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Caspase 1

Caspase 1 is a cysteine protease enzyme that plays a crucial role in the innate immune response and inflammation.
It is responsible for the proteolytic activation of the proinflammatory cytokines interleukin-1 beta and interleukin-18, and is involved in the process of pyroptosis, a form of programmed cell death.
Caspase 1 is implicated in the pathogenesis of various inflammatory and autoimmune disorders, as well as in the host defense against microbial infections.
Optimizing Caspase 1 research with PubCompare.ai's AI-driven protocol comparison can help researchers easily locate the best protocols from literature, preprints, and patents, ensuring reproducible and accurate results.
Leveraging AI to identify the optimal products and methodologies for Caspase 1 experiments can improve research outcomes and advance our understanding of this important enzyme.

Most cited protocols related to «Caspase 1»

1
Caspase-1 Regulates Alzheimer's Pathology
Cited 27 times
Caspase-1 activation of human and mouse brain tissue were analyzed by Western blot of cleaved caspase-1. IL-1β was quantified by ELISA. Microglial ASC speck formation was detected by immunohistochemistry. All mice were on C57/Bl6 background, including WT, NLRP3−/−,27 (link), APP/PS15 (link), APP/PS1/NLRP3−/−, Caspase-1−/−,28 (link), APP/PS1/Caspase-1−/− and were analyzed for cognitive function using the Morris Water Maze, the object recognition test and open field behavioural testing. Synaptic plasticity was determined by measuring long term potentiation (LTP) in acutely isolated hippocampal slices. Spine density was assessed by analyzing mid apical dendritic sections of pyramidal CA1 neurons. Cerebral Aβ load was determined by thioflavin-S-histochemistry of serial sections. Sequential extraction of homogenized brains by radio-immunoprecipitation assay, sodium dodecyl sulfate buffer and formic acid was employed to determine Aβ levels. Aβ nitration was determined by ELISA and immunohistochemistry using a specific antibodies against 3NTyr10 (link)-Aβ25 (link). Western blot detection was used to analyze the protein levels of APP, CTFs, Aβ, BACE1, IDE and NOS2. Inflammasome activation was confirmed by detection of ASC speck formation in microglia isolated from adult mouse. Microglial Aβ phagocytosis was determined after peripheral injection of methoxy-XO4, isolation of microglia and subsequent FACS analysis. Confirmatory immunocytochemistry was performed using antibody IC16 and the lysosomal marker LAMP2. Plaque morphology and microglial Aβ uptake was analyzed by coimmunostaining with Iba-1, methoxy-XO4 and IC16. mRNA levels of IDE, NEP, M1 and M2 markers were determined either from sorted microglia or from brain tissue by qPCR.
Heneka M.T., Kummer M.P., Stutz A., Delekate A., Schwartz S., Saecker A., Griep A., Axt D., Remus A., Tzeng T.C., Gelpi E., Halle A., Korte M., Latz E, & Golenbock D. (2012). NLRP3 is activated in Alzheimer´s disease and contributes to pathology in APP/PS1 mice. Nature, 493(7434), 674-678.
Publication 2012
Adult Antibodies BACE1 protein, human Biological Assay Brain Buffers Caspase 1 Cognition Dendrites Enzyme-Linked Immunosorbent Assay formic acid Histocytochemistry Homo sapiens Immunocytochemistry Immunoglobulins Immunohistochemistry Immunoprecipitation Inflammasomes Interleukin-1 beta isolation LAMP2 protein, human Long-Term Potentiation Lysosomes Mice, Laboratory Microglia Morris Water Maze Test Neuronal Plasticity Nitrates Nitric Oxide Synthase Type II Phagocytosis Proteins Pyramidal Cells RNA, Messenger Senile Plaques Sulfate, Sodium Dodecyl thioflavine Tissues Vertebral Column Western Blotting
2
NALP3 Inflammasome Activation Assay
Cited 25 times
THP-1, or immortalized WT or NALP3−/− macrophages were attached to 35 mm 6-well plates. Cells were then transfected with siRNA oligonucleotides (50 nM) for 24 h using Lipofectamine 2000 in 2 ml of SF OPTI-MEM® I. The following day, cells were washed with SF OPTI-MEM® I and then transfected with poly (dA:dT) (1 µg/ml) for 6 hours with Lipofectamine 2000 in 2 ml of SF OPTI-MEM® I. The culture supernatants and cells were separated and then processed for immunoblot analysis with anti-caspase-1 and anti-IL-1β specific antibodies.
Full Methods and any associated references are available in the online version of the paper at www.nature.com/nature.
Fernandes-Alnemri T., Yu J.W., Wu J., Datta P, & Alnemri E.S. (2009). AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature, 458(7237), 509-513.
Publication 2009
Anti-Antibodies Caspase 1 Cells Immunoblotting Interleukin-1 beta lipofectamine 2000 Macrophage Oligonucleotides Poly A RNA, Small Interfering
3
Caspase-1 and IL-1β Activation Assay
Cited 21 times
Cell culture supernatants were precipitated by adding an equal volume of methanol and 0.25 volumes of chloroform, vortexed and centrifuged at 20.000 × g for 10 min. The upper phase was discarded and 500 µl of methanol was added to the interphase. This mixture was centrifuged at 20.000 × g for 10 min and the protein pellet dried at 55 °C, resuspended in Laemmli buffer and boiled at 99°C for 5 min. Samples were separated by SDS-PAGE (15%) and transferred onto nitrocellulose membranes. As indicated, blots were incubated with rabbit polyclonal antibody to anti murine caspase-1 p10 (sc-514, Santa Cruz Biotechnology, Santa Cruz, CA), rabbit polyclonal anti human caspase-1 p10 (sc-515, Santa Cruz Biotechnology), rabbit polyclonal anti human cleaved IL-1β (Asp116) (Cell Signaling, Boston, MA) or rabbit polyclonal anti murine cathepsin B (R&D Systems, Minneapolis, MN).
Hornung V., Bauernfeind F., Halle A., Samstad E.O., Kono H., Rock K.L., Fitzgerald K.A, & Latz E. (2008). Silica crystals and aluminum salts mediate NALP-3 inflammasome activation via phagosomal destabilization. Nature immunology, 9(8), 847-856.
Publication 2008
Caspase 1 Cathepsin B Cell Culture Techniques Chloroform Homo sapiens Immunoglobulins Interleukin-1 beta Interphase Laemmli buffer Methanol Mus Nitrocellulose Proteins Rabbits SC 514 SDS-PAGE Tissue, Membrane
4
Inflammasome Activation Analysis by Flow Cytometry
Cited 16 times
Sester and colleagues performed an FCM method to detect ASC redistribution in myeloid cell defining speck formation by changes in fluorescence peak height and width [2156 (link), 2157 (link)]. This protocol permits to define the true activated inflammasome by assessment ASC speck formation, because until then the detection of inflammasome, activation was made by monitor its end products, IL-1β or IL-18, or activated caspase-1 detection. Notably different pathways can secrete IL-1β and the methods to analyze caspase-1 activity are not always specific, in both cases the outcomes could be inflammasome independent. Despite to ASC speck formation microscopy analysis, used in the past, this methodology is faster, more accurate, and sensitive. Recently a better method to analyze simultaneously ASC speck and caspase-1 activity was performed by Amnis ImageStreamX [2158 (link)]. This protocol eliminates false positive events detected by flow-cytometry method, by specific masks to select only single cell, excluding cells with nonspecific-like aggregation of ASC and also defining ASC speck size. Finally the study analyze the presence and distribution of active caspase-1, detected by FLICA spots, and ASC speck simultaneously, evaluating inflammasome activation.
In this section we show the analysis of inflammasome activation by FlowSight, performed utilizing ASC speck formation in LPS+Nig stimulated-THP1derived macrophage.
Cossarizza A., Chang H.D., Radbruch A., Acs A., Adam D., Adam-Klages S., Agace W.W., Aghaeepour N., Akdis M., Allez M., Almeida L.N., Alvisi G., Anderson G., Andrä I., Annunziato F., Anselmo A., Bacher P., Baldari C.T., Bari S., Barnaba V., Barros-Martins J., Battistini L., Bauer W., Baumgart S., Baumgarth N., Baumjohann D., Baying B., Bebawy M., Becher B., Beisker W., Benes V., Beyaert R., Blanco A., Boardman D.A., Bogdan C., Borger J.G., Borsellino G., Boulais P.E., Bradford J.A., Brenner D., Brinkman R.R., Brooks A.E., Busch D.H., Büscher M., Bushnell T.P., Calzetti F., Cameron G., Cammarata I., Cao X., Cardell S.L., Casola S., Cassatella M.A., Cavani A., Celada A., Chatenoud L., Chattopadhyay P.K., Chow S., Christakou E., Čičin-Šain L., Clerici M., Colombo F.S., Cook L., Cooke A., Cooper A.M., Corbett A.J., Cosma A., Cosmi L., Coulie P.G., Cumano A., Cvetkovic L., Dang V.D., Dang-Heine C., Davey M.S., Davies D., De Biasi S., Del Zotto G., Cruz G.V., Delacher M., Bella S.D., Dellabona P., Deniz G., Dessing M., Di Santo J.P., Diefenbach A., Dieli F., Dolf A., Dörner T., Dress R.J., Dudziak D., Dustin M., Dutertre C.A., Ebner F., Eckle S.B., Edinger M., Eede P., Ehrhardt G.R., Eich M., Engel P., Engelhardt B., Erdei A., Esser C., Everts B., Evrard M., Falk C.S., Fehniger T.A., Felipo-Benavent M., Ferry H., Feuerer M., Filby A., Filkor K., Fillatreau S., Follo M., Förster I., Foster J., Foulds G.A., Frehse B., Frenette P.S., Frischbutter S., Fritzsche W., Galbraith D.W., Gangaev A., Garbi N., Gaudilliere B., Gazzinelli R.T., Geginat J., Gerner W., Gherardin N.A., Ghoreschi K., Gibellini L., Ginhoux F., Goda K., Godfrey D.I., Goettlinger C., González-Navajas J.M., Goodyear C.S., Gori A., Grogan J.L., Grummitt D., Grützkau A., Haftmann C., Hahn J., Hammad H., Hämmerling G., Hansmann L., Hansson G., Harpur C.M., Hartmann S., Hauser A., Hauser A.E., Haviland D.L., Hedley D., Hernández D.C., Herrera G., Herrmann M., Hess C., Höfer T., Hoffmann P., Hogquist K., Holland T., Höllt T., Holmdahl R., Hombrink P., Houston J.P., Hoyer B.F., Huang B., Huang F.P., Huber J.E., Huehn J., Hundemer M., Hunter C.A., Hwang W.Y., Iannone A., Ingelfinger F., Ivison S.M., Jäck H.M., Jani P.K., Jávega B., Jonjic S., Kaiser T., Kalina T., Kamradt T., Kaufmann S.H., Keller B., Ketelaars S.L., Khalilnezhad A., Khan S., Kisielow J., Klenerman P., Knopf J., Koay H.F., Kobow K., Kolls J.K., Kong W.T., Kopf M., Korn T., Kriegsmann K., Kristyanto H., Kroneis T., Krueger A., Kühne J., Kukat C., Kunkel D., Kunze-Schumacher H., Kurosaki T., Kurts C., Kvistborg P., Kwok I., Landry J., Lantz O., Lanuti P., LaRosa F., Lehuen A., LeibundGut-Landmann S., Leipold M.D., Leung L.Y., Levings M.K., Lino A.C., Liotta F., Litwin V., Liu Y., Ljunggren H.G., Lohoff M., Lombardi G., Lopez L., López-Botet M., Lovett-Racke A.E., Lubberts E., Luche H., Ludewig B., Lugli E., Lunemann S., Maecker H.T., Maggi L., Maguire O., Mair F., Mair K.H., Mantovani A., Manz R.A., Marshall A.J., Martínez-Romero A., Martrus G., Marventano I., Maslinski W., Matarese G., Mattioli A.V., Maueröder C., Mazzoni A., McCluskey J., McGrath M., McGuire H.M., McInnes I.B., Mei H.E., Melchers F., Melzer S., Mielenz D., Miller S.D., Mills K.H., Minderman H., Mjösberg J., Moore J., Moran B., Moretta L., Mosmann T.R., Müller S., Multhoff G., Muñoz L.E., Münz C., Nakayama T., Nasi M., Neumann K., Ng L.G., Niedobitek A., Nourshargh S., Núñez G., O’Connor J.E., Ochel A., Oja A., Ordonez D., Orfao A., Orlowski-Oliver E., Ouyang W., Oxenius A., Palankar R., Panse I., Pattanapanyasat K., Paulsen M., Pavlinic D., Penter L., Peterson P., Peth C., Petriz J., Piancone F., Pickl W.F., Piconese S., Pinti M., Pockley A.G., Podolska M.J., Poon Z., Pracht K., Prinz I., Pucillo C.E., Quataert S.A., Quatrini L., Quinn K.M., Radbruch H., Radstake T.R., Rahmig S., Rahn H.P., Rajwa B., Ravichandran G., Raz Y., Rebhahn J.A., Recktenwald D., Reimer D., e Sousa C.R., Remmerswaal E.B., Richter L., Rico L.G., Riddell A., Rieger A.M., Robinson J.P., Romagnani C., Rubartelli A., Ruland J., Saalmüller A., Saeys Y., Saito T., Sakaguchi S., de-Oyanguren F.S., Samstag Y., Sanderson S., Sandrock I., Santoni A., Sanz R.B., Saresella M., Sautes-Fridman C., Sawitzki B., Schadt L., Scheffold A., Scherer H.U., Schiemann M., Schildberg F.A., Schimisky E., Schlitzer A., Schlosser J., Schmid S., Schmitt S., Schober K., Schraivogel D., Schuh W., Schüler T., Schulte R., Schulz A.R., Schulz S.R., Scottá C., Scott-Algara D., Sester D.P., Shankey T.V., Silva-Santos B., Simon A.K., Sitnik K.M., Sozzani S., Speiser D.E., Spidlen J., Stahlberg A., Stall A.M., Stanley N., Stark R., Stehle C., Steinmetz T., Stockinger H., Takahama Y., Takeda K., Tan L., Tárnok A., Tiegs G., Toldi G., Tornack J., Traggiai E., Trebak M., Tree T.I., Trotter J., Trowsdale J., Tsoumakidou M., Ulrich H., Urbanczyk S., van de Veen W., van den Broek M., van der Pol E., Van Gassen S., Van Isterdael G., van Lier R.A., Veldhoen M., Vento-Asturias S., Vieira P., Voehringer D., Volk H.D., von Borstel A., von Volkmann K., Waisman A., Walker R.V., Wallace P.K., Wang S.A., Wang X.M., Ward M.D., Ward-Hartstonge K.A., Warnatz K., Warnes G., Warth S., Waskow C., Watson J.V., Watzl C., Wegener L., Weisenburger T., Wiedemann A., Wienands J., Wilharm A., Wilkinson R.J., Willimsky G., Wing J.B., Winkelmann R., Winkler T.H., Wirz O.F., Wong A., Wurst P., Yang J.H., Yang J., Yazdanbakhsh M., Yu L., Yue A., Zhang H., Zhao Y., Ziegler S.M., Zielinski C., Zimmermann J, & Zychlinsky A. (2019). Guidelines for the use of flow cytometry and cell sorting in immunological studies (second edition). European journal of immunology, 49(10), 1457-1973.
Publication 2019
Activation Analysis Caspase 1 Cells Exanthema Flow Cytometry Fluorescence Inflammasomes Interleukin-1 beta interleukin 18 protein, human Macrophage Microscopy Myeloid Progenitor Cells
5
Comparative Meta-analysis of Microarray Datasets
Cited 15 times
To make data extracted from different microarray datasets comparable, the analysis was conducted on raw data in R statistical environment (Additional file 1: Figure S1C-1, Table S1). Differential expression analysis of the experimental group versus the control group in each study was conducted using scripts modified from GEO2R [29 ]. Briefly, a design matrix was set up containing the samples that were to be compared. Differential expression was tested by lmFit and eBayes function from “limma” package [28 ]. P value was adjusted by the Benjamini-Hochberg method [30 ]. For each gene in each study, we then calculated the effect size using the effectsize function from “metaMA” package [31 (link)]. The unbiased effect size and its variance were combined across multiple studies using the directEScombi function. P value was calculated from the combined statistics using normal distribution and adjusted by Benjamini-Hochberg method [30 ]. To calculate the combined fold change for each gene, we meta-analyzed the fold change across studies by inverse variance weighting method using metagen function from “meta” package [32 ].
Venn analysis was performed in R statistical environment using the package “Venn Diagram” to analyze Casp1-regulated gene expression among different tissues (Additional file 1: Figure S1C-2). Heat maps and scatter plots were made using statistical tools provided by the R and Bioconductor projects. Statistical significance in this study was set at p < 0.05. Meta-analysis was used to directly compare datasets derived from different microarray datasets. FC/FC ((FC) fold change) scatter plots were used to determine whether caspase−/−-regulated genes could cooperate with genes regulated by IL-1β, IL-18, or Sirt1 as was previously described (from herein referred as cooperation analysis) [33 (link)] (Additional file 1: Figure S1C-3). For microarray datasets extracted from caspase-1−/− liver and adipose tissue, direct cooperation analyses without the precedent meta-analyses were performed to determine whether the caspase-1 regulatory genes cooperate with IL-1β, IL-18, and Sirt-1 regulatory genes (Additional file 1: Figure S1C-4).
Li Y.F., Nanayakkara G., Sun Y., Li X., Wang L., Cueto R., Shao Y., Fu H., Johnson C., Cheng J., Chen X., Hu W., Yu J., Choi E.T., Wang H, & Yang X.F. (2017). Analyses of caspase-1-regulated transcriptomes in various tissues lead to identification of novel IL-1β-, IL-18- and sirtuin-1-independent pathways. Journal of Hematology & Oncology, 10, 40.
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Publication 2017
Caspase Caspase 1 Gene Expression Genes Genes, Regulator Interleukin-1 beta interleukin 18 protein, human Microarray Analysis Microtubule-Associated Proteins Sirtuin 1 Sirtuins Tissue, Adipose Tissues

Most recents protocols related to «Caspase 1»

1
Western Blot Analysis of Cellular Signaling
After the LPS and oridonin treatment for 24 h, cells from each group were collected and lysed on ice for 20 min by adding RIPA lysate (Solarbio). Next, the lysed cells were centrifuged at 10,000 rpm, 4 °C for 15 min to collect proteins and the protein concentrations were detected through a BCA kit (Solarbio). There was 30 μg of protein taken and denatured at 95 °C for 15 min with addition of the protein loading buffer. Later, the protein bands were separated by SDS PAGE electrophoresis, and then the protein was transferred to PVDF membranes and blocked in 5% skimmed milk blocking solution for 1–3 h. Subsequently, the membranes were washed three times in TBST buffer and then incubated overnight at 4 °C on a shaker with the addition of diluted primary antibodies (p65, ab16502, Abcam; p-p65, ab76302, Abcam; NLRP3, ab263899, Abcam; Caspase-1, ab138483, Abcam; GRP78, ab21685, Abcam; CHOP, #5554, CST; ATF4, ab184909, Abcam; ATF6, ab122897, Abcam; β-actin, ab6276, Abcam, UK). Afterwards, the membranes were washed with TBST twice, and diluted secondary antibody (Zhongshan Golden Bridge Biotechnology Co., Ltd., China) was added for 1-h incubation at ambient temperature. Again, the membranes were washed with TBST three times, and ECL hypersensitive luminescence solution (Solarbio) was added dropwise to develop the protein bands in a gel imager for photography. The protein bands were measured in grayscale employing Image J software and finally, the relative expression level of the target protein was analyzed with β-actin as an internal control.
Jiang J., Zhang N., Song H., Yang Y., Li J, & Hu X. (2023). Oridonin alleviates the inhibitory effect of lipopolysaccharide on the proliferation and osteogenic potential of periodontal ligament stem cells by inhibiting endoplasmic reticulum stress and NF-κB/NLRP3 inflammasome signaling. BMC Oral Health, 23, 137.
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Publication 2023
Actins activating transcription factor 6, human Antibodies ATF4 protein, human Buffers Caspase 1 Cells DDIT3 protein, human Electrophoresis Glucose Regulated Protein 78 kDa Hypersensitivity Immunoglobulins Luminescence Milk, Cow's oridonin polyvinylidene fluoride Proteins Protein Targeting, Cellular Radioimmunoprecipitation Assay SDS-PAGE Staphylococcal Protein A Tissue, Membrane
2
ChIP-seq Protocol for Transcription Factor Analysis
ChIP assays were performed using a kit following the manufacturer’s instructions (#17-295; Millipore). Accordingly, cells were first treated with 1% formaldehyde and incubated at 37°C for 10 min. Next, cells were washed twice with ice-cold PBS containing protease inhibitors. Cells were then scraped and pelleted by centrifugation at 2,000 RPM for 4 min at 4°C. Then, cells were resuspended in SDS Lysis Buffer (Millipore, #20-163) and incubated for 10 min on ice. After samples were centrifuged for 10 min at 13,000 RPM at 4°C, the supernatants were diluted 10 times by adding ChIP Dilution Buffer (#20-153; Millipore) containing protease inhibitors. The diluted supernatants were then treated with 75 μl of a 50% slurry of Protein-A Agarose/Salmon Sperm DNA (#16-157C; Millipore) at 4°C for 30 min with agitation. After centrifugation, supernatants were immunoprecipitated with antibodies against Smad4, Smad2, Smad3, Prdm16, GAPDH or isotype-matched control IgG and 60 μl of a 50% slurry of Protein-A Agarose/Salmon Sperm DNA at 4°C for 1 h with rotation. Agarose was pelleted using centrifugation at 1,000 RPM for 1 min at 4°C. The pellets were washed for 5 min in Low Salt Immune Complex Wash Buffer (#20-154; Millipore) once, High Salt Immune Complex Wash Buffer (#20-155; Millipore) once, LiCl Immune Complex Wash Buffer (#20-156; Millipore) once, and TE Buffer (#20-157; Millipore) twice. To amplify DNA bound to the immunoprecipitates, elution buffer (1% SDS, 0.1 M NaHCO3) was added to each sample followed by agitation and incubation for 15 min with rotation at room temperature. Eluates were then mixed with NaCl (final concentration of 0.2 M) and incubated for 4 h at 65°C followed by adding EDTA (0.01 M), Tris-HCl, pH 6.5 (0.04 M), and Proteinase K (0.04 mg/ml). Samples were then incubated for 1 h at 45°C, and DNA was recovered using phenol/chloroform extraction coupled with ethanol precipitation. Pellets were washed with 70% ethanol and air-dried. Lastly, pellets were resuspended in an appropriate buffer for PCR, and PCR products were analyzed on a 2% agarose gel. The immunoprecipitated DNA was also analyzed by qPCR using locus specific primers and normalized to input DNA. Relative fold enrichment in each locus was quantified relative to the control as described above (qRT-PCR) as well as in our published studies (Parajuli et al., 2018 (link); Zhang et al., 2015 (link)). The following primers were used: PRDM16-For 5′-CAT​CTC​CCC​AGC​ATT​GTC​AGT-3′; PRDM16-Rev 5′-GGA​GCG​CCG​AAC​ACG​GAA​TG-3′; JUNB-For 5′-GGC​AAA​GCC​CAG​GGT​CAA​TA-3′; JUNB-Rev 5′-AAA​GCT​AGT​AAG​CGG​CCT​GG-3′; GAPDH-For 5′-CGG​GAT​TGT​CTG​CCC​TAA​TTA​T-3′; GAPDH-Rev 5′-GCA​CGG​AAG​GTC​ACG​ATG​T-3′.
Hurwitz E., Parajuli P., Ozkan S., Prunier C., Nguyen T.L., Campbell D., Friend C., Bryan A.A., Lu T.X., Smith S.C., Razzaque M.S., Xu K, & Atfi A. (2023). Antagonism between Prdm16 and Smad4 specifies the trajectory and progression of pancreatic cancer. The Journal of Cell Biology, 222(4), e202203036.
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Publication 2023
5'-chloroacetamido-5'-deoxythymidine Antibodies Bicarbonate, Sodium Buffers Caspase 1 Cells Centrifugation Chloroform Cold Temperature Complex, Immune DNA Chips Edetic Acid Endopeptidase K Ethanol Formaldehyde GAPDH protein, human Immunoglobulin Isotypes Immunoprecipitation, Chromatin inhibitors MEL1S protein, human Oligonucleotide Primers Pellets, Drug Phenol Protease Inhibitors Salmo salar Sepharose SMAD2 protein, human SMAD3 protein, human SMAD4 protein, human Sodium Chloride Sperm Staphylococcal Protein A Technique, Dilution Tromethamine
3
Neuroinflammatory Profile in Cocaine Abstinence

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Publication 2023
Animals Biological Assay Brain Buffers Caspase 1 Cell Respiration Chemokine Cocaine Cold Temperature Cytokine Decapitation Growth Factor inhibitors Isoflurane Phosphoric Monoester Hydrolases Radioimmunoprecipitation Assay succinyl-trialanine-4-nitroanilide Tissues
4
Caspase-1 Activation Analysis in Living Cells
The activation of the enzyme was analyzed in living cells using the FAM-FLICA® Caspase 1 Assay kit (ImmunoChemistry Tech., Davis, CA) following the manufacturer’s instructions. Cells were labeled with the fluorescent inhibitor probe FAM-YVAD-FMK at the indicated times. After subsequent washes (to allow any unbound FAM-FLICA to diffuse out of cells), nuclei were stained with Hoechst 33,342 (1 μg/ml) for 10 min at 37 °C and cells were examined under a Zeiss Axiophot fluorescence microscope using a 40 × /1.3 N.A. objective. From each condition, 4 non-overlapping images from the top, middle and bottom areas were randomly taken. The number of green-positive and Hoechst-positive cells was determined by using the automated particle counting tool of ImageJ [34 (link)].
de Dios C., Abadin X., Roca-Agujetas V., Jimenez-Martinez M., Morales A., Trullas R., Mari M, & Colell A. (2023). Inflammasome activation under high cholesterol load triggers a protective microglial phenotype while promoting neuronal pyroptosis. Translational Neurodegeneration, 12, 10.
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Publication 2023
Biological Assay Caspase 1 Cell Nucleus Cells Enzyme Activation Fluorescent Probes Microscopy, Fluorescence tyrosyl-valyl-alanyl-aspartic acid fluoromethyl ketone
5
Caspase-1 Activation Analysis in Living Cells
The activation of the enzyme was analyzed in living cells using the FAM-FLICA® Caspase 1 Assay kit (ImmunoChemistry Tech., Davis, CA) following the manufacturer’s instructions. Cells were labeled with the fluorescent inhibitor probe FAM-YVAD-FMK at the indicated times. After subsequent washes (to allow any unbound FAM-FLICA to diffuse out of cells), nuclei were stained with Hoechst 33,342 (1 μg/ml) for 10 min at 37 °C and cells were examined under a Zeiss Axiophot fluorescence microscope using a 40 × /1.3 N.A. objective. From each condition, 4 non-overlapping images from the top, middle and bottom areas were randomly taken. The number of green-positive and Hoechst-positive cells was determined by using the automated particle counting tool of ImageJ [34 (link)].
de Dios C., Abadin X., Roca-Agujetas V., Jimenez-Martinez M., Morales A., Trullas R., Mari M, & Colell A. (2023). Inflammasome activation under high cholesterol load triggers a protective microglial phenotype while promoting neuronal pyroptosis. Translational Neurodegeneration, 12, 10.
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Publication 2023
Biological Assay Caspase 1 Cell Nucleus Cells Enzyme Activation Fluorescent Probes Microscopy, Fluorescence tyrosyl-valyl-alanyl-aspartic acid fluoromethyl ketone

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Gapdh by Cell Signaling Technology
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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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Nlrp3 by Cell Signaling Technology
Sourced in United States, China, United Kingdom
NLRP3 is a laboratory equipment product that functions as a sensor for detecting cellular stress and damage. It is involved in the activation of the inflammasome complex, which plays a role in the immune response. The NLRP3 product is used for research purposes to study cellular signaling pathways and immune system processes.
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Il 1β by Cell Signaling Technology
Sourced in United States, United Kingdom, China, