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Caspase

Caspases are a family of cysteine-aspartic acid proteases that play essential roles in programmed cell death (apoptosis) and inflammation.
These enzymes are involved in the cleavage of key cellular proteins, triggering a cascade of events that lead to cell dismantling and removal.
Caspases are classified into initiator (e.g. caspase-8, -9) and effector (e.g. caspase-3, -6, -7) subtypes based on their function in the apoptotic pathway.
Dysregulation of caspase activity has been implicated in a wide range of diseases, including neurodegenerative disorders, autoimmune conditions, and cancer.
Reserch into caspase function and regulation is crucial for understanding cell death mechanisms and developing targeted therapies.
PubCompare.ai streamlines this important resarch by empowering scientists to quickly identify the most accurate and reproducible caspase protocols from the literature, preprints, and patents using advanced AI-powered tools.

Most cited protocols related to «Caspase»

1
Genetic Manipulation of Apoptosis Pathways in Mice
Cited 44 times
Mice with a deleted allele of caspase-8 were generated by germ line deletion of a previously-described caspase-8flox allele2 (link). RIPK3 deficient animals were obtained from Vishva Dixit21 (link). Genotypes were confirmed by tail snip PCR as previously described. For Jo2 injections, animals were injected via tail vein with 15µg purified Jo2 in LPS-free PBS per animal. Liver enzymes were assayed using a Trilogy Multi-Purpose Analyzer System from Drew Scientific, and liver sections were created and stained with hematoxylin and eosin, in the St Jude Veterinary Pathology Core facility. For SEB injections, 50µg SEB (Toxin Technology Inc.) per animal was injected via tail vein and T-cell populations were monitored by retro-orbital bleed and FACS as detailed previously. The St. Jude Institutional Animal Care and Use Committee approved all procedures in accordance with the Guide for the Care and Use of Animals.
Oberst A., Dillon C.P., Weinlich R., McCormick L.L., Fitzgerald P., Pop C., Hakem R., Salvesen G.S, & Green D.R. (2011). Catalytic activity of the caspase-8-FLIPL complex inhibits RIPK3-dependent necrosis. Nature, 471(7338), 363-367.
Publication 2011
Alleles Animals Caspase Caspase-8 Deletion Mutation Enzymes Eosin Genotype Germ Line Institutional Animal Care and Use Committees Liver Mus Population Group RIPK3 protein, human T-Lymphocyte Tail Toxins, Biological Veins
2
Genetic Manipulation of Apoptosis Pathways in Mice
Cited 43 times
Mice with a deleted allele of caspase-8 were generated by germ line deletion of a previously-described caspase-8flox allele2 (link). RIPK3 deficient animals were obtained from Vishva Dixit21 (link). Genotypes were confirmed by tail snip PCR as previously described. For Jo2 injections, animals were injected via tail vein with 15µg purified Jo2 in LPS-free PBS per animal. Liver enzymes were assayed using a Trilogy Multi-Purpose Analyzer System from Drew Scientific, and liver sections were created and stained with hematoxylin and eosin, in the St Jude Veterinary Pathology Core facility. For SEB injections, 50µg SEB (Toxin Technology Inc.) per animal was injected via tail vein and T-cell populations were monitored by retro-orbital bleed and FACS as detailed previously. The St. Jude Institutional Animal Care and Use Committee approved all procedures in accordance with the Guide for the Care and Use of Animals.
Oberst A., Dillon C.P., Weinlich R., McCormick L.L., Fitzgerald P., Pop C., Hakem R., Salvesen G.S, & Green D.R. (2011). Catalytic activity of the caspase-8-FLIPL complex inhibits RIPK3-dependent necrosis. Nature, 471(7338), 363-367.
Publication 2011
Alleles Animals Caspase Caspase-8 Deletion Mutation Enzymes Eosin Genotype Germ Line Institutional Animal Care and Use Committees Liver Mus Population Group RIPK3 protein, human T-Lymphocyte Tail Toxins, Biological Veins
3
High-content Imaging of Cell Response to Drugs
Cited 24 times
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
High-content Imaging of Cell Response to Drugs
Cited 23 times
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
5
Transcriptomic Analysis of Tumor Microenvironment
Cited 22 times
Genesets of interest were identified by the consortium and separated in five main groups, as detailed in Supplementary Table 9 and below:

ESTIMATE algorithm: method that uses gene expression signatures to infer the fraction of stromal and immune cells in tumor samples30 (link);

Curated signatures: upper and lower normal colon crypt compartments51 , epithelial and mesenchymal markers7 (link), WNT52 and MYC downstream target53 , epithelial-mesenchymal transition core genes and TGFβ pathway54 , intestinal stem cells55 , matrix remodeling (REACTOME) and wound-response (GO BP);

Canonical genesets: MAPK and PI3K (GO BP), SRC, JAK-STAT, caspases (BIOCARTA), proteosome (KEGG), Notch, cell cycle, translation and ribosome, integrin beta3, VEGF/VEGFR interactions (REACTOME);

Immune activation: immune response (GO BP), PD1 activation (REACTOME), infiltration with T cytotoxic cells (CD8)56 and T helper cells (TH1) in cancer samples57 ,58 , infiltration with Natural Killer (NK) cells59 and follicular helper T (TFH) cells60 in cancer samples, activation of T helper 17 (TH17) cells61 , regulatory T cells (Treg)62 or myeloid-derived suppressor cells (MDSC)63 ;

Metabolic activation: sugar, amino acid, nucleotide, glucose, pentose, fructose, mannose, starch, sucrose, galactose, glutathione, nitrogen, tyrosine, glycerophospholipid, fatty acid, arachnoid acid, linoleic acid (KEGG), glutamine (GO BP), lysophospholipid (PID).

Gene symbols were mapped to Entrez IDs to determine overlap in each individual data set that was evaluated for geneset enrichment. Geneset enrichment was tested for each subtype as compared to all other subtypes using the GSA64 method and was performed for each geneset by data set combination using two-class unpaired tests with 10,000 permutations. A single P value per geneset was computed - consolidated across data sets - using Fisher’s combined probability test.
Guinney J., Dienstmann R., Wang X., de Reyniès A., Schlicker A., Soneson C., Marisa L., Roepman P., Nyamundanda G., Angelino P., Bot B.M., Morris J.S., Simon I.M., Gerster S., Fessler E., de Sousa e Melo F., Missiaglia E., Ramay H., Barras D., Homicsko K., Maru D., Manyam G.C., Broom B., Boige V., Perez-Villamil B., Laderas T., Salazar R., Gray J.W., Hanahan D., Tabernero J., Bernards R., Friend S.H., Laurent-Puig P., Medema J.P., Sadanandam A., Wessels L., Delorenzi M., Kopetz S., Vermeulen L, & Tejpar S. (2015). The Consensus Molecular Subtypes of Colorectal Cancer. Nature medicine, 21(11), 1350-1356.
Publication 2015
Acids Activation, Metabolic Amino Acids Arachnoid Maters Carbohydrates Caspase Cell Cycle Cells CFC1 protein, human Colon Cytotoxic T-Lymphocytes Fatty Acids FLT1 protein, human Fructose Galactose Genes Glucose Glutamine Glutathione Glycerophospholipids Helper-Inducer T-Lymphocyte Integrin beta3 Intestines Linoleic Acid Lysophospholipids Malignant Neoplasms Mannose Mesenchyma Multicatalytic Endopeptidase Complex Myeloid-Derived Suppressor Cells Neoplasms Nitrogen Nucleotides Pentoses Phosphatidylinositol 3-Kinases Regulatory T-Lymphocytes Response, Immune Ribosomes Starch Stem, Plant Sucrose Transforming Growth Factor beta Transition, Epithelial-Mesenchymal Tyrosine Vascular Endothelial Growth Factors Wounds

Most recents protocols related to «Caspase»

1
Brain Sections Immunohistochemistry Protocol
Brain sections were co-stained for the expression of the oxidative stress
marker nitrotyrosine and the neuron-specific neuronal nuclear antigen
(NeuN), nitrotyrosine, and the astrocyte marker the glial fibrillary acidic
protein (GFAP) or the apoptotic marker cleaved caspase-3 and NeuN as
previously described.34 (link),35 (link),38 (link) Briefly,
free-floating sections were rinsed in phosphate-buffered saline (PBS) and
blocked in 1% horse serum in PBS containing .3% Triton X for 1 h. Sections
were then transferred in an antibody mixture containing rabbit
anti-nitrotyrosine polyclonal antibody (1:2500; Sigma, MO) and chicken
anti-GFAP polyclonal antibody (1:3000; Novus Biologicals, CO), rabbit
anti-nitrotyrosine polyclonal antibody (1:2500; Sigma, MO) and mouse
anti-NeuN monoclonal antibody clone, A60 (1:1500; Millipore/Sigma, MO) or
rabbit anti-cleaved caspase 3 polyclonal antibody (1:7500; Millipore, MA)
and mouse anti-NeuN monoclonal antibody clone, A60 (1:1500 Millipore/Sigma,
MO) and incubated at 4°C overnight. Sections were washed in PBS and
incubated in a mixture of corresponding secondary antibodies containing
Alexa Fluor 594 and Alexa Fluor 488 or Alexa Fluor 547 (1:2000; Invitrogen,
NY) for 1 h at room temperature. Sections were washed with PBS,
counterstained with 4,6-diamidino-2-phenylindole (DAPI), and mounted with an
anti-fade mounting medium (Vector Labs, CA).
Tchantchou F., Hsia R.C., Puche A, & Fiskum G. (2023). Hippocampal vulnerability to hyperhomocysteinemia worsens pathological outcomes of mild traumatic brain injury in rats. Journal of Central Nervous System Disease, 15, 11795735231160025.
Publication 2023
3-nitrotyrosine alexa fluor 488 Antibodies Antibodies, Anti-Idiotypic Antigens, Nuclear Apoptosis Astrocytes Biological Factors Brain Caspase Caspase 3 Clone Cells Cloning Vectors Equus caballus Immunoglobulins Monoclonal Antibodies Mus Neuroglia Neurons Novus Phosphates Saline Solution Serum
2
Cell Viability and Apoptosis Assay Protocol
Cell counts and viability were determined using either trypan-blue staining and manual counting or using the Luna FL automated cell counter (Logos Biosystems, France). Percentage cell viability was calculated by dividing live cells over the total cell count.
Apoptosis was measured using the CellEvent Caspase-3/7 green detection reagent (ThermoFisher Scientific, United Kingdom) according to manufacturer’s instructions. Pelleted cells (20,000) were suspended in reagent and incubated for 45 min at room temperature. Counterstaining was performed with Hoechst for 1 min after which cells were transferred into a cytofunnel (ThermoFisher Scientific) and spun onto a microscope slide using the Cytospin 4 (ThermoFisher Scientific) at 20,000 g for 8 min. Slides were air-dried and mounted using Mowiol aqueous mounting media. Images were taken with a Nikon Eclipse 80i fluorescent microscope at ×40 magnification. For each treatment, green fluorescent cells were considered positive for activated caspase-3/7. For each slide, the total number of caspase positive cells in ten representative fields of view were recorded and calculated as a percentage of the total cells (positive and negative).
Wodi C., Belali T., Morse R., Porazinski S, & Ladomery M. (2023). SPHINX-Based Combination Therapy as a Potential Novel Treatment Strategy for Acute Myeloid Leukaemia. British Journal of Biomedical Science, 80, 11041.
Full text: Click here
Publication 2023
Apoptosis Caspase Caspase 3 Cells Cell Survival Microscopy Trypan Blue
3
Quantitative RT-PCR Analysis of Stress Markers

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2023
BCL2 protein, human Biological Assay Caspase Caspase 3 Cells DNA, Complementary GA-Binding Protein Transcription Factor Oligonucleotide Primers Peroxide, Hydrogen Real-Time Polymerase Chain Reaction Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger SYBR Green I trizol
4
Assessing Liver Injury in Alcohol Use Disorder
Patients with AUD (n=66) were enrolled from April 2017 until January 2019 at St. Luc University Hospital, Brussels, Belgium, as described before.7 (link) The study protocol conforms to the ethical guidelines of the 1975 Declaration of Helsinki and was approved by the institution’s human research and ethical committee (Université Catholique de Louvain, Brussels, Belgium; B403201422657). Written informed consent was obtained from all patients and healthy volunteers.
Standard biochemical serum studies, including measurement of aspartate and alanine aminotransferases (AST, ALT), gamma-glutamyltransferase (GGT), alkaline phosphatase, were performed at the clinical laboratory associated with St. Luc University Hospital, Brussels, Belgium.7 (link) Serum caspase-cleaved and intact cytokeratin 18 (CK18-M65) was used to assess liver cell necrosis and apoptosis (CK18-M65 ELISA kit; TECO medical AG, Sissach, Switzerland).7 (link),18 (link),19 (link)
Fecal DNA extraction, sequencing, and analysis was performed as previously described and data presented in this study have been reanalyzed.7 (link) Raw sequences from ITS2 gene sequencing were registered previously at NCBI under BioProject PRJNA703732 (refer to https://www.ncbi.nlm.nih.gov/bioproject/?term=PRJNA703732), as described.7 (link)
Zeng S., Hartmann P., Park M., Duan Y., Lang S., Llorente C., Wang Y., Cabré N., Fouts D.E., Bacher P., Jung W.H., Stärkel P, & Schnabl B. (2023). Malassezia restricta promotes alcohol-induced liver injury. Hepatology Communications, 7(2), e0029.
Publication 2023
Alanine Transaminase Alkaline Phosphatase Apoptosis Aspartate Caspase Clinical Laboratory Services Cytokeratin 18 Enzyme-Linked Immunosorbent Assay Feces gamma-Glutamyl Transpeptidase Genes Healthy Volunteers Hepatocyte Homo sapiens Necrosis Patients Serum
5
qPCR Analysis of Apoptosis Regulators
The qPCR experiments were performed as described previously [19 (link), 20 (link)]. The total RNA (Ribonucleic Acid) of cells were extracted using the Trizol buffer (Beyotime) and were reverse-transcribed by Multiscribe™ Reverse Transcriptase (Applied Biosystems, Thermo Scientific Corporation) according to the manufacturer’s instructions. The relative expression was calculated by the comparative Ct method. The primers used for qPCR analysis were shown in Table 1.

The primers used in this work

TargetsPrimer sequence (5′–3′)
MMP-9Forward: 5′-GGGACGCAGACATCGTCATC-3′
Reverse: 5′-TCGTCATCGTCGAAATGGGC-3′
BaxForward: 5′-TGAAGCGACTGATGTCCCTG-3′
Reverse: 5′-CAAAGATGGTCACGGTCTGC-3′
Caspase-3Forward: 5′-CCTGGTTCATCCAGTCGCTT-3′
Reverse: 5′-TCTGTTGCCACCTTTCGGTT-3′
Bcl-2Forward: 5′-GTGAAGTCAACATGCCTGCC-3′
Reverse: 5′-ACAGCCTGCAGCTTTGTTTC-3′
Zhen H., Tian J., Li G., Zhao P., Zhang Y., Che J, & Cao B. (2023). Raltitrexed enhanced antitumor effect of anlotinib in human esophageal squamous carcinoma cells on proliferation, invasiveness, and apoptosis. BMC Cancer, 23, 207.
Full text: Click here
Publication 2023
Buffers Caspase Cells Oligonucleotide Primers RNA RNA-Directed DNA Polymerase trizol

Top products related to «Caspase»

1
Caspase glo 3 7 assay by Promega
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The Caspase-Glo 3/7 Assay is a luminescent-based assay that measures the activities of caspase-3 and caspase-7, two key enzymes involved in the execution phase of apoptosis. The assay utilizes a luminogenic caspase-3/7 substrate, which, upon cleavage by the enzymes, generates a glow-type luminescent signal that is proportional to the amount of caspase activity present in the sample.
2
Caspase glo 3 7 assay kit by Promega
Sourced in United States, United Kingdom, Germany, France
The Caspase-Glo 3/7 assay kit is a luminescent-based assay that measures the activity of caspase-3 and caspase-7 enzymes. The kit uses a proluminescent caspase-3/7 substrate, which can be cleaved by these enzymes, resulting in the release of a signal that is proportional to the amount of caspase activity present in the sample.
3
Apo one homogeneous caspase 3 7 assay by Promega
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The Apo-ONE® Homogeneous Caspase-3/7 Assay is a laboratory equipment product that measures the activity of caspase-3 and caspase-7 enzymes, which are important mediators of apoptosis or programmed cell death. The assay provides a simple, homogeneous method for quantifying caspase-3 and caspase-7 activity in cells.
4
Apo one homogeneous caspase 3 7 assay kit by Promega
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The Apo-ONE Homogeneous Caspase-3/7 Assay kit is a fluorometric assay designed to measure the activity of caspase-3 and caspase-7, two key enzymes involved in the process of apoptosis, or programmed cell death. The assay provides a sensitive and quantitative method for determining the extent of apoptosis in cell-based samples.
5
Caspase glo assay kit by Promega
Sourced in United States, Switzerland, Italy
The Caspase-Glo assay kit is a luminescent-based reagent system designed to measure caspase-3 and -7 activities in cell-based assays. The kit provides a luminogenic caspase-3/7 substrate, which is cleaved by these enzymes, resulting in the generation of a luminescent signal proportional to caspase-3/7 activities.
6
Caspase glo 3 7 assay system by Promega
Sourced in United States, Germany, France, Australia, Italy
The Caspase-Glo 3/7 Assay System is a luminescent assay that measures the activities of caspase-3 and caspase-7, two key executioner caspases involved in the process of apoptosis. The assay provides a quick and sensitive method for quantifying these caspase activities in cultured cells.
7
Caspase glo 3 7 by Promega
Sourced in United States, United Kingdom, Germany, France
Caspase-Glo 3/7 is a luminescent assay system that quantifies caspase-3 and caspase-7 activities in cultured cells. It provides a quick and simple method for determining the activities of these key apoptosis effector caspases.
8
Caspase glo assay by Promega
Sourced in United States, United Kingdom, Germany
The Caspase-Glo assay is a luminescent-based kit designed to measure caspase activity in cell-based assays. It provides a convenient way to quantify the activation of caspase enzymes, which are key mediators of apoptosis or programmed cell death.
9
Cellevent caspase 3 7 green detection reagent by Thermo Fisher Scientific
Sourced in United States, Germany, United Kingdom, Japan, Sweden, Italy
The CellEvent Caspase-3/7 Green Detection Reagent is a fluorogenic substrate for the detection of caspase-3 and caspase-7 activity in live cells. It consists of a four-amino acid peptide (DEVD) conjugated to a nucleic acid-binding dye. Upon cleavage by active caspase-3 and caspase-7, the dye is released and can bind to DNA, resulting in a bright green fluorescent signal.
10
Caspase glo by Promega
Sourced in United States, Germany, United Kingdom
Caspase-Glo is a luminescent assay system that measures caspase activity in cell-based apoptosis assays. The assay provides a homogeneous, plate-ready format that is designed to be sensitive, robust, and easy to use.

More about "Caspase"

Caspases are a family of cysteine-aspartic acid proteases that play essential roles in programmed cell death (apoptosis) and inflammation.
These enzymes, also known as cysteine-dependent aspartate-directed proteases, are involved in the cleavage of key cellular proteins, triggering a cascade of events that lead to cell dismantling and removal.
Caspases are classified into initiator (e.g., caspase-8, -9) and effector (e.g., caspase-3, -6, -7) subtypes based on their function in the apoptotic pathway.
Dysregulation of caspase activity has been implicated in a wide range of diseases, including neurodegenerative disorders, autoimmune conditions, and cancer.
Understanding the role of caspases in these pathological processes is crucial for developing targeted therapies.
Researchers can utilize various caspase assays, such as the Caspase-Glo 3/7 Assay, Apo-ONE® Homogeneous Caspase-3/7 Assay, and CellEvent Caspase-3/7 Green Detection Reagent, to measure caspase activity and monitor apoptosis in cell-based experiments.
PubCompare.ai streamlines caspase research by empowering scientists to quickly identify the most accurate and reproducible caspase protocols from the literature, preprints, and patents using advanced AI-powered tools.
This platform leverages artificial intelligence to help researchers make informed decisions and optimize their caspase studies with confidence, contributing to the understanding of cell death mechanisms and the development of novel therapies.