Structured Review

Santa Cruz Biotechnology anti cleaved caspase 3
BA improves HG-induced podocyte apoptosis. Following serum starvation for 12 h, podocytes were cultured with HG (30 mM D-glucose) or normal glucose (5 mM D-glucose) for 48 h and then treated with 6.25, 12.5 or 25 µM BA for 24 h. (A and B) Flow cytometry was used to determine the cell apoptotic rate. (C) Western blotting was performed to determine the protein expression levels of the apoptosis-associated proteins <t>pro-caspase-3</t> and cleaved caspase-3. (D) Semi-quantification of the ratio between cleaved-caspase-3/pro-caspase-3. All data are presented as the mean ± SD. ** P
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1) Product Images from "Baicalin serves a protective role in diabetic nephropathy through preventing high glucose-induced podocyte apoptosis"

Article Title: Baicalin serves a protective role in diabetic nephropathy through preventing high glucose-induced podocyte apoptosis

Journal: Experimental and Therapeutic Medicine

doi: 10.3892/etm.2020.8701

BA improves HG-induced podocyte apoptosis. Following serum starvation for 12 h, podocytes were cultured with HG (30 mM D-glucose) or normal glucose (5 mM D-glucose) for 48 h and then treated with 6.25, 12.5 or 25 µM BA for 24 h. (A and B) Flow cytometry was used to determine the cell apoptotic rate. (C) Western blotting was performed to determine the protein expression levels of the apoptosis-associated proteins pro-caspase-3 and cleaved caspase-3. (D) Semi-quantification of the ratio between cleaved-caspase-3/pro-caspase-3. All data are presented as the mean ± SD. ** P
Figure Legend Snippet: BA improves HG-induced podocyte apoptosis. Following serum starvation for 12 h, podocytes were cultured with HG (30 mM D-glucose) or normal glucose (5 mM D-glucose) for 48 h and then treated with 6.25, 12.5 or 25 µM BA for 24 h. (A and B) Flow cytometry was used to determine the cell apoptotic rate. (C) Western blotting was performed to determine the protein expression levels of the apoptosis-associated proteins pro-caspase-3 and cleaved caspase-3. (D) Semi-quantification of the ratio between cleaved-caspase-3/pro-caspase-3. All data are presented as the mean ± SD. ** P

Techniques Used: Cell Culture, Flow Cytometry, Western Blot, Expressing

BA promotes podocyte viability and decreases apoptosis. Podocytes were treated with 6.25, 12.5 or 25 µM BA for 24 h. (A) MTT assay was used to determine the cell viability. (B) Apoptotic rate of podocytes was analyzed using flow cytometry. (C) Cell apoptotic rate was calculated. (D) Western blotting was used to analyze the protein expression levels of pro-caspase-3 and cleaved caspase-3. (E) Semi-quantification of the ratio between cleaved caspase-3/pro-caspase-3. All data are presented as the mean ± SD. * P
Figure Legend Snippet: BA promotes podocyte viability and decreases apoptosis. Podocytes were treated with 6.25, 12.5 or 25 µM BA for 24 h. (A) MTT assay was used to determine the cell viability. (B) Apoptotic rate of podocytes was analyzed using flow cytometry. (C) Cell apoptotic rate was calculated. (D) Western blotting was used to analyze the protein expression levels of pro-caspase-3 and cleaved caspase-3. (E) Semi-quantification of the ratio between cleaved caspase-3/pro-caspase-3. All data are presented as the mean ± SD. * P

Techniques Used: MTT Assay, Flow Cytometry, Western Blot, Expressing

2) Product Images from "miR-128 induces pancreas cancer cell apoptosis by targeting MDM4"

Article Title: miR-128 induces pancreas cancer cell apoptosis by targeting MDM4

Journal: Experimental and Therapeutic Medicine

doi: 10.3892/etm.2018.6047

Expression of p53 is enhanced by miR-128 mimics via inhibition of MDM4 expression. (A) Western blot analysis of MDM4, p53 and cleaved caspase-3 expression following transfection with miR-128 mimics. (B) Quantification of MDM4 expression. (C) Quantification of p53 expression. (D) Quantification of cleaved caspase-3 expression. **P
Figure Legend Snippet: Expression of p53 is enhanced by miR-128 mimics via inhibition of MDM4 expression. (A) Western blot analysis of MDM4, p53 and cleaved caspase-3 expression following transfection with miR-128 mimics. (B) Quantification of MDM4 expression. (C) Quantification of p53 expression. (D) Quantification of cleaved caspase-3 expression. **P

Techniques Used: Expressing, Inhibition, Western Blot, Transfection

3) Product Images from "Episode-like pulse testosterone supplementation induces tumor senescence and growth arrest down-modulating androgen receptor through modulation of p-ERK1/2, pARser81 and CDK1 signaling: biological implications for men treated with testosterone replacement therapy"

Article Title: Episode-like pulse testosterone supplementation induces tumor senescence and growth arrest down-modulating androgen receptor through modulation of p-ERK1/2, pARser81 and CDK1 signaling: biological implications for men treated with testosterone replacement therapy

Journal: Oncotarget

doi: 10.18632/oncotarget.22776

Percentage of live (Annexin V negative/PI negative cells), apoptotic (AnnexinV positive/PI negative cells) and dead (AnnexinV positive/PI positive cells or AnnexinV negative/PI positive cells) cells in LnCaP (A) and CW22rv1 (B) cell populations treated with continuous or pulsed Testosterone for 48 hours. The bars show the mean and SD of 36 replicates. Student-Newman-Keuls test for all pairwise comparisons in CW22rv1 and LnCaP cells at 48 hours after treatments. Expression levels, by western blot analysis, of pro-caspase-3 and cleaved caspase3 in LnCaP (C) and CW22rv1 (D) tumor cells tumor cells treated with continuous or pulsed Testosterone for 48 hours.
Figure Legend Snippet: Percentage of live (Annexin V negative/PI negative cells), apoptotic (AnnexinV positive/PI negative cells) and dead (AnnexinV positive/PI positive cells or AnnexinV negative/PI positive cells) cells in LnCaP (A) and CW22rv1 (B) cell populations treated with continuous or pulsed Testosterone for 48 hours. The bars show the mean and SD of 36 replicates. Student-Newman-Keuls test for all pairwise comparisons in CW22rv1 and LnCaP cells at 48 hours after treatments. Expression levels, by western blot analysis, of pro-caspase-3 and cleaved caspase3 in LnCaP (C) and CW22rv1 (D) tumor cells tumor cells treated with continuous or pulsed Testosterone for 48 hours.

Techniques Used: Expressing, Western Blot

4) Product Images from "The Novel miR-9600 Suppresses Tumor Progression and Promotes Paclitaxel Sensitivity in Non–small-cell Lung Cancer Through Altering STAT3 Expression"

Article Title: The Novel miR-9600 Suppresses Tumor Progression and Promotes Paclitaxel Sensitivity in Non–small-cell Lung Cancer Through Altering STAT3 Expression

Journal: Molecular Therapy. Nucleic Acids

doi: 10.1038/mtna.2016.96

Ectopic expression of miR-9600 promotes apoptosis in A549 and SPC-A-1 cells . ( a ) Shown are statistical analysis of flow cytometric analysis. ( b,c ). Quantitative representation of caspase-3 and caspase-7 activity in A549 and SPC-A-1 cells transfected with NC, miR-9600, si-STAT3, and ASO-9600 for 48 hours. ( d–l ) Western-blot of Bcl2, Mcl-1, Bcl-xL, caspase-3, cleaved-caspase-3, caspase-7, and cleaved-caspase-7 protein in A549 and SPC-A-1 cells after transfection. Assays were performed in triplicate. * P
Figure Legend Snippet: Ectopic expression of miR-9600 promotes apoptosis in A549 and SPC-A-1 cells . ( a ) Shown are statistical analysis of flow cytometric analysis. ( b,c ). Quantitative representation of caspase-3 and caspase-7 activity in A549 and SPC-A-1 cells transfected with NC, miR-9600, si-STAT3, and ASO-9600 for 48 hours. ( d–l ) Western-blot of Bcl2, Mcl-1, Bcl-xL, caspase-3, cleaved-caspase-3, caspase-7, and cleaved-caspase-7 protein in A549 and SPC-A-1 cells after transfection. Assays were performed in triplicate. * P

Techniques Used: Expressing, Flow Cytometry, Activity Assay, Transfection, Allele-specific Oligonucleotide, Western Blot

5) Product Images from "Curcumin inhibits the replication of enterovirus 71 in vitro"

Article Title: Curcumin inhibits the replication of enterovirus 71 in vitro

Journal: Acta Pharmaceutica Sinica. B

doi: 10.1016/j.apsb.2014.06.006

Curcumin suppresses apoptosis induced by EV71 infection. (A) Vero cells were infected with EV71 and grown in the medium containing curcumin for 8 h. Cells were stained with Hoechst33342 to view the nuclei. (B) Cells were infected with EV71 for 8 h and curcumin was added to the culture medium at 1 h after p.i. PARP-1, cleaved caspase 3 and VP1 were determined by western blotting. Cells treated with DMSO were used as controls. (C) Cells were infected with EV71 for 8 h. Curcumin was added to the culture medium at various time points after p.i. PARP-1, cleaved caspase 3 and VP1 were determined by western blotting. Results are representative of three independent infection experiments.
Figure Legend Snippet: Curcumin suppresses apoptosis induced by EV71 infection. (A) Vero cells were infected with EV71 and grown in the medium containing curcumin for 8 h. Cells were stained with Hoechst33342 to view the nuclei. (B) Cells were infected with EV71 for 8 h and curcumin was added to the culture medium at 1 h after p.i. PARP-1, cleaved caspase 3 and VP1 were determined by western blotting. Cells treated with DMSO were used as controls. (C) Cells were infected with EV71 for 8 h. Curcumin was added to the culture medium at various time points after p.i. PARP-1, cleaved caspase 3 and VP1 were determined by western blotting. Results are representative of three independent infection experiments.

Techniques Used: Infection, Staining, Western Blot

6) Product Images from "Resveratrol attenuates constitutive STAT3 and STAT5 activation through induction of PTPε and SHP-2 tyrosine phosphatases and potentiates sorafenib-induced apoptosis in renal cell carcinoma"

Article Title: Resveratrol attenuates constitutive STAT3 and STAT5 activation through induction of PTPε and SHP-2 tyrosine phosphatases and potentiates sorafenib-induced apoptosis in renal cell carcinoma

Journal: BMC Nephrology

doi: 10.1186/s12882-016-0233-7

RES suppresses expression of various proteins involved in anti-apoptosis, proliferation, and angiogenesis. a - d After Caki-1 and 786-O cells (1 × 10 6 cells/well) were incubated with the indicated various concentrations of RES for 24 h. Whole-cell extracts were prepared, and 20 μg of the whole-cell lysate was resolved by SDS-PAGE, electrotransferred to nitrocellulose membrane, and then probed with antibodies against bcl-2, bcl-xL, survivin, IAP1/2, COX-2, VEGF, MMP-9, caspase-3, PARP, cyclin D1, cyclin E, p21, Bax, and p53 as described in “Materials and methods.” The same blots were stripped and reprobed with β-actin antibody to verify equal protein loading. The results shown here are representative of three independent experiments. e Cell proliferation assay was performed using the Roche xCELLigence Real-Time Cell Analyzer (RTCA) DP instrument (Roche Diagnostics GmbH, Germany) as described in “Material and methods”. After Caki-1 and 786-O cells (5 × 10 3 cells/well) were seeded onto 16-well E-plates and continuously monitored using impedance technology. f Caki-1 and 786-O cells were added to the upper side of the invasion chamber, the cells on the upper surface of the filter were removed after 24 h of incubation in the presence or absence of 10 μM of RES. The cells on the lower surface were fixed, stained and monitored by photographing, then counted. Randomly chosen fields were photographed under a light microscope at 100× magnification and invaded cells were counted
Figure Legend Snippet: RES suppresses expression of various proteins involved in anti-apoptosis, proliferation, and angiogenesis. a - d After Caki-1 and 786-O cells (1 × 10 6 cells/well) were incubated with the indicated various concentrations of RES for 24 h. Whole-cell extracts were prepared, and 20 μg of the whole-cell lysate was resolved by SDS-PAGE, electrotransferred to nitrocellulose membrane, and then probed with antibodies against bcl-2, bcl-xL, survivin, IAP1/2, COX-2, VEGF, MMP-9, caspase-3, PARP, cyclin D1, cyclin E, p21, Bax, and p53 as described in “Materials and methods.” The same blots were stripped and reprobed with β-actin antibody to verify equal protein loading. The results shown here are representative of three independent experiments. e Cell proliferation assay was performed using the Roche xCELLigence Real-Time Cell Analyzer (RTCA) DP instrument (Roche Diagnostics GmbH, Germany) as described in “Material and methods”. After Caki-1 and 786-O cells (5 × 10 3 cells/well) were seeded onto 16-well E-plates and continuously monitored using impedance technology. f Caki-1 and 786-O cells were added to the upper side of the invasion chamber, the cells on the upper surface of the filter were removed after 24 h of incubation in the presence or absence of 10 μM of RES. The cells on the lower surface were fixed, stained and monitored by photographing, then counted. Randomly chosen fields were photographed under a light microscope at 100× magnification and invaded cells were counted

Techniques Used: Expressing, Incubation, SDS Page, Proliferation Assay, Staining, Light Microscopy

RES potentiates the cytotoxic and apoptotic effects of sorafenib in renal cell carcinoma. a and b Caki-1 and 786-O cells (5× 10 3 cells/well) were treated with indicated concentration of RES, and sorafenib for 24 h. The cytotoxicity was determined by MTT assays ( left panel ). The combination index (CI) values were obtained using BiosoftCalcuSyn software (Biosoft, Cambridge, UK) ( right panel ). c Caki-1 and 786-O cells (1 × 10 6 cells/well) were treated with indicated concentration of RES, and sorafenibfor6h. After which whole-cell extracts were prepared and 15 μg portions of those extracts were resolved on 8 % SDS-PAGE gel, electrotransferred onto nitrocellulose membranes, and probed against p-STAT3(Tyr705), p-STAT3(Ser727), STAT3, p-STAT5(Tyr694/699), and STAT5. The results shown here are representative of three independent experiments. d and e Caki-1 and 786-O cells (1 × 10 6 cells/well) were treated with indicated concentration of RES, and sorafenibfor24h. Whole-cell extracts were prepared, and 20 μg of the whole-cell lysate was resolved by SDS-PAGE, electrotransferred to nitrocellulose membrane, and then probed with antibodies against bcl-2, bcl-xL, survivin, caspase-3, and PARP. The same blots were stripped and reprobed with β-actin antibody to verify equal protein loading
Figure Legend Snippet: RES potentiates the cytotoxic and apoptotic effects of sorafenib in renal cell carcinoma. a and b Caki-1 and 786-O cells (5× 10 3 cells/well) were treated with indicated concentration of RES, and sorafenib for 24 h. The cytotoxicity was determined by MTT assays ( left panel ). The combination index (CI) values were obtained using BiosoftCalcuSyn software (Biosoft, Cambridge, UK) ( right panel ). c Caki-1 and 786-O cells (1 × 10 6 cells/well) were treated with indicated concentration of RES, and sorafenibfor6h. After which whole-cell extracts were prepared and 15 μg portions of those extracts were resolved on 8 % SDS-PAGE gel, electrotransferred onto nitrocellulose membranes, and probed against p-STAT3(Tyr705), p-STAT3(Ser727), STAT3, p-STAT5(Tyr694/699), and STAT5. The results shown here are representative of three independent experiments. d and e Caki-1 and 786-O cells (1 × 10 6 cells/well) were treated with indicated concentration of RES, and sorafenibfor24h. Whole-cell extracts were prepared, and 20 μg of the whole-cell lysate was resolved by SDS-PAGE, electrotransferred to nitrocellulose membrane, and then probed with antibodies against bcl-2, bcl-xL, survivin, caspase-3, and PARP. The same blots were stripped and reprobed with β-actin antibody to verify equal protein loading

Techniques Used: Concentration Assay, MTT Assay, Software, SDS Page

7) Product Images from "CREB Negatively Regulates IGF2R Gene Expression and Downstream Pathways to Inhibit Hypoxia-Induced H9c2 Cardiomyoblast Cell Death"

Article Title: CREB Negatively Regulates IGF2R Gene Expression and Downstream Pathways to Inhibit Hypoxia-Induced H9c2 Cardiomyoblast Cell Death

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms161126067

Hypoxia-induced apoptosis was blocked by transfection with CREB in H9c2 cells. ( A ) The effects of hypoxia on the protein levels of CREB, HIF1α, IGF2R, caspase-3, p-AKT and Bcl-2, as detected by Western blot; and ( B ) CREB over-expression further reduced HIF1α, IGF2R, and caspase-3 protein expression levels to inhibit hypoxia-induced apoptosis in H9c2 cells. After being transfected with CREB plasmid for 24 h, H9c2 cells were treated with hypoxia for 24 h. Hypoxia-induced apoptosis-related proteins were measured by Western blot.
Figure Legend Snippet: Hypoxia-induced apoptosis was blocked by transfection with CREB in H9c2 cells. ( A ) The effects of hypoxia on the protein levels of CREB, HIF1α, IGF2R, caspase-3, p-AKT and Bcl-2, as detected by Western blot; and ( B ) CREB over-expression further reduced HIF1α, IGF2R, and caspase-3 protein expression levels to inhibit hypoxia-induced apoptosis in H9c2 cells. After being transfected with CREB plasmid for 24 h, H9c2 cells were treated with hypoxia for 24 h. Hypoxia-induced apoptosis-related proteins were measured by Western blot.

Techniques Used: Transfection, Western Blot, Over Expression, Expressing, Plasmid Preparation

8) Product Images from "The polyamidoamine-mediated inhibition of bcl-2 by small hairpin RNA to induce apoptosis in human lens epithelial cells"

Article Title: The polyamidoamine-mediated inhibition of bcl-2 by small hairpin RNA to induce apoptosis in human lens epithelial cells

Journal: Molecular Vision

doi:

Western blot analysis of cytochrome c and cleaved caspase-3 protein. At 48 h after transfection, the cells were harvested and processed for western blotting. β-Actin was used as the internal control. The immunoblot was a representative of three independent experiments. The expression of cytochrome c and the activity of cleaved caspase-3 were greatly improved (p
Figure Legend Snippet: Western blot analysis of cytochrome c and cleaved caspase-3 protein. At 48 h after transfection, the cells were harvested and processed for western blotting. β-Actin was used as the internal control. The immunoblot was a representative of three independent experiments. The expression of cytochrome c and the activity of cleaved caspase-3 were greatly improved (p

Techniques Used: Western Blot, Transfection, Expressing, Activity Assay

9) Product Images from "PQ1, a Quinoline Derivative, Induces Apoptosis in T47D Breast Cancer Cells through Activation of Caspase-8 and Caspase-9"

Article Title: PQ1, a Quinoline Derivative, Induces Apoptosis in T47D Breast Cancer Cells through Activation of Caspase-8 and Caspase-9

Journal: Apoptosis : an international journal on programmed cell death

doi: 10.1007/s10495-013-0855-1

Effects of caspase inhibitors on the cytotoxicity of PQ1 T47D cells were pre-treated with 20 μM caspase-3 inhibitor (Ac-DMQD-CHO), caspase-8 inhibitor (Ac-IETD-CHO), or caspase-9 inhibitor (Ac-LEHD-CHO) for 1 hour, and exposed to 500 nM PQ1 for 23 hours. Cells without treatments and cells treated with 500 nM PQ1 for 24 hours were used as controls. Cell viability was determined by trypan blue method. Data were obtained in three independent experiments and are represented as the mean ± S.D. * P-value is
Figure Legend Snippet: Effects of caspase inhibitors on the cytotoxicity of PQ1 T47D cells were pre-treated with 20 μM caspase-3 inhibitor (Ac-DMQD-CHO), caspase-8 inhibitor (Ac-IETD-CHO), or caspase-9 inhibitor (Ac-LEHD-CHO) for 1 hour, and exposed to 500 nM PQ1 for 23 hours. Cells without treatments and cells treated with 500 nM PQ1 for 24 hours were used as controls. Cell viability was determined by trypan blue method. Data were obtained in three independent experiments and are represented as the mean ± S.D. * P-value is

Techniques Used:

PQ1 activates caspase-3 in T47D breast cancer cells T47D cells were treated with DMSO and various concentrations of PQ1 for 48 hours. Cells without treatments were used as controls. Expression of cleaved caspase-3 was determined by confocal microscopic analysis using immunofluorescence staining. Red indicates cleaved caspase-3 and blue indicates nuclei stained by DAPI. Percentages of cells with positive staining were labeled on the right of images.
Figure Legend Snippet: PQ1 activates caspase-3 in T47D breast cancer cells T47D cells were treated with DMSO and various concentrations of PQ1 for 48 hours. Cells without treatments were used as controls. Expression of cleaved caspase-3 was determined by confocal microscopic analysis using immunofluorescence staining. Red indicates cleaved caspase-3 and blue indicates nuclei stained by DAPI. Percentages of cells with positive staining were labeled on the right of images.

Techniques Used: Expressing, Immunofluorescence, Staining, Labeling

10) Product Images from "Beauvericin Ameliorates Experimental Colitis by Inhibiting Activated T Cells via Downregulation of the PI3K/Akt Signaling Pathway"

Article Title: Beauvericin Ameliorates Experimental Colitis by Inhibiting Activated T Cells via Downregulation of the PI3K/Akt Signaling Pathway

Journal: PLoS ONE

doi: 10.1371/journal.pone.0083013

Effects of beauvericin on caspase-dependent apoptosis in Con A-activated T cells. Cells were seeded in 6-well plates and incubated with 1.25–10 µM beauvericin for 24 h in the presence of 5 µg/mL ConA. (A) Apoptosis was determined by Annexin V/PI staining. (B) Annexin V + /PI −  and Annexin V + /PI +  cells from 3 independent experiments are shown in columns. Representative western blot bands (C) and data summary (D) for cleaved caspase 3, 9, 12, PARP and Bcl-2/Bad in activated T cells after treatment with 1.25–10 µM beauvericin for 24 h. Data are expressed as a histogram of mean ± SEM of 3 independent experiments. * P
Figure Legend Snippet: Effects of beauvericin on caspase-dependent apoptosis in Con A-activated T cells. Cells were seeded in 6-well plates and incubated with 1.25–10 µM beauvericin for 24 h in the presence of 5 µg/mL ConA. (A) Apoptosis was determined by Annexin V/PI staining. (B) Annexin V + /PI − and Annexin V + /PI + cells from 3 independent experiments are shown in columns. Representative western blot bands (C) and data summary (D) for cleaved caspase 3, 9, 12, PARP and Bcl-2/Bad in activated T cells after treatment with 1.25–10 µM beauvericin for 24 h. Data are expressed as a histogram of mean ± SEM of 3 independent experiments. * P

Techniques Used: Incubation, Staining, Western Blot

11) Product Images from "Luteolin improves cardiac dysfunction in heart failure rats by regulating sarcoplasmic reticulum Ca2+-ATPase 2a"

Article Title: Luteolin improves cardiac dysfunction in heart failure rats by regulating sarcoplasmic reticulum Ca2+-ATPase 2a

Journal: Scientific Reports

doi: 10.1038/srep41017

Expression of apoptosis related protein in myocardium in vivo . Expression of Bcl-2, Bax, caspase-3, cleaved-caspase-3 in myocardium. n = 3 independent experiment. Results were normalized to β-actin. Data are expressed as mean ± SEM. *** p
Figure Legend Snippet: Expression of apoptosis related protein in myocardium in vivo . Expression of Bcl-2, Bax, caspase-3, cleaved-caspase-3 in myocardium. n = 3 independent experiment. Results were normalized to β-actin. Data are expressed as mean ± SEM. *** p

Techniques Used: Expressing, In Vivo

12) Product Images from "Holotoxin A1 Induces Apoptosis by Activating Acid Sphingomyelinase and Neutral Sphingomyelinase in K562 and Human Primary Leukemia Cells"

Article Title: Holotoxin A1 Induces Apoptosis by Activating Acid Sphingomyelinase and Neutral Sphingomyelinase in K562 and Human Primary Leukemia Cells

Journal: Marine Drugs

doi: 10.3390/md16040123

Holotoxin A 1 induces apoptosis through extrinsic pathway activation in human leukemic cells. ( A ) Analysis of the mechanism underlying apoptosis. Western blot of K562 cell proteins after treating cells with 0.06 μM holotoxin A 1 shows changes in protein levels over time. β-actin served as a loading control. This blot is representative of three separate experiments. Densitometry values above the bands indicate the fractional changes in protein levels, compared to initial levels at time 0; ( B ) Functional involvement of caspases in holotoxin A 1 -induced apoptosis in K562 cells. Cells were pretreated for 1 h with the pan-caspase inhibitor Z-VAD-FMK (25 μM), the caspase-8 inhibitor Z-IETD-FMK (20 μM), the caspase-9 inhibitor Z-LEHD-FMK (20 μM), or the caspase-3 inhibitor Z-DEVD-FMK (50 μM), followed by treatment with 0.06 μM holotoxin A 1 for 6 h. (Upper panel) Representative flow cytometry results indicate the extent of apoptosis (Lower panel) The mean ± SD of three independent experiments. ** p
Figure Legend Snippet: Holotoxin A 1 induces apoptosis through extrinsic pathway activation in human leukemic cells. ( A ) Analysis of the mechanism underlying apoptosis. Western blot of K562 cell proteins after treating cells with 0.06 μM holotoxin A 1 shows changes in protein levels over time. β-actin served as a loading control. This blot is representative of three separate experiments. Densitometry values above the bands indicate the fractional changes in protein levels, compared to initial levels at time 0; ( B ) Functional involvement of caspases in holotoxin A 1 -induced apoptosis in K562 cells. Cells were pretreated for 1 h with the pan-caspase inhibitor Z-VAD-FMK (25 μM), the caspase-8 inhibitor Z-IETD-FMK (20 μM), the caspase-9 inhibitor Z-LEHD-FMK (20 μM), or the caspase-3 inhibitor Z-DEVD-FMK (50 μM), followed by treatment with 0.06 μM holotoxin A 1 for 6 h. (Upper panel) Representative flow cytometry results indicate the extent of apoptosis (Lower panel) The mean ± SD of three independent experiments. ** p

Techniques Used: Activation Assay, Western Blot, Functional Assay, Flow Cytometry, Cytometry

13) Product Images from "bFGF attenuates endoplasmic reticulum stress and mitochondrial injury on myocardial ischaemia/reperfusion via activation of PI3K/Akt/ERK1/2 pathway"

Article Title: bFGF attenuates endoplasmic reticulum stress and mitochondrial injury on myocardial ischaemia/reperfusion via activation of PI3K/Akt/ERK1/2 pathway

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.12346

Basic fibroblast growth factor (bFGF) reduces myocardial apoptosis and the caspase cascade pathway in the hearts of mice after myocardial ischaemia/reperfusion. (A) Representative terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (TUNEL) immunofluorescence of sections from the ischaemic area in the hearts of mice that received bFGF or vehicle. (B) The detection of endoplasmic reticulum (ER) stress-related and mitochondrial dysfunction-related apoptosis proteins was performed by western blotting. The protein expression levels of cleaved-PARP, caspase-3, caspase-9 and caspase-12 in the hearts of control, ischaemia/reperfusion (I/R) mice and I/R mice treated with bFGF. (C) The optical density analysis of cleaved-PARP, caspase-3, caspase-9 and caspase-12 in the heart. (D) The percentage of apoptosis was counted from three random 1 mm 2 areas. * P
Figure Legend Snippet: Basic fibroblast growth factor (bFGF) reduces myocardial apoptosis and the caspase cascade pathway in the hearts of mice after myocardial ischaemia/reperfusion. (A) Representative terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (TUNEL) immunofluorescence of sections from the ischaemic area in the hearts of mice that received bFGF or vehicle. (B) The detection of endoplasmic reticulum (ER) stress-related and mitochondrial dysfunction-related apoptosis proteins was performed by western blotting. The protein expression levels of cleaved-PARP, caspase-3, caspase-9 and caspase-12 in the hearts of control, ischaemia/reperfusion (I/R) mice and I/R mice treated with bFGF. (C) The optical density analysis of cleaved-PARP, caspase-3, caspase-9 and caspase-12 in the heart. (D) The percentage of apoptosis was counted from three random 1 mm 2 areas. * P

Techniques Used: Mouse Assay, TUNEL Assay, Immunofluorescence, Western Blot, Expressing

14) Product Images from "Effects of hydrogen-rich saline on early acute kidney injury in severely burned rats by suppressing oxidative stress induced apoptosis and inflammation"

Article Title: Effects of hydrogen-rich saline on early acute kidney injury in severely burned rats by suppressing oxidative stress induced apoptosis and inflammation

Journal: Journal of Translational Medicine

doi: 10.1186/s12967-015-0548-3

Analysis of apoptosis in renal tissues post burn. TUNEL staining revealed increased numbers of apoptotic cells at 6, 24, and 72 h post burn, whereas corresponding reductions in the time-paired groups were observed with the regular administration of HS ( a ) (vs Sham, magnification ×200). The quantitative assessment of the numbers of apoptotic cells is shown ( b ). In addition, cleaved caspase-3 protein expression, as a marker of apoptotic activation, revealed significant gradual elevations over time, and HS markedly down-regulated cleaved caspase-3 expression ( c – f ). The sample size was n = 5 for TUNEL staining and n = 6 for Western blotting for each group. The results were expressed as the means ± SEMs. **p
Figure Legend Snippet: Analysis of apoptosis in renal tissues post burn. TUNEL staining revealed increased numbers of apoptotic cells at 6, 24, and 72 h post burn, whereas corresponding reductions in the time-paired groups were observed with the regular administration of HS ( a ) (vs Sham, magnification ×200). The quantitative assessment of the numbers of apoptotic cells is shown ( b ). In addition, cleaved caspase-3 protein expression, as a marker of apoptotic activation, revealed significant gradual elevations over time, and HS markedly down-regulated cleaved caspase-3 expression ( c – f ). The sample size was n = 5 for TUNEL staining and n = 6 for Western blotting for each group. The results were expressed as the means ± SEMs. **p

Techniques Used: TUNEL Assay, Staining, Expressing, Marker, Activation Assay, Western Blot

15) Product Images from "Dicumarol inhibits PDK1 and targets multiple malignant behaviors of ovarian cancer cells"

Article Title: Dicumarol inhibits PDK1 and targets multiple malignant behaviors of ovarian cancer cells

Journal: PLoS ONE

doi: 10.1371/journal.pone.0179672

DIC inhibits cell viability and induces apoptosis in A2780 cells. (A) A2780 cells were treated with increasing concentrations of DIC for 24 h, and cell viability was measured by the MTT assay. (B) After the indicated treatments for 24 h, A2780 cells were stained with annexin V and PI, and analyzed by flow cytometry. (C) The quantification of annexin V + PI + apoptotic cells. (D) Upon treatment, the protein levels of caspase-3, cleaved caspase-3, PARP, and cleaved PARP in A2780 cells were examined by western blot, with representative western blot images presented on the left and the quantitation of protein expression relative to β-actin (internal control) presented on the right. Data are presented as the mean ± SE from three independent experiments, *P
Figure Legend Snippet: DIC inhibits cell viability and induces apoptosis in A2780 cells. (A) A2780 cells were treated with increasing concentrations of DIC for 24 h, and cell viability was measured by the MTT assay. (B) After the indicated treatments for 24 h, A2780 cells were stained with annexin V and PI, and analyzed by flow cytometry. (C) The quantification of annexin V + PI + apoptotic cells. (D) Upon treatment, the protein levels of caspase-3, cleaved caspase-3, PARP, and cleaved PARP in A2780 cells were examined by western blot, with representative western blot images presented on the left and the quantitation of protein expression relative to β-actin (internal control) presented on the right. Data are presented as the mean ± SE from three independent experiments, *P

Techniques Used: MTT Assay, Staining, Flow Cytometry, Cytometry, Western Blot, Quantitation Assay, Expressing

DIC suppresses tumor growth in vivo . SKOV3 xenografts were established in nude mice, and the mice were treated as indicated. (A) The body weights of mice from all groups were monitored during the 12-day treatment period. (B) The tumor volume and tumor weight were measured at the indicated time points during treatment and at the time of sacrifice, respectively. (C) The protein levels of PDK1, PDHA1, and p-PDHA1 were examined by western immunoblotting, with β-actin examined as the internal control. Representative western blot images are shown on the left, and the quantification of protein levels relative to β-actin are shown on the right. (D) The protein levels of caspase-3, cleaved caspase-3, PARP, and cleaved-PARP in the SKOV3 xenografts were examined by western immunoblotting. Representative western blot images are shown on the left, and the quantification of protein levels relative to β-actin are shown on the right. Data are presented as the mean ± SE for all mice in each group. *P
Figure Legend Snippet: DIC suppresses tumor growth in vivo . SKOV3 xenografts were established in nude mice, and the mice were treated as indicated. (A) The body weights of mice from all groups were monitored during the 12-day treatment period. (B) The tumor volume and tumor weight were measured at the indicated time points during treatment and at the time of sacrifice, respectively. (C) The protein levels of PDK1, PDHA1, and p-PDHA1 were examined by western immunoblotting, with β-actin examined as the internal control. Representative western blot images are shown on the left, and the quantification of protein levels relative to β-actin are shown on the right. (D) The protein levels of caspase-3, cleaved caspase-3, PARP, and cleaved-PARP in the SKOV3 xenografts were examined by western immunoblotting. Representative western blot images are shown on the left, and the quantification of protein levels relative to β-actin are shown on the right. Data are presented as the mean ± SE for all mice in each group. *P

Techniques Used: In Vivo, Mouse Assay, Western Blot

DIC inhibits cell viability and induces apoptosis in SKOV3 cells. (A) SKOV3 cells were treated with increasing concentrations of DIC for 24 h, and cell viability was measured by the MTT assay. (B) After the indicated treatments for 24 h, SKOV3 cells were stained with Hoechst 33342 and imaged by confocal microscopy (scale bar, 50 μm; arrows, Hoechst-positive apoptotic cells). (C) Cells were treated as indicated for 24 h, stained with annexin V and PI, and analyzed by flow cytometry. Representative flow cytometry images are shown on the left, and the quantification of annexin V + PI + apoptotic cells is shown on the right. (D) Upon treatment, the protein levels of caspase-3, cleaved caspase-3, PARP, and cleaved PARP in SKOV3 cells were examined by western blot, with representative western blot images presented on the left and the quantitation of protein expression relative to β-actin (internal control) presented on the right. Data are presented as the mean ± SE from three independent experiments, *P
Figure Legend Snippet: DIC inhibits cell viability and induces apoptosis in SKOV3 cells. (A) SKOV3 cells were treated with increasing concentrations of DIC for 24 h, and cell viability was measured by the MTT assay. (B) After the indicated treatments for 24 h, SKOV3 cells were stained with Hoechst 33342 and imaged by confocal microscopy (scale bar, 50 μm; arrows, Hoechst-positive apoptotic cells). (C) Cells were treated as indicated for 24 h, stained with annexin V and PI, and analyzed by flow cytometry. Representative flow cytometry images are shown on the left, and the quantification of annexin V + PI + apoptotic cells is shown on the right. (D) Upon treatment, the protein levels of caspase-3, cleaved caspase-3, PARP, and cleaved PARP in SKOV3 cells were examined by western blot, with representative western blot images presented on the left and the quantitation of protein expression relative to β-actin (internal control) presented on the right. Data are presented as the mean ± SE from three independent experiments, *P

Techniques Used: MTT Assay, Staining, Confocal Microscopy, Flow Cytometry, Cytometry, Western Blot, Quantitation Assay, Expressing

16) Product Images from "Processing of Kansui Roots Stir-Baked with Vinegar Reduces Kansui-Induced Hepatocyte Cytotoxicity by Decreasing the Contents of Toxic Terpenoids and Regulating the Cell Apoptosis Pathway"

Article Title: Processing of Kansui Roots Stir-Baked with Vinegar Reduces Kansui-Induced Hepatocyte Cytotoxicity by Decreasing the Contents of Toxic Terpenoids and Regulating the Cell Apoptosis Pathway

Journal: Molecules

doi: 10.3390/molecules19067237

The expression of cleaved-caspase-3 and cleaved-caspase-9 protein in LO2 cells detected by western blotting ( A , B ) and the activation of caspase-3 ( C ) and caspase-9 ( D ) were assayed by Elisa according to the manufacturer’s instructions. Values expressed as mean ± SD from three independent experiments, * p
Figure Legend Snippet: The expression of cleaved-caspase-3 and cleaved-caspase-9 protein in LO2 cells detected by western blotting ( A , B ) and the activation of caspase-3 ( C ) and caspase-9 ( D ) were assayed by Elisa according to the manufacturer’s instructions. Values expressed as mean ± SD from three independent experiments, * p

Techniques Used: Expressing, Western Blot, Activation Assay, Enzyme-linked Immunosorbent Assay

17) Product Images from "Sevoflurane post-conditioning protects isolated rat hearts against ischemia-reperfusion injury via activation of the ERK1/2 pathway"

Article Title: Sevoflurane post-conditioning protects isolated rat hearts against ischemia-reperfusion injury via activation of the ERK1/2 pathway

Journal: Acta Pharmacologica Sinica

doi: 10.1038/aps.2014.78

Western blot of cleaved caspase-3 (A) and caspase-8 (B) from left ventricular samples were acquired at the end of reperfusion. Compared with the CON group, the expression of cleaved caspase-3 and caspase-8 in the other groups significantly increased. Compared with the I/R groups, the expression of cleaved caspase-3 and caspase-8 in the SEVO group decreased. There were no obvious differences between levels in the I/R, DMSO, PD, PD+SEVO groups. Data are presented as mean±SD. n =3. b P
Figure Legend Snippet: Western blot of cleaved caspase-3 (A) and caspase-8 (B) from left ventricular samples were acquired at the end of reperfusion. Compared with the CON group, the expression of cleaved caspase-3 and caspase-8 in the other groups significantly increased. Compared with the I/R groups, the expression of cleaved caspase-3 and caspase-8 in the SEVO group decreased. There were no obvious differences between levels in the I/R, DMSO, PD, PD+SEVO groups. Data are presented as mean±SD. n =3. b P

Techniques Used: Western Blot, Expressing

18) Product Images from "KIF20A promotes cellular malignant behavior and enhances resistance to chemotherapy in colorectal cancer through regulation of the JAK/STAT3 signaling pathway"

Article Title: KIF20A promotes cellular malignant behavior and enhances resistance to chemotherapy in colorectal cancer through regulation of the JAK/STAT3 signaling pathway

Journal: Aging (Albany NY)

doi: 10.18632/aging.102505

KIF20A induces chemo-resistance in CRC.  ( A ,  C ) Western blot analysis of apoptosis-related factors (cleaved-caspase 3, bax, bcl-2) in different transfected groups in HCT-116 cell line treated with 4ug/ml 5-FU (left) or 8 ug/ml oxaliplatin (right) and LOVO cell line treated with 1.5 ug/ml 5-FU (left) or 1 ug/ml oxaliplatin (right). ( B ,  D ) Cell viability was measured using CCK-8 analysis and compared between different groups with different treatments at indicated times. ( E – H ) The apoptotic rates of different transfected groups with different treatments were measured by flow cytometry. Data are presented as mean ± SEM. *P
Figure Legend Snippet: KIF20A induces chemo-resistance in CRC. ( A , C ) Western blot analysis of apoptosis-related factors (cleaved-caspase 3, bax, bcl-2) in different transfected groups in HCT-116 cell line treated with 4ug/ml 5-FU (left) or 8 ug/ml oxaliplatin (right) and LOVO cell line treated with 1.5 ug/ml 5-FU (left) or 1 ug/ml oxaliplatin (right). ( B , D ) Cell viability was measured using CCK-8 analysis and compared between different groups with different treatments at indicated times. ( E – H ) The apoptotic rates of different transfected groups with different treatments were measured by flow cytometry. Data are presented as mean ± SEM. *P

Techniques Used: Western Blot, Transfection, CCK-8 Assay, Flow Cytometry, Cytometry

19) Product Images from "Antitumor Effect of n-Butylidenephthalide Encapsulated on B16/F10 Melanoma Cells In Vitro with a Polycationic Liposome Containing PEI and Polyethylene Glycol Complex"

Article Title: Antitumor Effect of n-Butylidenephthalide Encapsulated on B16/F10 Melanoma Cells In Vitro with a Polycationic Liposome Containing PEI and Polyethylene Glycol Complex

Journal: Molecules

doi: 10.3390/molecules23123224

BP/LPPC-induced apoptosis morphology and associated protein expression on B16/F10 cells. ( A ) BP or BP/LPPC-treated cell showed TUNEL positive results and apoptotic cell morphology, including chromatin condensation, DNA fragmentation, and apoptotic bodies. ( B ) BP or BP/LPPC-induced extrinsic (Fas, FasL, and Cleaved-Caspase-8) and intrinsic (Bax, AIF, and Cleaved-Caspase-9) apoptotic pathways and downstream Cleaved-Caspase-3 activation by immunocytochemistry staining. ( C ) The protein expression of Cleaved-Caspase-9, Pro-Caspase-8, and Pro-Caspase-3 were analyzed by western blotting. # p
Figure Legend Snippet: BP/LPPC-induced apoptosis morphology and associated protein expression on B16/F10 cells. ( A ) BP or BP/LPPC-treated cell showed TUNEL positive results and apoptotic cell morphology, including chromatin condensation, DNA fragmentation, and apoptotic bodies. ( B ) BP or BP/LPPC-induced extrinsic (Fas, FasL, and Cleaved-Caspase-8) and intrinsic (Bax, AIF, and Cleaved-Caspase-9) apoptotic pathways and downstream Cleaved-Caspase-3 activation by immunocytochemistry staining. ( C ) The protein expression of Cleaved-Caspase-9, Pro-Caspase-8, and Pro-Caspase-3 were analyzed by western blotting. # p

Techniques Used: Expressing, TUNEL Assay, Activation Assay, Immunocytochemistry, Staining, Western Blot

20) Product Images from "α-santalol inhibits the angiogenesis and growth of human prostate tumor growth by targeting vascular endothelial growth factor receptor 2-mediated AKT/mTOR/P70S6K signaling pathway"

Article Title: α-santalol inhibits the angiogenesis and growth of human prostate tumor growth by targeting vascular endothelial growth factor receptor 2-mediated AKT/mTOR/P70S6K signaling pathway

Journal: Molecular Cancer

doi: 10.1186/1476-4598-12-147

α-santalol potentiates apoptosis in HUVECs and PC-3 cells in a dose-dependent manner. (A) Apoptotic population of HUVEC and PC-3 tumor cells treated with α-santalol was detected by Hoechst 33258 staining. Apoptosis cells were observed in a large number of treated cells in both HUVEC and PC-3 cells. α-santalol induced cleavage of (B) caspase- 3 and (C) PARP. Proteins from HUVECs treated with α-santalol were analyzed by Western blotting analysis for cleaved caspase-3 and cleaved PARP. (D) Cells were grown at standard culture conditions as mentioned in Materials and methods, and treated with α- santalol, and cell lysates were prepared following cytometric bead array vendor manual. Beads containing active human caspase 3 were resolved in FL3 channel of flow cytometer followed by acquisition of sample data. BD CBA analysis software was used to analyze the data. Active caspase 3 was quantified using 4-parameter logistic curve-fit model generated standard curve from ‘human active caspase 3 lysate standard’ supplied with the kit, and presented as pg/ml cell lysate. Values are mean ± SEM (n = 6) of three independent experiments. *p
Figure Legend Snippet: α-santalol potentiates apoptosis in HUVECs and PC-3 cells in a dose-dependent manner. (A) Apoptotic population of HUVEC and PC-3 tumor cells treated with α-santalol was detected by Hoechst 33258 staining. Apoptosis cells were observed in a large number of treated cells in both HUVEC and PC-3 cells. α-santalol induced cleavage of (B) caspase- 3 and (C) PARP. Proteins from HUVECs treated with α-santalol were analyzed by Western blotting analysis for cleaved caspase-3 and cleaved PARP. (D) Cells were grown at standard culture conditions as mentioned in Materials and methods, and treated with α- santalol, and cell lysates were prepared following cytometric bead array vendor manual. Beads containing active human caspase 3 were resolved in FL3 channel of flow cytometer followed by acquisition of sample data. BD CBA analysis software was used to analyze the data. Active caspase 3 was quantified using 4-parameter logistic curve-fit model generated standard curve from ‘human active caspase 3 lysate standard’ supplied with the kit, and presented as pg/ml cell lysate. Values are mean ± SEM (n = 6) of three independent experiments. *p

Techniques Used: Staining, Western Blot, Flow Cytometry, Cytometry, Crocin Bleaching Assay, Software, Generated

21) Product Images from "Simultaneous detection of nucleotide excision repair events and apoptosis-induced DNA fragmentation in genotoxin-treated cells"

Article Title: Simultaneous detection of nucleotide excision repair events and apoptosis-induced DNA fragmentation in genotoxin-treated cells

Journal: Scientific Reports

doi: 10.1038/s41598-018-20527-6

Effects of caspase 3 knockdown on the generation of large DNAs and excised oligomers.  (A)  HeLa cells were transfected with control non-targeting siRNA or caspase 3 siRNA, exposed to 20 J/m 2  of UVC 48 h later and harvested at the indicated time points. The cells were analyzed for the soluble DNAs (upper panel), and used for immunoblotting with the indicated antibodies (lower panel). Quantitative analysis of the generation of large DNAs  (B)  and excised oligomers  (C)  is also shown.
Figure Legend Snippet: Effects of caspase 3 knockdown on the generation of large DNAs and excised oligomers. (A) HeLa cells were transfected with control non-targeting siRNA or caspase 3 siRNA, exposed to 20 J/m 2 of UVC 48 h later and harvested at the indicated time points. The cells were analyzed for the soluble DNAs (upper panel), and used for immunoblotting with the indicated antibodies (lower panel). Quantitative analysis of the generation of large DNAs (B) and excised oligomers (C) is also shown.

Techniques Used: Transfection

22) Product Images from "α-santalol inhibits the angiogenesis and growth of human prostate tumor growth by targeting vascular endothelial growth factor receptor 2-mediated AKT/mTOR/P70S6K signaling pathway"

Article Title: α-santalol inhibits the angiogenesis and growth of human prostate tumor growth by targeting vascular endothelial growth factor receptor 2-mediated AKT/mTOR/P70S6K signaling pathway

Journal: Molecular Cancer

doi: 10.1186/1476-4598-12-147

α-santalol potentiates apoptosis in HUVECs and PC-3 cells in a dose-dependent manner. (A) Apoptotic population of HUVEC and PC-3 tumor cells treated with α-santalol was detected by Hoechst 33258 staining. Apoptosis cells were observed in a large number of treated cells in both HUVEC and PC-3 cells. α-santalol induced cleavage of (B) caspase- 3 and (C) PARP. Proteins from HUVECs treated with α-santalol were analyzed by Western blotting analysis for cleaved caspase-3 and cleaved PARP. (D) Cells were grown at standard culture conditions as mentioned in Materials and methods, and treated with α- santalol, and cell lysates were prepared following cytometric bead array vendor manual. Beads containing active human caspase 3 were resolved in FL3 channel of flow cytometer followed by acquisition of sample data. BD CBA analysis software was used to analyze the data. Active caspase 3 was quantified using 4-parameter logistic curve-fit model generated standard curve from ‘human active caspase 3 lysate standard’ supplied with the kit, and presented as pg/ml cell lysate. Values are mean ± SEM (n = 6) of three independent experiments. *p
Figure Legend Snippet: α-santalol potentiates apoptosis in HUVECs and PC-3 cells in a dose-dependent manner. (A) Apoptotic population of HUVEC and PC-3 tumor cells treated with α-santalol was detected by Hoechst 33258 staining. Apoptosis cells were observed in a large number of treated cells in both HUVEC and PC-3 cells. α-santalol induced cleavage of (B) caspase- 3 and (C) PARP. Proteins from HUVECs treated with α-santalol were analyzed by Western blotting analysis for cleaved caspase-3 and cleaved PARP. (D) Cells were grown at standard culture conditions as mentioned in Materials and methods, and treated with α- santalol, and cell lysates were prepared following cytometric bead array vendor manual. Beads containing active human caspase 3 were resolved in FL3 channel of flow cytometer followed by acquisition of sample data. BD CBA analysis software was used to analyze the data. Active caspase 3 was quantified using 4-parameter logistic curve-fit model generated standard curve from ‘human active caspase 3 lysate standard’ supplied with the kit, and presented as pg/ml cell lysate. Values are mean ± SEM (n = 6) of three independent experiments. *p

Techniques Used: Staining, Western Blot, Flow Cytometry, Cytometry, Crocin Bleaching Assay, Software, Generated

23) Product Images from "Antitumor Effect of n-Butylidenephthalide Encapsulated on B16/F10 Melanoma Cells In Vitro with a Polycationic Liposome Containing PEI and Polyethylene Glycol Complex"

Article Title: Antitumor Effect of n-Butylidenephthalide Encapsulated on B16/F10 Melanoma Cells In Vitro with a Polycationic Liposome Containing PEI and Polyethylene Glycol Complex

Journal: Molecules

doi: 10.3390/molecules23123224

BP/LPPC-induced apoptosis morphology and associated protein expression on B16/F10 cells. ( A ) BP or BP/LPPC-treated cell showed TUNEL positive results and apoptotic cell morphology, including chromatin condensation, DNA fragmentation, and apoptotic bodies. ( B ) BP or BP/LPPC-induced extrinsic (Fas, FasL, and Cleaved-Caspase-8) and intrinsic (Bax, AIF, and Cleaved-Caspase-9) apoptotic pathways and downstream Cleaved-Caspase-3 activation by immunocytochemistry staining. ( C ) The protein expression of Cleaved-Caspase-9, Pro-Caspase-8, and Pro-Caspase-3 were analyzed by western blotting. # p
Figure Legend Snippet: BP/LPPC-induced apoptosis morphology and associated protein expression on B16/F10 cells. ( A ) BP or BP/LPPC-treated cell showed TUNEL positive results and apoptotic cell morphology, including chromatin condensation, DNA fragmentation, and apoptotic bodies. ( B ) BP or BP/LPPC-induced extrinsic (Fas, FasL, and Cleaved-Caspase-8) and intrinsic (Bax, AIF, and Cleaved-Caspase-9) apoptotic pathways and downstream Cleaved-Caspase-3 activation by immunocytochemistry staining. ( C ) The protein expression of Cleaved-Caspase-9, Pro-Caspase-8, and Pro-Caspase-3 were analyzed by western blotting. # p

Techniques Used: Expressing, TUNEL Assay, Activation Assay, Immunocytochemistry, Staining, Western Blot

24) Product Images from "Simultaneous detection of nucleotide excision repair events and apoptosis-induced DNA fragmentation in genotoxin-treated cells"

Article Title: Simultaneous detection of nucleotide excision repair events and apoptosis-induced DNA fragmentation in genotoxin-treated cells

Journal: Scientific Reports

doi: 10.1038/s41598-018-20527-6

Effects of caspase 3 knockdown on the generation of large DNAs and excised oligomers.  (A)  HeLa cells were transfected with control non-targeting siRNA or caspase 3 siRNA, exposed to 20 J/m 2  of UVC 48 h later and harvested at the indicated time points. The cells were analyzed for the soluble DNAs (upper panel), and used for immunoblotting with the indicated antibodies (lower panel). Quantitative analysis of the generation of large DNAs  (B)  and excised oligomers  (C)  is also shown.
Figure Legend Snippet: Effects of caspase 3 knockdown on the generation of large DNAs and excised oligomers. (A) HeLa cells were transfected with control non-targeting siRNA or caspase 3 siRNA, exposed to 20 J/m 2 of UVC 48 h later and harvested at the indicated time points. The cells were analyzed for the soluble DNAs (upper panel), and used for immunoblotting with the indicated antibodies (lower panel). Quantitative analysis of the generation of large DNAs (B) and excised oligomers (C) is also shown.

Techniques Used: Transfection

25) Product Images from "Knockdown of long non-coding RNA TP73-AS1 inhibits cell proliferation and induces apoptosis in esophageal squamous cell carcinoma"

Article Title: Knockdown of long non-coding RNA TP73-AS1 inhibits cell proliferation and induces apoptosis in esophageal squamous cell carcinoma

Journal: Oncotarget

doi: 10.18632/oncotarget.6963

BDH2 or lncRNA TP73-AS1 knockdown activates apoptosis protein expression and enhances chemo-sensitivity to 5-FU or cisplatin in EC cells A. B. Western blot analysis showed that BDH2 or lncRNATP73-AS1 knockdown enhanced expression of cleaved caspase-3 and cleaved caspase-9 in EC9706 and KYSE30 cells. C. D. Knockdown of BDH2 or lncRNA TP73-AS1 also enhanced chemo-sensitivity to 5-FU or cisplatin in EC9706 and KYSE30 cells. (* P
Figure Legend Snippet: BDH2 or lncRNA TP73-AS1 knockdown activates apoptosis protein expression and enhances chemo-sensitivity to 5-FU or cisplatin in EC cells A. B. Western blot analysis showed that BDH2 or lncRNATP73-AS1 knockdown enhanced expression of cleaved caspase-3 and cleaved caspase-9 in EC9706 and KYSE30 cells. C. D. Knockdown of BDH2 or lncRNA TP73-AS1 also enhanced chemo-sensitivity to 5-FU or cisplatin in EC9706 and KYSE30 cells. (* P

Techniques Used: Expressing, Western Blot

26) Product Images from "Gambogenic acid synergistically potentiates bortezomib-induced apoptosis in multiple myeloma"

Article Title: Gambogenic acid synergistically potentiates bortezomib-induced apoptosis in multiple myeloma

Journal: Journal of Cancer

doi: 10.7150/jca.17657

Western blot analysis of BTZ, GNA and the combination on apoptosis-related proteins of tumor tissues. (A) Western blot analysis of Ki-67, PARP cleavage, P53, Caspase-3 cleavage, Bax and Bcl-2. The protein expression levels (relative to GAPDH) were assessed. (B) The normalized intensity of cleaved PARP, P53, cleaved Caspase-3, Bax and Bcl-2 proteins were processed statistically. Columns, means for three replicate determinations; bars, s.d. * P
Figure Legend Snippet: Western blot analysis of BTZ, GNA and the combination on apoptosis-related proteins of tumor tissues. (A) Western blot analysis of Ki-67, PARP cleavage, P53, Caspase-3 cleavage, Bax and Bcl-2. The protein expression levels (relative to GAPDH) were assessed. (B) The normalized intensity of cleaved PARP, P53, cleaved Caspase-3, Bax and Bcl-2 proteins were processed statistically. Columns, means for three replicate determinations; bars, s.d. * P

Techniques Used: Western Blot, Expressing

Representative photographs of immunochemistry of Ki-67, PARP cleavage, P53, Caspase-3 cleavage, Bax and Bcl-2 in different groups. Staining was performed with anti-ki-67 antibody for proliferation, anti-PARP cleavage, -P53, Caspase-3 cleavage, -Bax and -Bcl-2 polyclonal antibodies for apoptosis. Magnification, ×400. Columns, means of four quadrants of positive cells; bars, s.d. ** P
Figure Legend Snippet: Representative photographs of immunochemistry of Ki-67, PARP cleavage, P53, Caspase-3 cleavage, Bax and Bcl-2 in different groups. Staining was performed with anti-ki-67 antibody for proliferation, anti-PARP cleavage, -P53, Caspase-3 cleavage, -Bax and -Bcl-2 polyclonal antibodies for apoptosis. Magnification, ×400. Columns, means of four quadrants of positive cells; bars, s.d. ** P

Techniques Used: Staining

Effects of BTZ, GNA and the combination on apoptosis-related proteins of MM.1S cells. MM.1S cells were treated with DMSO control, BTZ, GNA, or combination of two concentrations, respectively. (A) Western blot analysis of BTZ and GNA-induced PARP, P53, Caspase-3, Bax and Bcl-2 levels in MM.1S for 48h. (B) The normalized intensity of cleaved PARP, P53, cleaved Caspase-3, Bax and Bcl-2 proteins were processed statistically. DMSO, dimethyl sulfoxide. Columns, means for three replicate determinations; bars, s.d. * P
Figure Legend Snippet: Effects of BTZ, GNA and the combination on apoptosis-related proteins of MM.1S cells. MM.1S cells were treated with DMSO control, BTZ, GNA, or combination of two concentrations, respectively. (A) Western blot analysis of BTZ and GNA-induced PARP, P53, Caspase-3, Bax and Bcl-2 levels in MM.1S for 48h. (B) The normalized intensity of cleaved PARP, P53, cleaved Caspase-3, Bax and Bcl-2 proteins were processed statistically. DMSO, dimethyl sulfoxide. Columns, means for three replicate determinations; bars, s.d. * P

Techniques Used: Western Blot

27) Product Images from "Inhibition of autophagy enhances apoptosis induced by proteasome inhibitor bortezomib in human glioblastoma U87 and U251 cells"

Article Title: Inhibition of autophagy enhances apoptosis induced by proteasome inhibitor bortezomib in human glioblastoma U87 and U251 cells

Journal: Molecular and Cellular Biochemistry

doi: 10.1007/s11010-013-1835-z

Inhibition of autophagy by Atg7 siRNA enhances apoptosis induced by bortezomib in U251 cells. a U251 cells were treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). Cells viability was determined by MTT assay. Data are presented as mean ± SD, n = 6. b U251 cells treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). The cells were harvested after treatment and were stained with JC-1. c Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and Cytochrome C in U251 cells treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). d Quantitation of Cleaved caspase-3 and Cytochrome C levels in U251 cells treated with control siRNA or Atg7 siRNA with or without bortezomib. Data are presented as mean ± SD, n = 3, * P
Figure Legend Snippet: Inhibition of autophagy by Atg7 siRNA enhances apoptosis induced by bortezomib in U251 cells. a U251 cells were treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). Cells viability was determined by MTT assay. Data are presented as mean ± SD, n = 6. b U251 cells treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). The cells were harvested after treatment and were stained with JC-1. c Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and Cytochrome C in U251 cells treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). d Quantitation of Cleaved caspase-3 and Cytochrome C levels in U251 cells treated with control siRNA or Atg7 siRNA with or without bortezomib. Data are presented as mean ± SD, n = 3, * P

Techniques Used: Inhibition, MTT Assay, Staining, Western Blot, Quantitation Assay

Inhibition of autophagy by autophagy inhibitor 3-MA enhances apoptosis induced by bortezomib in U87 cells. a U87 cells were treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. Cells viability was determined by MTT assay. Data are presented as mean ± SD, n = 6. b U87 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. The cells were harvested after treatment and were stained with JC-1. c Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and Cytochrome C in U87 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. d Quantitation of Cleaved caspase-3 and Cytochrome C levels in U87 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. Data are presented as mean ± SD, n = 3, * P
Figure Legend Snippet: Inhibition of autophagy by autophagy inhibitor 3-MA enhances apoptosis induced by bortezomib in U87 cells. a U87 cells were treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. Cells viability was determined by MTT assay. Data are presented as mean ± SD, n = 6. b U87 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. The cells were harvested after treatment and were stained with JC-1. c Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and Cytochrome C in U87 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. d Quantitation of Cleaved caspase-3 and Cytochrome C levels in U87 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. Data are presented as mean ± SD, n = 3, * P

Techniques Used: Inhibition, MTT Assay, Staining, Western Blot, Quantitation Assay

Inhibition of autophagy by Atg7 siRNA enhances apoptosis induced by bortezomib in U87 cells. a U87 cells were treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). Cells viability was determined by MTT assay. Data are presented as mean ± SD, n = 6. b U87 cells treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). The cells were harvested after treatment and were stained with JC-1. c Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and Cytochrome C in U87 cells treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). d Quantitation of Cleaved caspase-3 and Cytochrome C levels in U87 cells treated with control siRNA or Atg7 siRNA with or without bortezomib. Data are presented as mean ± SD, n = 3, * P
Figure Legend Snippet: Inhibition of autophagy by Atg7 siRNA enhances apoptosis induced by bortezomib in U87 cells. a U87 cells were treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). Cells viability was determined by MTT assay. Data are presented as mean ± SD, n = 6. b U87 cells treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). The cells were harvested after treatment and were stained with JC-1. c Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and Cytochrome C in U87 cells treated with control siRNA or Atg7 siRNA with or without bortezomib (10 nM, 24 h). d Quantitation of Cleaved caspase-3 and Cytochrome C levels in U87 cells treated with control siRNA or Atg7 siRNA with or without bortezomib. Data are presented as mean ± SD, n = 3, * P

Techniques Used: Inhibition, MTT Assay, Staining, Western Blot, Quantitation Assay

Inhibition of autophagy by autophagy inhibitor 3-MA enhances apoptosis induced by bortezomib in U251 cells. a U251 cells were treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. Cells viability was determined by MTT assay. Data are presented as mean ± SD, n = 6. b U251 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. The cells were harvested after treatment and were stained with JC-1. c Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and Cytochrome C in U251 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. d Quantitation of Cleaved caspase-3 and Cytochrome C levels in U251 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. Data are presented as mean ± SD, n = 3, * P
Figure Legend Snippet: Inhibition of autophagy by autophagy inhibitor 3-MA enhances apoptosis induced by bortezomib in U251 cells. a U251 cells were treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. Cells viability was determined by MTT assay. Data are presented as mean ± SD, n = 6. b U251 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. The cells were harvested after treatment and were stained with JC-1. c Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and Cytochrome C in U251 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. d Quantitation of Cleaved caspase-3 and Cytochrome C levels in U251 cells treated with control (DMSO) or 3-MA (5 mM) with or without bortezomib (10 nM) for 24 h. Data are presented as mean ± SD, n = 3, * P

Techniques Used: Inhibition, MTT Assay, Staining, Western Blot, Quantitation Assay

Bortezomib increased the apoptotic-related proteins in U87 and U251 cells. a Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and PARP in U87 cells treated by 0, 5, 10, and 15 nM bortezomib for 24 h. b Quantitation of Cleaved caspase-3 and Cleaved PARP proteins levels in U87 cells. c Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and PARP in U251 cells treated by 0, 5, 10, and 15 nM bortezomib for 24 h. d Quantitation of Cleaved caspase-3 and Cleaved PARP proteins levels in U251 cells. Data are presented as mean ± SD, n = 3, * P
Figure Legend Snippet: Bortezomib increased the apoptotic-related proteins in U87 and U251 cells. a Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and PARP in U87 cells treated by 0, 5, 10, and 15 nM bortezomib for 24 h. b Quantitation of Cleaved caspase-3 and Cleaved PARP proteins levels in U87 cells. c Western blot analysis for the expressions of Caspase-3, Cleaved caspase-3, and PARP in U251 cells treated by 0, 5, 10, and 15 nM bortezomib for 24 h. d Quantitation of Cleaved caspase-3 and Cleaved PARP proteins levels in U251 cells. Data are presented as mean ± SD, n = 3, * P

Techniques Used: Western Blot, Quantitation Assay

28) Product Images from "Exogenous hydrogen sulfide restores cardioprotection of ischemic post-conditioning via inhibition of mPTP opening in the aging cardiomyocytes"

Article Title: Exogenous hydrogen sulfide restores cardioprotection of ischemic post-conditioning via inhibition of mPTP opening in the aging cardiomyocytes

Journal: Cell & Bioscience

doi: 10.1186/s13578-015-0035-9

Expression of Bcl-2, cleaved caspase-3 and cleaved caspase-9, cytosolic Cyt c in the d- galactose age-induced primary cultured neonatal cardiomyocytes by western blot analysis. The intensity of each band was quantified by densitometry, and data were normalized to the GAPDH signal. All data were from four independent experiments. *p
Figure Legend Snippet: Expression of Bcl-2, cleaved caspase-3 and cleaved caspase-9, cytosolic Cyt c in the d- galactose age-induced primary cultured neonatal cardiomyocytes by western blot analysis. The intensity of each band was quantified by densitometry, and data were normalized to the GAPDH signal. All data were from four independent experiments. *p

Techniques Used: Expressing, Cell Culture, Western Blot

29) Product Images from "Suppression of chloride voltage-gated channel 3 expression increases sensitivity of human glioma U251 cells to cisplatin through lysosomal dysfunction"

Article Title: Suppression of chloride voltage-gated channel 3 expression increases sensitivity of human glioma U251 cells to cisplatin through lysosomal dysfunction

Journal: Oncology Letters

doi: 10.3892/ol.2018.8736

Effect of CLCN3 antisense transfection on cisplatin cytotoxicity and lysosome dysfunction. U251 cells were treated with or without cisplatin (15 µmol/l) for 24 h following transfection of nonsense or CLCN3 antisense. (A) Analysis of apoptotic pathways triggered by cisplatin and CLCN3 antisense. Western blot analysis of TP53, BCL2, BAX, Cathepsin D expression and caspase 3 cleavage. β-actin was used as the loading control. Values represent means of three independent experiments. (B) Cathepsin D activity in cell lysates. Values represent means of three independent experiments. (C) Effects of cisplatin and CLCN3 antisense on AO emission spectra in red-stained organelles. U251 cells were treated with or without cisplatin (15 µmol/l) for 12 h following transfection of nonsense or CLCN3 antisense. Fluorescence emission of AO from red-stained organelles after 30 min of incubation with AO (5 µmol/l). The contribution of the red band within the whole spectrum (R%) is shown. A total of 25 cells were analyzed for each condition. magnification ×400 (*P
Figure Legend Snippet: Effect of CLCN3 antisense transfection on cisplatin cytotoxicity and lysosome dysfunction. U251 cells were treated with or without cisplatin (15 µmol/l) for 24 h following transfection of nonsense or CLCN3 antisense. (A) Analysis of apoptotic pathways triggered by cisplatin and CLCN3 antisense. Western blot analysis of TP53, BCL2, BAX, Cathepsin D expression and caspase 3 cleavage. β-actin was used as the loading control. Values represent means of three independent experiments. (B) Cathepsin D activity in cell lysates. Values represent means of three independent experiments. (C) Effects of cisplatin and CLCN3 antisense on AO emission spectra in red-stained organelles. U251 cells were treated with or without cisplatin (15 µmol/l) for 12 h following transfection of nonsense or CLCN3 antisense. Fluorescence emission of AO from red-stained organelles after 30 min of incubation with AO (5 µmol/l). The contribution of the red band within the whole spectrum (R%) is shown. A total of 25 cells were analyzed for each condition. magnification ×400 (*P

Techniques Used: Transfection, Western Blot, Expressing, Activity Assay, Staining, Fluorescence, Incubation

30) Product Images from "Effect of histone deacetylase inhibitors trichostatin A and valproic acid on hair cell regeneration in zebrafish lateral line neuromasts"

Article Title: Effect of histone deacetylase inhibitors trichostatin A and valproic acid on hair cell regeneration in zebrafish lateral line neuromasts

Journal: Frontiers in Cellular Neuroscience

doi: 10.3389/fncel.2014.00382

Effects of HDAC inhibitors on apoptosis. (A) Cleaved caspase-3 staining in the neuromast from a control and TSA- or VPA-treated larva. White arrows indicate cells with cleaved caspase-3. Scale bar = 10 μm. (B) After treatment of larvae with 0.1 μM TSA or 100 μM VPA for 48 h, protein extracts were prepared and subjected to western blot assay using an antibody against cleaved caspase-3. β-Actin was included as the control.
Figure Legend Snippet: Effects of HDAC inhibitors on apoptosis. (A) Cleaved caspase-3 staining in the neuromast from a control and TSA- or VPA-treated larva. White arrows indicate cells with cleaved caspase-3. Scale bar = 10 μm. (B) After treatment of larvae with 0.1 μM TSA or 100 μM VPA for 48 h, protein extracts were prepared and subjected to western blot assay using an antibody against cleaved caspase-3. β-Actin was included as the control.

Techniques Used: Staining, Western Blot

31) Product Images from "?V Integrin Induces Multicellular Radioresistance in Human Nasopharyngeal Carcinoma via Activating SAPK/JNK Pathway"

Article Title: ?V Integrin Induces Multicellular Radioresistance in Human Nasopharyngeal Carcinoma via Activating SAPK/JNK Pathway

Journal: PLoS ONE

doi: 10.1371/journal.pone.0038737

Molecular response of αV integrin mediate radioresistance in MCSs. A:  Time-course level of phosphorylated JNK in presence of irradiation.  B:  The level of phosphorylated JNK 2 hrs after irradiation.  C:  The level of cleaved caspase 3 in MCSs treated with or without SAPK/JNK pathway inhibitor SP-600125.  D:  Apoptosis in MCSs treated with or without SAPK/JNK pathway inhibitor SP-600125.
Figure Legend Snippet: Molecular response of αV integrin mediate radioresistance in MCSs. A: Time-course level of phosphorylated JNK in presence of irradiation. B: The level of phosphorylated JNK 2 hrs after irradiation. C: The level of cleaved caspase 3 in MCSs treated with or without SAPK/JNK pathway inhibitor SP-600125. D: Apoptosis in MCSs treated with or without SAPK/JNK pathway inhibitor SP-600125.

Techniques Used: Irradiation

32) Product Images from "Rap1 Ameliorates Renal Tubular Injury in Diabetic Nephropathy"

Article Title: Rap1 Ameliorates Renal Tubular Injury in Diabetic Nephropathy

Journal: Diabetes

doi: 10.2337/db13-1412

Overexpression of Rap1b inhibits generation of ROS and mCyto C release from mitochondria and decreases apoptotic protein expression and mitochondrial altered dynamics in HK-2 cells induced by HG. A : Confocal images reveal the levels of mitochondrial ROS and intracellular ROS in HK-2 cells. B : The bar graphs represent a summary of FACS experiments of MitoSOX ( B-1 ) or DFC ( B-2 ) studies. C : FACS analyses depict cell survival ( C-1 ), the bar graph represents a summary of FACS experiment from FITC Annexin V studies ( C-2 ). D : Western blots of cytosolic proteins show an altered expression of mCyto C and cleaved caspase-3 and procaspase-3 and -9. E : The bar graphs represent the quantification of average band intensity of D . F : Confocal microscopy of HK-2 cells stained with MitoTracker (red) and anti-p-Drp (Ser637) antibody (green). G : Mitochondrial fragmentation in HK-2 cells treated with 5 and 30 mmol/L d -glucose for 24–168 h. H : Flow cytometric analyses with FITC Annexin V staining. I : Western blot analyses ( I-1 ) of mitochondrial extract from HK-2 cells and bar graphs ( I-2 and I-3 ) represent the band intensity. Values are means ± SE. * P
Figure Legend Snippet: Overexpression of Rap1b inhibits generation of ROS and mCyto C release from mitochondria and decreases apoptotic protein expression and mitochondrial altered dynamics in HK-2 cells induced by HG. A : Confocal images reveal the levels of mitochondrial ROS and intracellular ROS in HK-2 cells. B : The bar graphs represent a summary of FACS experiments of MitoSOX ( B-1 ) or DFC ( B-2 ) studies. C : FACS analyses depict cell survival ( C-1 ), the bar graph represents a summary of FACS experiment from FITC Annexin V studies ( C-2 ). D : Western blots of cytosolic proteins show an altered expression of mCyto C and cleaved caspase-3 and procaspase-3 and -9. E : The bar graphs represent the quantification of average band intensity of D . F : Confocal microscopy of HK-2 cells stained with MitoTracker (red) and anti-p-Drp (Ser637) antibody (green). G : Mitochondrial fragmentation in HK-2 cells treated with 5 and 30 mmol/L d -glucose for 24–168 h. H : Flow cytometric analyses with FITC Annexin V staining. I : Western blot analyses ( I-1 ) of mitochondrial extract from HK-2 cells and bar graphs ( I-2 and I-3 ) represent the band intensity. Values are means ± SE. * P

Techniques Used: Over Expression, Expressing, FACS, Western Blot, Confocal Microscopy, Staining, Flow Cytometry

33) Product Images from "Holotoxin A1 Induces Apoptosis by Activating Acid Sphingomyelinase and Neutral Sphingomyelinase in K562 and Human Primary Leukemia Cells"

Article Title: Holotoxin A1 Induces Apoptosis by Activating Acid Sphingomyelinase and Neutral Sphingomyelinase in K562 and Human Primary Leukemia Cells

Journal: Marine Drugs

doi: 10.3390/md16040123

Holotoxin A 1 induces apoptosis through extrinsic pathway activation in human leukemic cells. ( A ) Analysis of the mechanism underlying apoptosis. Western blot of K562 cell proteins after treating cells with 0.06 μM holotoxin A 1 shows changes in protein levels over time. β-actin served as a loading control. This blot is representative of three separate experiments. Densitometry values above the bands indicate the fractional changes in protein levels, compared to initial levels at time 0; ( B ) Functional involvement of caspases in holotoxin A 1 -induced apoptosis in K562 cells. Cells were pretreated for 1 h with the pan-caspase inhibitor Z-VAD-FMK (25 μM), the caspase-8 inhibitor Z-IETD-FMK (20 μM), the caspase-9 inhibitor Z-LEHD-FMK (20 μM), or the caspase-3 inhibitor Z-DEVD-FMK (50 μM), followed by treatment with 0.06 μM holotoxin A 1 for 6 h. (Upper panel) Representative flow cytometry results indicate the extent of apoptosis (Lower panel) The mean ± SD of three independent experiments. ** p
Figure Legend Snippet: Holotoxin A 1 induces apoptosis through extrinsic pathway activation in human leukemic cells. ( A ) Analysis of the mechanism underlying apoptosis. Western blot of K562 cell proteins after treating cells with 0.06 μM holotoxin A 1 shows changes in protein levels over time. β-actin served as a loading control. This blot is representative of three separate experiments. Densitometry values above the bands indicate the fractional changes in protein levels, compared to initial levels at time 0; ( B ) Functional involvement of caspases in holotoxin A 1 -induced apoptosis in K562 cells. Cells were pretreated for 1 h with the pan-caspase inhibitor Z-VAD-FMK (25 μM), the caspase-8 inhibitor Z-IETD-FMK (20 μM), the caspase-9 inhibitor Z-LEHD-FMK (20 μM), or the caspase-3 inhibitor Z-DEVD-FMK (50 μM), followed by treatment with 0.06 μM holotoxin A 1 for 6 h. (Upper panel) Representative flow cytometry results indicate the extent of apoptosis (Lower panel) The mean ± SD of three independent experiments. ** p

Techniques Used: Activation Assay, Western Blot, Functional Assay, Flow Cytometry, Cytometry

34) Product Images from "Discovery of novel non-ATP competitive FGFR1 inhibitors and evaluation of their anti-tumor activity in non-small cell lung cancer in vitro and in vivo"

Article Title: Discovery of novel non-ATP competitive FGFR1 inhibitors and evaluation of their anti-tumor activity in non-small cell lung cancer in vitro and in vivo

Journal: Oncotarget

doi:

Aea4 and Aea25 inhibited proliferation and induced apoptosis in H460 cells (A) H460 cells were pretreated with compounds at indicated concentrations, followed by the treatment with bFGF (30 ng/mL) for 10 min. The phosphorylation level of FGFR1 in cell lysates was measured by western blot analysis. The column figures show the normalized optical density as a percentage of total FGFR1 control. (B) H460 cells were treated with compounds at concentrations (0.74, 2.22, 6.67, 20, and 60 μM) for 72 h. The MTT assay gives the respective IC 50 values of compounds. (C) The time-course cell survival profile of H460 cells treated by compounds at 20 μM was detected through an MTT assay. (D) Effects of Aea4 and Aea25 on caspase activation in H460 cells. H460 cells were harvested and lysated after incubated with Aea4 (10 μM) and Aea25 (10 μM) for 12 h. The levels of cleaved caspase-3 and cleaved caspase-9 were determined by western blot analysis. (E) Aea4 and Aea25 induced cell apoptosis in H460 cells. H460 cells were treated with Aea4 and Aea25 at indicated concentrations for 24 h, and then stained with Annexin V and PI, followed by detection using flow cytometry. The figures were representative of three separate experiments. (F) The column figure shows the apoptotic cell rate detected by flow cytometer. (* P
Figure Legend Snippet: Aea4 and Aea25 inhibited proliferation and induced apoptosis in H460 cells (A) H460 cells were pretreated with compounds at indicated concentrations, followed by the treatment with bFGF (30 ng/mL) for 10 min. The phosphorylation level of FGFR1 in cell lysates was measured by western blot analysis. The column figures show the normalized optical density as a percentage of total FGFR1 control. (B) H460 cells were treated with compounds at concentrations (0.74, 2.22, 6.67, 20, and 60 μM) for 72 h. The MTT assay gives the respective IC 50 values of compounds. (C) The time-course cell survival profile of H460 cells treated by compounds at 20 μM was detected through an MTT assay. (D) Effects of Aea4 and Aea25 on caspase activation in H460 cells. H460 cells were harvested and lysated after incubated with Aea4 (10 μM) and Aea25 (10 μM) for 12 h. The levels of cleaved caspase-3 and cleaved caspase-9 were determined by western blot analysis. (E) Aea4 and Aea25 induced cell apoptosis in H460 cells. H460 cells were treated with Aea4 and Aea25 at indicated concentrations for 24 h, and then stained with Annexin V and PI, followed by detection using flow cytometry. The figures were representative of three separate experiments. (F) The column figure shows the apoptotic cell rate detected by flow cytometer. (* P

Techniques Used: Western Blot, MTT Assay, Activation Assay, Incubation, Staining, Flow Cytometry, Cytometry

35) Product Images from "Administration of AMD3100 in endotoxemia is associated with pro-inflammatory, pro-oxidative, and pro-apoptotic effects in vivo"

Article Title: Administration of AMD3100 in endotoxemia is associated with pro-inflammatory, pro-oxidative, and pro-apoptotic effects in vivo

Journal: Journal of Biomedical Science

doi: 10.1186/s12929-016-0286-8

Spleen weights and CD3 and cleaved caspase-3 expression in the spleen. C57BL/6 N mice were treated either with LPS (5 mg/kg body weight), AMD3100 (5 mg/kg body weight), with both substances or with the solvent PBS (control). 24 h thereafter, the mice were sacrificed and the spleens were collected for further analysis. a : Spleen weights. Data are given as mean ± standard error of the mean (SEM); n = 7 for each group. Statistical significant differences between the different treatment groups were determined by using the one-way analysis of variance (ANOVA) and the Tukey post hoc test and are indicated as follows: *, p
Figure Legend Snippet: Spleen weights and CD3 and cleaved caspase-3 expression in the spleen. C57BL/6 N mice were treated either with LPS (5 mg/kg body weight), AMD3100 (5 mg/kg body weight), with both substances or with the solvent PBS (control). 24 h thereafter, the mice were sacrificed and the spleens were collected for further analysis. a : Spleen weights. Data are given as mean ± standard error of the mean (SEM); n = 7 for each group. Statistical significant differences between the different treatment groups were determined by using the one-way analysis of variance (ANOVA) and the Tukey post hoc test and are indicated as follows: *, p

Techniques Used: Expressing, Mouse Assay

36) Product Images from "Neuroprotective Effect of Hydrogen-Rich Saline against Neurologic Damage and Apoptosis in Early Brain Injury following Subarachnoid Hemorrhage: Possible Role of the Akt/GSK3? Signaling Pathway"

Article Title: Neuroprotective Effect of Hydrogen-Rich Saline against Neurologic Damage and Apoptosis in Early Brain Injury following Subarachnoid Hemorrhage: Possible Role of the Akt/GSK3? Signaling Pathway

Journal: PLoS ONE

doi: 10.1371/journal.pone.0096212

Representative western blots and quantitative analysis of Bcl-2, Bax and cleaved caspase-3 in the left cortex at 24 hours after SAH. The Bcl-2 protein level was significantly up-regulated by HS administration compared with the SAH and SAH + saline groups, which was down-regulated by Ly294002 ( P
Figure Legend Snippet: Representative western blots and quantitative analysis of Bcl-2, Bax and cleaved caspase-3 in the left cortex at 24 hours after SAH. The Bcl-2 protein level was significantly up-regulated by HS administration compared with the SAH and SAH + saline groups, which was down-regulated by Ly294002 ( P

Techniques Used: Western Blot

37) Product Images from "Uncoupling Protein 2 Increases Susceptibility to Lipopolysaccharide-Induced Acute Lung Injury in Mice"

Article Title: Uncoupling Protein 2 Increases Susceptibility to Lipopolysaccharide-Induced Acute Lung Injury in Mice

Journal: Mediators of Inflammation

doi: 10.1155/2016/9154230

UCP2 enhanced DNA damage and increased caspase-3 cleavage, cytochrome c release, and proapoptotic Bax protein expression but reduced Bcl-2 expression. (a) Western blot showed the expression of cleaved and total caspase-3 from lung tissues of mice in each group. (c) Western blot analysis detected the expression of Bcl-2, Bax, and cytochrome c protein in each group. (b, d–f) Densitometric analysis of these proteins immunoreactive bands is shown as fold difference normalized to actin expression. (g) The percentage of apoptotic positive cells was detected by the TUNEL assay. (h) The mitochondrial ATP levels were measured by a luciferase-based assay after oligomycin (1 mg/kg) preinjection in mice. (i) Western blot analysis detected the expression of cleaved and total caspase-3. (j) Densitometric analysis of cleaved caspase-3 proteins immunoreactive bands is shown as fold difference normalized to actin expression. ( ∗ P
Figure Legend Snippet: UCP2 enhanced DNA damage and increased caspase-3 cleavage, cytochrome c release, and proapoptotic Bax protein expression but reduced Bcl-2 expression. (a) Western blot showed the expression of cleaved and total caspase-3 from lung tissues of mice in each group. (c) Western blot analysis detected the expression of Bcl-2, Bax, and cytochrome c protein in each group. (b, d–f) Densitometric analysis of these proteins immunoreactive bands is shown as fold difference normalized to actin expression. (g) The percentage of apoptotic positive cells was detected by the TUNEL assay. (h) The mitochondrial ATP levels were measured by a luciferase-based assay after oligomycin (1 mg/kg) preinjection in mice. (i) Western blot analysis detected the expression of cleaved and total caspase-3. (j) Densitometric analysis of cleaved caspase-3 proteins immunoreactive bands is shown as fold difference normalized to actin expression. ( ∗ P

Techniques Used: Expressing, Western Blot, Mouse Assay, TUNEL Assay, Luciferase

UCP2-induced inflammation in LPS-induced ALI is mediated by JNK and p38 MAPK pathway. (a) Western blot detected the expression of ERK, JNK, and p38 MAPKs and their phosphorylated protein in lung tissue after LPS-induced injury. (b) Western blot detected cytochrome c and caspase-3 expression after inhibition of UCP2-induced activation of MAPK signaling pathways by the inhibitors of specific MAPK signaling pathways, respectively. (c-d) Quantification of cytochrome c and caspase-3 immunoreactivity using Western blot analysis. (e) Quantification of the phosphorylated protein p-ERK, p-JNK, and p-p38 shown in graphs using densitometric analysis. (f) The levels of TNF- α in BALF were measured by ELISA. (g) The levels of IL-1 β in BALF were measured by ELISA. (h) The levels of ROS in lung were detected by MDA assay ( ∗ P
Figure Legend Snippet: UCP2-induced inflammation in LPS-induced ALI is mediated by JNK and p38 MAPK pathway. (a) Western blot detected the expression of ERK, JNK, and p38 MAPKs and their phosphorylated protein in lung tissue after LPS-induced injury. (b) Western blot detected cytochrome c and caspase-3 expression after inhibition of UCP2-induced activation of MAPK signaling pathways by the inhibitors of specific MAPK signaling pathways, respectively. (c-d) Quantification of cytochrome c and caspase-3 immunoreactivity using Western blot analysis. (e) Quantification of the phosphorylated protein p-ERK, p-JNK, and p-p38 shown in graphs using densitometric analysis. (f) The levels of TNF- α in BALF were measured by ELISA. (g) The levels of IL-1 β in BALF were measured by ELISA. (h) The levels of ROS in lung were detected by MDA assay ( ∗ P

Techniques Used: Western Blot, Expressing, Inhibition, Activation Assay, Enzyme-linked Immunosorbent Assay, Multiple Displacement Amplification

38) Product Images from "Sevoflurane post-conditioning protects isolated rat hearts against ischemia-reperfusion injury via activation of the ERK1/2 pathway"

Article Title: Sevoflurane post-conditioning protects isolated rat hearts against ischemia-reperfusion injury via activation of the ERK1/2 pathway

Journal: Acta Pharmacologica Sinica

doi: 10.1038/aps.2014.78

Western blot of cleaved caspase-3 (A) and caspase-8 (B) from left ventricular samples were acquired at the end of reperfusion. Compared with the CON group, the expression of cleaved caspase-3 and caspase-8 in the other groups significantly increased.
Figure Legend Snippet: Western blot of cleaved caspase-3 (A) and caspase-8 (B) from left ventricular samples were acquired at the end of reperfusion. Compared with the CON group, the expression of cleaved caspase-3 and caspase-8 in the other groups significantly increased.

Techniques Used: Western Blot, Expressing

39) Product Images from "Endothelial cell-derived exosomes protect SH-SY5Y nerve cells against ischemia/reperfusion injury"

Article Title: Endothelial cell-derived exosomes protect SH-SY5Y nerve cells against ischemia/reperfusion injury

Journal: International Journal of Molecular Medicine

doi: 10.3892/ijmm.2017.3106

Influence of endothelial exosomes on the expression of Bax, Bcl-2, caspase-3 in I/R SH-SY5Y cells. Effects of exosomes derived from the endothelial cell model of ischemia and reperfusion on expression of Bax, Bcl-2, caspase-3 in I/R SH-SY5Y nerve cells. The mRNA expressions of (A) Bax, (B) Bcl-2 and (C) cleaved caspase-3. (D) Western blot analysis of Bax, Bcl-2 and caspase-3. * P
Figure Legend Snippet: Influence of endothelial exosomes on the expression of Bax, Bcl-2, caspase-3 in I/R SH-SY5Y cells. Effects of exosomes derived from the endothelial cell model of ischemia and reperfusion on expression of Bax, Bcl-2, caspase-3 in I/R SH-SY5Y nerve cells. The mRNA expressions of (A) Bax, (B) Bcl-2 and (C) cleaved caspase-3. (D) Western blot analysis of Bax, Bcl-2 and caspase-3. * P

Techniques Used: Expressing, Derivative Assay, Western Blot

40) Product Images from "Fibroblast-Derived Extracellular Matrix Induces Chondrogenic Differentiation in Human Adipose-Derived Mesenchymal Stromal/Stem Cells in Vitro"

Article Title: Fibroblast-Derived Extracellular Matrix Induces Chondrogenic Differentiation in Human Adipose-Derived Mesenchymal Stromal/Stem Cells in Vitro

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms17081259

Ad-MSCs express pluripotency markers and are viable over several passages. ( A ) Vimentin and CD44 expression in ad-MSCs from three donors was determined by immunoblot analysis. GAPDH was used as a loading control; ( B , C ) Ad-MSCs express Octamer-binding transcription factor 4 (Oct4) over several passages. The expression of pluripotency markers Oct4 and Nanog expression in ad-MSCs was determined over several passages was determined by immunoblot analysis and RT-qPCR; ( D ) Cleaved caspase 3 and 9 in ad-MSCs was determined by immunoblot analysis over several passages; and ( E ) Flow cytometric analysis was done to determine the effect of prolonged culture on ad-MSCs’ cell cycling.
Figure Legend Snippet: Ad-MSCs express pluripotency markers and are viable over several passages. ( A ) Vimentin and CD44 expression in ad-MSCs from three donors was determined by immunoblot analysis. GAPDH was used as a loading control; ( B , C ) Ad-MSCs express Octamer-binding transcription factor 4 (Oct4) over several passages. The expression of pluripotency markers Oct4 and Nanog expression in ad-MSCs was determined over several passages was determined by immunoblot analysis and RT-qPCR; ( D ) Cleaved caspase 3 and 9 in ad-MSCs was determined by immunoblot analysis over several passages; and ( E ) Flow cytometric analysis was done to determine the effect of prolonged culture on ad-MSCs’ cell cycling.

Techniques Used: Expressing, Binding Assay, Quantitative RT-PCR, Flow Cytometry

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  • 92
    Santa Cruz Biotechnology anti activated caspase 3
    The analysis of apoptosis pathways in Trp53 +/- mouse testes. (A) Apoptotic spermatogenic cells stained with TUNEL in Trp53 +/- mouse testes (magnification, 200×; scale bar = 100 μm), arrows indicate TUNEL-positive cells (red) in the seminiferous tubule (lu, lumen; sg, spermatogonia; ps, pachytene spermatocyte; ls, leptotene stage spermatocyte; lc, leydig cell; sp, spermatozoa). (B) Representative images of Western blotting for Apaf-1, bax, bcl-2, cytochrome c, <t>caspase-3</t> and activated caspase-3 in Trp53 +/- mouse testes of each group. (C) Relative each protein expression compared with control; Values represent the average ± S.E.M from three gels per group. Asterisks indicate a statistically significant difference from control: * P
    Anti Activated Caspase 3, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti activated caspase 3/product/Santa Cruz Biotechnology
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    anti activated caspase 3 - by Bioz Stars, 2020-09
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    89
    Santa Cruz Biotechnology mouse anti caspase 3 antibody
    Effect of remifentanil on <t>caspase-3</t> expression in the dentate gyrus following transient global ischemia. Results show that induction of ischemia increased caspase-3 expression in the dentate gyrus and treatment with remifentanil inhibited ischemia-induced increase in caspase-3 expression. Upper: Photomicrographs of caspase-3-positive cells. (a) Sham-operation group, (b) ischemia-induction group, (c) ischemia-induction and 0.2 mg/kg remifentanil-treated group. Scale bar represents 25 µm. Lower: number of caspase-3-positive cells in each group. Values shown are the mean ± SEM. * P
    Mouse Anti Caspase 3 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 89/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse anti caspase 3 antibody/product/Santa Cruz Biotechnology
    Average 89 stars, based on 39 article reviews
    Price from $9.99 to $1999.99
    mouse anti caspase 3 antibody - by Bioz Stars, 2020-09
    89/100 stars
      Buy from Supplier

    91
    Santa Cruz Biotechnology rabbit anti caspase 3 antibody
    Pancreatic tissue expression of proapoptotic proteins caspases-3 and -9). A) Immunoblots of caspase-9 and C) <t>caspase-3</t> protein expressions normalized to β-actin and corresponding densitometry scans ( B and D , respectively) expressed as relative fold change in band intensity to control. *, ** p
    Rabbit Anti Caspase 3 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti caspase 3 antibody/product/Santa Cruz Biotechnology
    Average 91 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    rabbit anti caspase 3 antibody - by Bioz Stars, 2020-09
    91/100 stars
      Buy from Supplier

    Image Search Results


    The analysis of apoptosis pathways in Trp53 +/- mouse testes. (A) Apoptotic spermatogenic cells stained with TUNEL in Trp53 +/- mouse testes (magnification, 200×; scale bar = 100 μm), arrows indicate TUNEL-positive cells (red) in the seminiferous tubule (lu, lumen; sg, spermatogonia; ps, pachytene spermatocyte; ls, leptotene stage spermatocyte; lc, leydig cell; sp, spermatozoa). (B) Representative images of Western blotting for Apaf-1, bax, bcl-2, cytochrome c, caspase-3 and activated caspase-3 in Trp53 +/- mouse testes of each group. (C) Relative each protein expression compared with control; Values represent the average ± S.E.M from three gels per group. Asterisks indicate a statistically significant difference from control: * P

    Journal: International Journal of Biological Sciences

    Article Title: Apoptosis Induction by Iron Radiation via Inhibition of Autophagy in Trp53+/-Mouse Testes: Is Chronic Restraint-Induced Stress a Modifying Factor?

    doi: 10.7150/ijbs.22805

    Figure Lengend Snippet: The analysis of apoptosis pathways in Trp53 +/- mouse testes. (A) Apoptotic spermatogenic cells stained with TUNEL in Trp53 +/- mouse testes (magnification, 200×; scale bar = 100 μm), arrows indicate TUNEL-positive cells (red) in the seminiferous tubule (lu, lumen; sg, spermatogonia; ps, pachytene spermatocyte; ls, leptotene stage spermatocyte; lc, leydig cell; sp, spermatozoa). (B) Representative images of Western blotting for Apaf-1, bax, bcl-2, cytochrome c, caspase-3 and activated caspase-3 in Trp53 +/- mouse testes of each group. (C) Relative each protein expression compared with control; Values represent the average ± S.E.M from three gels per group. Asterisks indicate a statistically significant difference from control: * P

    Article Snippet: The sections were blocked with 5% BSA (5 g BSA in 100 mL TBS) for 30 min, then were applied with primary antibody anti-GRP78, anti-activated caspase 3 and anti-Cytochrome c (1:100, Bioworld), anti-p62 (1:100, Santa cruz), anti-Atg5 and CHOP (1:100, Abcam).

    Techniques: Staining, TUNEL Assay, Western Blot, Expressing

    Effect of remifentanil on caspase-3 expression in the dentate gyrus following transient global ischemia. Results show that induction of ischemia increased caspase-3 expression in the dentate gyrus and treatment with remifentanil inhibited ischemia-induced increase in caspase-3 expression. Upper: Photomicrographs of caspase-3-positive cells. (a) Sham-operation group, (b) ischemia-induction group, (c) ischemia-induction and 0.2 mg/kg remifentanil-treated group. Scale bar represents 25 µm. Lower: number of caspase-3-positive cells in each group. Values shown are the mean ± SEM. * P

    Journal: Korean Journal of Anesthesiology

    Article Title: Remifentanil alleviates transient cerebral ischemia-induced memory impairment through suppression of apoptotic neuronal cell death in gerbils

    doi: 10.4097/kjae.2011.61.1.63

    Figure Lengend Snippet: Effect of remifentanil on caspase-3 expression in the dentate gyrus following transient global ischemia. Results show that induction of ischemia increased caspase-3 expression in the dentate gyrus and treatment with remifentanil inhibited ischemia-induced increase in caspase-3 expression. Upper: Photomicrographs of caspase-3-positive cells. (a) Sham-operation group, (b) ischemia-induction group, (c) ischemia-induction and 0.2 mg/kg remifentanil-treated group. Scale bar represents 25 µm. Lower: number of caspase-3-positive cells in each group. Values shown are the mean ± SEM. * P

    Article Snippet: Briefly, sections were drawn from each brain and then incubated overnight with mouse anti-caspase-3 antibody (1 : 500; Santa Cruz Biotechnology, Santa Cruz, CA, USA).

    Techniques: Expressing

    Western blots showing PARP fragmentation and caspase 3 activation during 24 h treatment of CML cells (a) or PBL (b). Cells were treated by actinomycin D (A), sodium butyrate (B), SAHA (S), decitabine (D), or their combination (AB, AS, DS). Symbol C denotes untreated cells. β -actin expression is showed as a loading control.

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Generation of Reactive Oxygen Species during Apoptosis Induced by DNA-Damaging Agents and/or Histone Deacetylase Inhibitors

    doi: 10.1155/2011/253529

    Figure Lengend Snippet: Western blots showing PARP fragmentation and caspase 3 activation during 24 h treatment of CML cells (a) or PBL (b). Cells were treated by actinomycin D (A), sodium butyrate (B), SAHA (S), decitabine (D), or their combination (AB, AS, DS). Symbol C denotes untreated cells. β -actin expression is showed as a loading control.

    Article Snippet: Primary rabbit polyclonal anti-PARP and mouse monoclonal anti-caspase 3 were from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA, USA), mouse monoclonal anti-β -actin was originated from Sigma-Aldrich.

    Techniques: Western Blot, Activation Assay, Expressing

    Pancreatic tissue expression of proapoptotic proteins caspases-3 and -9). A) Immunoblots of caspase-9 and C) caspase-3 protein expressions normalized to β-actin and corresponding densitometry scans ( B and D , respectively) expressed as relative fold change in band intensity to control. *, ** p

    Journal: PLoS ONE

    Article Title: Naringin prevents HIV-1 protease inhibitors-induced metabolic complications in vivo

    doi: 10.1371/journal.pone.0183355

    Figure Lengend Snippet: Pancreatic tissue expression of proapoptotic proteins caspases-3 and -9). A) Immunoblots of caspase-9 and C) caspase-3 protein expressions normalized to β-actin and corresponding densitometry scans ( B and D , respectively) expressed as relative fold change in band intensity to control. *, ** p

    Article Snippet: Thereafter, the membranes were incubated overnight at 4.0°C with primary antibody (1:1000 dilution in TBS-T) rabbit p-IRS-1/2 (Tyr 612, Santa Cruz Biotechnology), p-Akt1/2/3 (Ser 473, Santa Cruz Biotechnology), goat UCP-2 N-19 (sc-6526), rabbit anti-caspase-3 antibody (ab2302), rabbit anti-caspase-9 antibody (ab25758) (Santa Cruz Biotechnology), respectively.

    Techniques: Expressing, Western Blot