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Caspase 3

Caspase 3 is a cysteine-aspartic acid protease that plays a central role in the execution-phase of cell apoptosis (programmed cell death).
It is responsible for the proteolytic cleavage of many key cellular proteins, ultimately leading to the characteristic morphological and biochemical changes observed in cells undergoing apoptosis.
Caspase 3 is considered a key mediator of apoptosis in mammalian cells and has been extensively studied as a potential therapeutic target for a variety of diseases, including cancer, neurodegenerative disorders, and autoimmune conditions.
Understanding the regulation and activation of Caspase 3 is crucial for develping effective interventions to modulate cell death pathways.

Most cited protocols related to «Caspase 3»

1
In vivo Plasmid Transfection and dsRNA Analysis
Subretinal injections (1 µL) were performed using a Pico-Injector (PLI-100, Harvard Apparatus). Plasmids were transfection in vivo using 10% Neuroporter (Genlantis). Immunolabeling was performed using antibodies against dsRNA (clone J2, English & Scientific Consulting), DICER1 (Santa Cruz Biotechnology), zonula occludens-1 (Invitrogen), Cre recombinase (EMD4Biosciences), or cleaved caspase-3 (Cell Signaling). dsRNA was isolated by immunoprecipitating homogenized tissue lysates with 40 µg of J2 for 16 h at 4 °C. Purified dsRNA was ligated to an anchor primer and purified by MinElute Gel extraction columns (Qiagen). Ligated dsRNA was denatured, reverse transcribed, and amplified by PCR. Amplified cDNA products were cloned into PCRII TOPO vector (Invitrogen) and sequenced. Homology to Alu consensus sequences was determined using CENSOR. Cell viability was assessed using CellTiter 96 AQueous One Solution Cell Proliferation Assay (Promega). Total RNA (1 µg) was reverse transcribed using qScript cDNA SuperMix (Quanta Biosciences) and amplified by real-time quantitative PCR (Applied Biosystems 7900 HT) with Power SYBR green Master Mix. Relative expressions were determined by the 2−ΔΔCt method. miRNA abundance was quantified using All-in-One™ miRNA qRT-PCR Detection Kit (GeneCopoeia).
Full Methods and any associated references are available in the online version of the paper at www.nature.com/nature.
Kaneko H., Dridi S., Tarallo V., Gelfand B.D., Fowler B.J., Cho W.G., Kleinman M.E., Ponicsan S.L., Hauswirth W.W., Chiodo V.A., Karikó K., Yoo J.W., Lee D.K., Hadziahmetovic M., Song Y., Misra S., Chaudhuri G., Buaas F.W., Braun R.E., Hinton D.R., Zhang Q., Grossniklaus H.E., Provis J.M., Madigan M.C., Milam A.H., Justice N.L., Albuquerque R.J., Blandford A.D., Bogdanovich S., Hirano Y., Witta J., Fuchs E., Littman D.R., Ambati B.K., Rudin C.M., Chong M.M., Provost P., Kugel J.F., Goodrich J.A., Dunaief J.L., Baffi J.Z, & Ambati J. (2011). DICER1 deficit induces Alu RNA toxicity in age-related macular degeneration. Nature, 471(7338), 325-330.
Publication 2011
Antibodies Biological Assay Caspase 3 Cell Proliferation Cell Survival Cloning Vectors Cre recombinase DICER1 protein, human DNA, Complementary Homologous Sequences MicroRNAs Oligonucleotide Primers Plasmids Real-Time Polymerase Chain Reaction RNA, Double-Stranded SYBR Green I Tight Junctions Tissues Topotecan Transfection
2
High-content Imaging of Cell Response to Drugs
MCF 10A-H2B-mCherry cells were plated at densities that ranged from 156 to 5000 cells per well in 384-well plates using the Multidrop Combi Reagent Dispenser (Thermo Scientific) and grown for 24 hours. Cells were treated with a dilution series of drugs using a D300 Digital Dispenser (Hewlett-Packard) and imaged after drug addition in an Operetta (Perkin Elmer) for high content imaging system equipped with a live-cell chamber over a period of 72 hours.
