3 min p.i. Mira-900 system (left) and Meta system (right) with and without PARP inhibitor NU1025. Scale bar = 10 μm.

    Article Snippet: The following primary antibodies were used: mouse monoclonal antibodies specific for γH2AX (05–636, Millipore), PAR polymers (BML-SA216–0100, Enzo Life Sciences, Inc.), ubiquitin (Ub) (spa-205, StressGen), TRF2 (NB100–56506, Novus Biologicals), XRCC1 (GTX72311, Gene Tex, Inc.), ATM (GTX70103, Gene Tex, Inc.), DNA–PKcs (ab1832, Abcam), 53BP1 (MAB3802, Millipore), and cyclobutane pyrimidine dimer (CPD) (MC-062, Kamiya Biomedical Company) as well as rabbit polyclonal antibodies specific for γH2AX (07–164; Millipore), PAR (4336-BPC-100, Trevigen), XPA (GTX100112, Gene Tex, Inc.), CtIP (ab70163, Abcam), 53BP1 (sc-22760, Santa Cruz Biotech., Inc.), phosphor-Chk1 Ser-345 (2348, Cell Signaling), phosphor-Chk2 Thr-68 (2661, Cell Signaling) and MDC1 (NB100–395, Novus Biologicals).

    Techniques: Immunostaining, Staining

    Protein expression analysis in a panel of human breast cancer cell lines and effect of NVP-AUY922 on the HSP90-p23 complex in BT-474 cells. (a) The expression of HSP90 and specific proteins affected by HSP90 inhibition (Her3 [EGFR3], Her2 [ErbB2, EGFR2], phospho Her2 [pHer2], EGFR, AKT [PKB], phospho-AKT [pAkt], estrogen receptor-alpha [ERa], PI3K [p110α], PDK1, HSP70, Hsc70, Rb, pMEK1/2, pERK, Bax, Bcl-2, Bad, and Bcl-XL) was analyzed in seven human breast cancer cell lines (BT20, BT-474, MDA-MB-157 [MB-157], MDA-MB-231 [MB-231], MDA-MB-468 [MB-468], SKBr3, and MCF-7) by Western blot analysis. (b) The ERBB2-overexpressing and estrogen receptor-positive cell line BT-474 was chosen for studies of the kinetics and concentration-dependent dissociation of HSP90-p23 complexes and client proteins in the presence of NVP-AUY922 or tanespimycin (17-AAG). The amount of p23 associated with HSP90 was determined by immunoprecipitating p23 followed by immunoblotting for HSP90. The levels of ERBB2, AKT, phosphorylated AKT and β-tubulin were determined by immunoblotting. DMSO, dimethyl sulfoxide; HSP90, heat shock protein 90.

    Journal: Breast Cancer Research : BCR

    Article Title: NVP-AUY922: a small molecule HSP90 inhibitor with potent antitumor activity in preclinical breast cancer models

    doi: 10.1186/bcr1996

    Figure Lengend Snippet: Protein expression analysis in a panel of human breast cancer cell lines and effect of NVP-AUY922 on the HSP90-p23 complex in BT-474 cells. (a) The expression of HSP90 and specific proteins affected by HSP90 inhibition (Her3 [EGFR3], Her2 [ErbB2, EGFR2], phospho Her2 [pHer2], EGFR, AKT [PKB], phospho-AKT [pAkt], estrogen receptor-alpha [ERa], PI3K [p110α], PDK1, HSP70, Hsc70, Rb, pMEK1/2, pERK, Bax, Bcl-2, Bad, and Bcl-XL) was analyzed in seven human breast cancer cell lines (BT20, BT-474, MDA-MB-157 [MB-157], MDA-MB-231 [MB-231], MDA-MB-468 [MB-468], SKBr3, and MCF-7) by Western blot analysis. (b) The ERBB2-overexpressing and estrogen receptor-positive cell line BT-474 was chosen for studies of the kinetics and concentration-dependent dissociation of HSP90-p23 complexes and client proteins in the presence of NVP-AUY922 or tanespimycin (17-AAG). The amount of p23 associated with HSP90 was determined by immunoprecipitating p23 followed by immunoblotting for HSP90. The levels of ERBB2, AKT, phosphorylated AKT and β-tubulin were determined by immunoblotting. DMSO, dimethyl sulfoxide; HSP90, heat shock protein 90.

    Article Snippet: The following antibodies were used for immunoblotting: Her3 (sc-285; Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), Her2 (ab8054; Abcam, Cambridge, UK), phosphor-Her2 (Tyr1248) (44 & #8211900, Invitrogen Corporation, Carlsbad, CA, USA) EGFR (#2232; Cell Signaling Technology, Inc., Danvers, MA, USA), phosphor-Akt (Ser473) (#9271; Cell Signaling Technology, Inc.), Akt (#9272, Cell Signaling Technology, Inc.), ER-α (sc-542; Santa Cruz Biotechnology, Inc.), PI3K (p110α) (#4254; Cell Signaling Technology, Inc.), PDK1 (#3062; Cell Signaling Technology, Inc.), HSP70 (SPA-810; Stressgen Bioreagents, now part of Assay Designs, Inc., Ann Arbor, MI, USA), HSP90 (SPA-845; Assay Designs, Inc.), Hsc70 (sc-7298, Santa Cruz Biotechnology, Inc.), Rb (#9309; Cell Signaling Technology, Inc.), pMEK1/2 (#9121, Cell Signaling Technology, Inc.), pERK (#9101; Cell Signaling Technology, Inc.), Bax (#2772, Cell Signaling Technology, Inc.), Bcl-2 (sc-492; Santa Cruz Biotechnology, Inc.), Bad (#9292; Cell Signaling Technology, Inc.), Bad (#9292; Cell Signaling Technology, Inc.), and Bcl-XL (#2762; Cell Signaling Technology, Inc.).

    Techniques: Expressing, Inhibition, Multiple Displacement Amplification, Western Blot, Concentration Assay

    Analysis of the kinetics of HSP70 induction and ERBB2 degradation following a singe dose of NVP-AUY922. BT-474 tumor-bearing animals were administered 50 mg/kg NVP-AUY922 at 0 hours. (a) The protein levels of HSP70 were determined by immunohistochemistry during the following week. (b) The quantification of the protein levels of HSP70. (c) ERBB2 protein levels were determined by immunohistochemistry and Western blot analysis. (d) The lowest single dose of NVP-AUY922 which mediates HSP90-p23 dissociation and reduced AKT phosphorylation was determined by immunoprecipitation and Western blot analysis. HSP70, heat shock protein 70; HSP90, heat shock protein 90.

    Journal: Breast Cancer Research : BCR

    Article Title: NVP-AUY922: a small molecule HSP90 inhibitor with potent antitumor activity in preclinical breast cancer models

    doi: 10.1186/bcr1996

    Figure Lengend Snippet: Analysis of the kinetics of HSP70 induction and ERBB2 degradation following a singe dose of NVP-AUY922. BT-474 tumor-bearing animals were administered 50 mg/kg NVP-AUY922 at 0 hours. (a) The protein levels of HSP70 were determined by immunohistochemistry during the following week. (b) The quantification of the protein levels of HSP70. (c) ERBB2 protein levels were determined by immunohistochemistry and Western blot analysis. (d) The lowest single dose of NVP-AUY922 which mediates HSP90-p23 dissociation and reduced AKT phosphorylation was determined by immunoprecipitation and Western blot analysis. HSP70, heat shock protein 70; HSP90, heat shock protein 90.

    Article Snippet: The following antibodies were used for immunoblotting: Her3 (sc-285; Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), Her2 (ab8054; Abcam, Cambridge, UK), phosphor-Her2 (Tyr1248) (44 & #8211900, Invitrogen Corporation, Carlsbad, CA, USA) EGFR (#2232; Cell Signaling Technology, Inc., Danvers, MA, USA), phosphor-Akt (Ser473) (#9271; Cell Signaling Technology, Inc.), Akt (#9272, Cell Signaling Technology, Inc.), ER-α (sc-542; Santa Cruz Biotechnology, Inc.), PI3K (p110α) (#4254; Cell Signaling Technology, Inc.), PDK1 (#3062; Cell Signaling Technology, Inc.), HSP70 (SPA-810; Stressgen Bioreagents, now part of Assay Designs, Inc., Ann Arbor, MI, USA), HSP90 (SPA-845; Assay Designs, Inc.), Hsc70 (sc-7298, Santa Cruz Biotechnology, Inc.), Rb (#9309; Cell Signaling Technology, Inc.), pMEK1/2 (#9121, Cell Signaling Technology, Inc.), pERK (#9101; Cell Signaling Technology, Inc.), Bax (#2772, Cell Signaling Technology, Inc.), Bcl-2 (sc-492; Santa Cruz Biotechnology, Inc.), Bad (#9292; Cell Signaling Technology, Inc.), Bad (#9292; Cell Signaling Technology, Inc.), and Bcl-XL (#2762; Cell Signaling Technology, Inc.).

    Techniques: Immunohistochemistry, Western Blot, Immunoprecipitation