In the case of methotrexate and oligomycin, 1250 cells were plated in 20–120 µl of media per well, treated with a dilution series of drug, and imaged for 72 hours.
In the case of linsitinib, cells were treated with a dilution series of linsitinib either with or without 10µM batimastat using a D300 Digital Dispenser and imaged in an IncuCyte ZOOM live cell imager (Essen Bioscience) for an additional 72 hours.
In the case of paclitaxel, cells were treated with a dilution series of paclitaxel and 200 nM of NucView 488 caspase 3 substrate (Biotium) using a D300 Digital Dispenser (Hewlett-Packard) and imaged after drug in an IncuCyte ZOOM live cell imager (Essen Bioscience) for an additional 72 hours. For immunofluorescence experiments, cells were grown for 24 hours and then treated with a dilution series of paclitaxel using a D300 Digital Dispenser (Hewlett-Packard) and incubated for 3, 6, 12, and 24 hours. Cells were fixed for 30 min in 3% formaldehyde, permeabilized for 30 min in phosphate buffered saline (PBS) with 0.3% Triton X-100 (Sigma-Aldrich), washed twice in PBS with 0.1% Tween 20 (Sigma-Aldrich; PBS-T), and blocked for 60 min with Odyssey blocking buffer. Anti-active Caspase-3 antibody (BD Biosciences) was diluted 1:1000 in Odyssey blocking buffer and incubated for 16 h at 4°C. Cells were washed three times in PBS-T for 5 min and incubated with Alexa Fluor 488 conjugated goat anti-rabbit secondary antibody for 60 min at room. Cells were washed two times in PBS-T, once with PBS, and stained for 30 min with whole cell stain (Thermo Fisher Scientific) and Hoechst (Thermo Fisher Scientific), and washed three times in PBS.
Hafner M., Niepel M., Chung M, & Sorger P.K. (2016). Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nature methods, 13(6), 521-527.
Publication 2016
alexa fluor 488 Antibodies, Anti-Idiotypic batimastat Cardiac Arrest Caspase Caspase 3 Cells Fingers Formaldehyde Goat Immunofluorescence linsitinib Methotrexate Oligomycins Paclitaxel Pharmaceutical Preparations Phosphates Rabbits Saline Solution Stains Technique, Dilution Triton X-100 Tween 20
3
High-content Imaging of Cell Response to Drugs
MCF 10A-H2B-mCherry cells were plated at densities that ranged from 156 to 5000 cells per well in 384-well plates using the Multidrop Combi Reagent Dispenser (Thermo Scientific) and grown for 24 hours. Cells were treated with a dilution series of drugs using a D300 Digital Dispenser (Hewlett-Packard) and imaged after drug addition in an Operetta (Perkin Elmer) for high content imaging system equipped with a live-cell chamber over a period of 72 hours.
In the case of methotrexate and oligomycin, 1250 cells were plated in 20–120 µl of media per well, treated with a dilution series of drug, and imaged for 72 hours.
In the case of linsitinib, cells were treated with a dilution series of linsitinib either with or without 10µM batimastat using a D300 Digital Dispenser and imaged in an IncuCyte ZOOM live cell imager (Essen Bioscience) for an additional 72 hours.
In the case of paclitaxel, cells were treated with a dilution series of paclitaxel and 200 nM of NucView 488 caspase 3 substrate (Biotium) using a D300 Digital Dispenser (Hewlett-Packard) and imaged after drug in an IncuCyte ZOOM live cell imager (Essen Bioscience) for an additional 72 hours. For immunofluorescence experiments, cells were grown for 24 hours and then treated with a dilution series of paclitaxel using a D300 Digital Dispenser (Hewlett-Packard) and incubated for 3, 6, 12, and 24 hours. Cells were fixed for 30 min in 3% formaldehyde, permeabilized for 30 min in phosphate buffered saline (PBS) with 0.3% Triton X-100 (Sigma-Aldrich), washed twice in PBS with 0.1% Tween 20 (Sigma-Aldrich; PBS-T), and blocked for 60 min with Odyssey blocking buffer. Anti-active Caspase-3 antibody (BD Biosciences) was diluted 1:1000 in Odyssey blocking buffer and incubated for 16 h at 4°C. Cells were washed three times in PBS-T for 5 min and incubated with Alexa Fluor 488 conjugated goat anti-rabbit secondary antibody for 60 min at room. Cells were washed two times in PBS-T, once with PBS, and stained for 30 min with whole cell stain (Thermo Fisher Scientific) and Hoechst (Thermo Fisher Scientific), and washed three times in PBS.
Hafner M., Niepel M., Chung M, & Sorger P.K. (2016). Growth rate inhibition metrics correct for confounders in measuring sensitivity to cancer drugs. Nature methods, 13(6), 521-527.
Publication 2016
alexa fluor 488 Antibodies, Anti-Idiotypic batimastat Cardiac Arrest Caspase Caspase 3 Cells Fingers Formaldehyde Goat Immunofluorescence linsitinib Methotrexate Oligomycins Paclitaxel Pharmaceutical Preparations Phosphates Rabbits Saline Solution Stains Technique, Dilution Triton X-100 Tween 20
4
In situ Immunohistochemical Analysis of Colon
In situ immunohistochemical analysis of colonic paraffin sections was performed as described previously [35–37 (link)]. Primary antibodies against cleaved caspase-3 (Asp175, Cell Signaling, Beverly, MA, USA, 1:200), Ki67 (TEC3, Dako, Denmark, 1:100), myeloperoxidase (MPO-7, no. A0398, Dako, 1:500), F4/80 (no. 14-4801, clone BM8, eBioscience, San Diego, CA, USA, 1:50), CD3 (no. N1580, Dako, 1:10), FOXP3 (FJK-16s, eBioscience, 1:100), and B220 (eBioscience, 1:200) were used. For each animal, the average number of positively stained cells within at least six high power fields (HPF, 0.287 mm2 (link), 400× magnification) were determined microscopically by a double-blinded investigator.
Alutis M.E., Grundmann U., Fischer A., Hagen U., Kühl A.A., Göbel U.B., Bereswill S, & Heimesaat M.M. (2015). The Role of Gelatinases in Campylobacter Jejuni Infection of Gnotobiotic Mice. European Journal of Microbiology & Immunology, 5(4), 256-267.
Publication 2015
Animals Antibodies Caspase 3 Clone Cells Colon Paraffin Peroxidase
5
Protein Extraction and Western Blot Analysis
Cells and tissues were lysed in RIPA buffer. Tumors were ground in liquid nitrogen and lysed. Protein concentration was determined using the BCA Kit (Beyotime Institute of Biotechnology). Proteins were mixed with loading buffer and heated at 70°C for 10 minutes on sodium dodecyl sulfate (SDS)-polyacrylamide gels at 30 μg per lane. The proteins were transferred to polyvinylidene fluoride (PVDF, Millipore, MA, USA) after electrophoresis. Membranes were blocked for 2 hours in 5% BSA and incubated overnight at 4°C with antibodies against γ-H2AX, ATM, ATR, Chk1, cell-cycle controller-2 (Cdc2), E-cadherin, vimentin, caspase-3, and caveolin-1 (Cav-1). The blots were then incubated with HRP-conjugated secondary antibody (1:1000; Santa Cruz Biotechnology). Finally, bands were visualized by enhanced chemiluminescence (Thermo Scientific Pierce, IL, USA).
Tian Y., Xie Q., He J., Luo X., Zhou T., Liu Y., Huang Z., Tian Y., Sun D, & Yao K. (2015). Radioactive 125I seeds inhibit cell growth and epithelial-mesenchymal transition in human glioblastoma multiforme via a ROS-mediated signaling pathway. BMC Cancer, 15, 1.
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Publication 2015
Antibodies Buffers Caspase 3 Caveolin 1 Cell Cycle Cells Chemiluminescence E-Cadherin Electrophoresis Immunoglobulins Neoplasms Nitrogen polyacrylamide gels polyvinylidene fluoride Proteins Radioimmunoprecipitation Assay Sulfate, Sodium Dodecyl Tissue, Membrane Tissues Vimentin

Most recents protocols related to «Caspase 3»

1
Targeted Delivery of TNF Reduces Glioblastoma
Not available on PMC !

Example 1

Three patients with recurrent glioblastoma were treated with L19-TNFα at a dose level of 10 μg/kg. Already twenty-four hours after the infusion, a decrease in overall tumor perfusion and an emerging tumor necrosis was detected, as shown in FIG. 1A. One patient had progressive disease after three months and two patients still have stable disease with an increasing area of necrosis in the tumor region at six months after treatment. This is surprising considering that the Progression Free Survival (PFS) for recurrent glioblastoma is 1.5 months.

The patient with progressive disease underwent re-section and the tissue from this surgery, i.e. after treatment with L19-TNFα, was compared with the tissue obtained during first surgery. By immunohistochemistry, a significant increase in tumor-infiltrating CD4 and CD8 T-cells in the tumor after L19-TNFα treatment was detected. Furthermore, increased levels of cleaved caspase-3 were found suggesting a higher number of dead tumor cells, as shown in FIG. 1B. These data demonstrate the in situ activation due to the targeted delivery of TNF.

US11872288B2. TNF-alpha immunoconjugate therapy for the treatment of brain tumors (2024-01-16). PHILOGEN S.P.A [IT]. Inventors: Theresa Hemmerle [CH].
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Patent 2024
Aftercare Caspase 3 CD8-Positive T-Lymphocytes Glioblastoma Immunohistochemistry Necrosis Neoplasms Obstetric Delivery Operative Surgical Procedures Patients Perfusion Recurrent Brain Tumors Tissues Tumor Necrosis Factor-alpha
2
Evaluating HIIT Effects on HF Patients
Values are shown as the mean ± standard error of mean (SEM), and error bars for scatter dot plots represent one SEM. Since aerobic capacity and cardiac fibrosis are significant clinical outcomes related to the survival of HF patients [4 (link), 8 (link)], power (1- β) analysis for paired sample t tests used to compare the difference in V O2peak and ECV fractions before and after HIIT. Differences in physical PCS, MCS, and LVWMS were estimated by the chi-square test.
The nonparametric test was used in the study owing to the limited sample size. The Wilcoxon signed rank test was conducted to estimate within-group differences between data before and after HIIT, including exercise capacity function, CMR-LGE results (LV geometry, functions, and ECV fractions), and blood chemistry data. The Mann‒Whitney U test was used to estimate differences in selected protein amounts obtained from LC‒MS results and methylation levels between cells incubated in patient serum before and after HIIT. Relationships between the DNMT1 levels and health-related physical fitness and CMR-LGE findings were assessed by Spearman’s correlation analysis.
Relative protein expression (measurements/baseline) of VLCAD, Cyto C, CASP3, lamin B1, actin and Arp2 in HCFs between the original and knockdown of ACADVL was compared by the Mann‒Whitney U test. This test was also used to assess mitochondrial intensity in HCFs treated with patient serum before and after HIIT and in cells with and without ACADVL knockdown. Kruskall-Wallis test was conducted to assess cell migration speed in three different culture media and with different cell numbers at different times (baseline, 24 h and 48 h after inoculation). Multiple comparisons Dunn’s test was used to estimate differences of cell behaviours between each of the above sampling time. The relationships between normalized changes (  ΔValue=Valuepost-HIIT-Valuepre-HIITValuepre-HIIT ) in exercise performance and CMR-LGE measurements after HIIT were estimated by Spearman correlation and partial correlation analysis after controlling LV mass. All statistical assessments were considered significant at p < 0.05.
Hsu C.C., Wang J.S., Shyu Y.C., Fu T.C., Juan Y.H., Yuan S.S., Wang C.H., Yeh C.H., Liao P.C., Wu H.Y, & Hsu P.H. (2023). Hypermethylation of ACADVL is involved in the high-intensity interval training-associated reduction of cardiac fibrosis in heart failure patients. Journal of Translational Medicine, 21, 187.
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Publication 2023
Actins Acyl-Coa Dehydrogenase Very Long Chain Deficiency Blood Chemical Analysis Caspase 3 Cells Culture Media DNMT1 protein, human Exercise, Aerobic Fibrosis Heart lamin B1 Long-Chain-Acyl-CoA Dehydrogenase Methylation Migration, Cell Mitochondria Patients Physical Examination Proteins Serum Vaccination
3
Downregulating ACADVL Gene Expression
The ACADVL gene encodes for very long-chain acyl-CoA dehydrogenase (VLCAD), which functions within mitochondria and is essential for fatty acid oxidation. HCFs were prepared for western blot analysis of VLCAD, caspase-3 (CASP3), cytochrome c (Cyto C), lamin B1, β-actin, and Arp2 with the internal reference protein glyceraldehyde 3-phosphate dehydrogenase (GAPDH) before knockdown of the ACADVL gene. The above proteins were quantified again after knockdown of ACADVL. Detailed methods of the western blotting and knockdown procedure are provided in Additional file 2.
Knockdown of DNMT1 leads to generally decreased DNA methylation and activates cascades of genotoxic stress [31 (link)] in cells, resulting in signal transduction unrelated to cardiac fibrosis. Thus, we preferred to downregulate the ACADVL gene expression to simulate the HIIT-associated inhibition of human cardiac fibroblast activities.
Hsu C.C., Wang J.S., Shyu Y.C., Fu T.C., Juan Y.H., Yuan S.S., Wang C.H., Yeh C.H., Liao P.C., Wu H.Y, & Hsu P.H. (2023). Hypermethylation of ACADVL is involved in the high-intensity interval training-associated reduction of cardiac fibrosis in heart failure patients. Journal of Translational Medicine, 21, 187.
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Publication 2023
Actin-Related Protein 2 Actins Acyl-Coa Dehydrogenase Very Long Chain Deficiency Caspase 3 Cells Cytochromes c DNA Methylation DNMT1 protein, human Fatty Acids, Essential Fibroblasts Fibrosis Gene Expression Gene Knockdown Techniques Genes Genotoxic Stress Glyceraldehyde-3-Phosphate Dehydrogenases Heart lamin B1 Long-Chain-Acyl-CoA Dehydrogenase Mitochondria Proteins Psychological Inhibition Signal Transduction Western Blot
4
Evaluating PDTO Responses to Diverse Treatments
The evaluation of the response to treatments will be performed when PDTO have reached a diameter of 150 μm in « PDTO treatment medium », corresponding to the PDTO culture medium lacking N-Acetylcysteine, Y-27632 and primocin.
PDTO will be collected, resuspended in 2% extracellular matrix/PDTO culture medium and then platted in white and clear bottom 96-well plates previously coated with a 1:1 volume mix of PDTO treatment medium with extracellular matrix. In the case of evaluation of the response to radiotherapy, PDTO will be before irradiated using the CellRad System (FAXITRON Bioptics). In the case of evaluation of the response to chemotherapy or PARP inhibitors, drugs are prepared in 2% extracellular matrix/PDTO culture medium and added 1 hour after PDTO have been plated.
In the case of evaluation of the response to immunotherapies, PDTO will be co-cultured with PDTO specific T cells previously generated (see co-culture of PDTO with immune cells) at a 5:1 ratio. Treatments (such as Nivolumab or Pembrolizumab) will be added directly in the co-culture. A condition containing an MHC-I blocking antibody will be added to control for antigen specific killing.
PDTO morphology will be monitored by taking images during the required time using Incucyte S3 (Sartorius). At the endpoint, PDTO response will be assessed using CellTiter-Glo 3D cell viability assay (Promega) according to the manufacturer’s instruction and luminescence will be measured using GloMax Discover GM3000 (Promega) with the associated software. Results will be normalized to the control condition. IC50 will be calculated with GraphPad software. The ability of T cells to recognize and induce lysis of PDTO will be monitored via analysis of caspase 3 cleavage within PDTO and visualization of LAMP-1 on the membrane of CD8+ T cells.
The treatment response of the PDTO will be finally compared to the clinical response (PFS/DFS/OS) of the patient from whom they are derived in order to validate the predictive value of this model for HNSCC.
Perréard M., Florent R., Divoux J., Grellard J.M., Lequesne J., Briand M., Clarisse B., Rousseau N., Lebreton E., Dubois B., Harter V., Lasne-Cardon A., Drouet J., Johnson A., Le Page A.L., Bazille C., Jeanne C., Figeac M., Goardon N., Vaur D., Micault E., Humbert M., Thariat J., Babin E., Poulain L., Weiswald L.B, & Bastit V. (2023). ORGAVADS: establishment of tumor organoids from head and neck squamous cell carcinoma to assess their response to innovative therapies. BMC Cancer, 23, 223.
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Publication 2023
Acetylcysteine Antibodies, Blocking Antigens Biological Assay Caspase 3 CD8-Positive T-Lymphocytes Cells Cell Survival Coculture Techniques Cultured Cells Culture Media Cytokinesis Extracellular Matrix Immunotherapy Luminescence lysosomal-associated membrane protein 1, human Nivolumab Patients pembrolizumab Pharmaceutical Preparations Pharmacotherapy Poly(ADP-ribose) Polymerase Inhibitors Promega Squamous Cell Carcinoma of the Head and Neck T-Lymphocyte Tissue, Membrane Y 27632
5
Western Blot Analysis of Cellular Markers

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Publication 2023
Aggrecans Antibodies BCL2 protein, human Biological Assay Buffers Caspase 3 Cells Centrifugation Chemiluminescence Cold Temperature Collagen Goat Mitogen-Activated Protein Kinase 3 MMP2 protein, human MMP3 protein, human MMP13 protein, human Mus NFE2L2 protein, human polyvinylidene fluoride Proteins Rabbits Radioimmunoprecipitation Assay SDS-PAGE SOD2 protein, human SOX9 protein, human Super C resin Tissue, Membrane

Top products related to «Caspase 3»

1
Cleaved caspase 3 by Cell Signaling Technology
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Cleaved caspase-3 is an antibody that detects the activated form of caspase-3 protein. Caspase-3 is a key enzyme involved in the execution phase of apoptosis, or programmed cell death. The cleaved caspase-3 antibody specifically recognizes the active, cleaved form of the enzyme and can be used to monitor and quantify apoptosis in experimental systems.
2
Caspase 3 by Cell Signaling Technology
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Caspase-3 is a key enzyme involved in the execution phase of cell apoptosis (programmed cell death). It plays a central role in the apoptotic pathway by cleaving various cellular substrates, leading to the characteristic morphological and biochemical changes associated with apoptosis.
3
Anti cleaved caspase 3 by Cell Signaling Technology
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Anti-cleaved caspase-3 is a lab equipment product that detects the cleaved form of caspase-3, a key executioner caspase involved in apoptosis.
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Bcl 2 by Cell Signaling Technology
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Bcl-2 is a protein that plays a key role in regulating apoptosis, or programmed cell death. It functions as an anti-apoptotic protein, helping to prevent cell death by inhibiting the activity of pro-apoptotic proteins.
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β-actin is a cytoskeletal protein that is ubiquitously expressed in eukaryotic cells. It is an important component of the microfilament system and is involved in various cellular processes such as cell motility, structure, and integrity.
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GAPDH is a protein that functions as an enzyme involved in the glycolysis process, catalyzing the conversion of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. It is a common reference or housekeeping protein used in various assays and analyses.
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β actin by Merck Group
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β-actin is a protein that is found in all eukaryotic cells and is involved in the structure and function of the cytoskeleton. It is a key component of the actin filaments that make up the cytoskeleton and plays a critical role in cell motility, cell division, and other cellular processes.

More about "Caspase 3"

Caspase-3, also known as apopain, is a crucial enzyme in the apoptosis (programmed cell death) pathway.
As a cysteine-aspartic acid protease, it plays a central role in the execution phase of cell apoptosis, responsible for the proteolytic cleavage of many key cellular proteins.
This ultimately leads to the characteristic morphological and biochemical changes observed in cells undergoing apoptosis.
Caspase-3 is considered a key mediator of apoptosis in mammalian cells and has been extensively studied as a potential therapeutic target for various diseases, including cancer, neurodegenerative disorders, and autoimmune conditions.
Understanding the regulation and activation of Caspase-3 is crucial for developing effective interventions to modulate cell death pathways.
Closely related terms include Cleaved caspase-3, Anti-cleaved caspase-3, Bcl-2, Bax, and GAPDH, which are all involved in the apoptotic process or serve as important markers.
Researchers can leverge AI-driven insights from PubCompare.ai to optimize their Caspase-3 research protocols for reproducibility and accuracy, ensuring confidence in their findings and advancing the field of cell death studies.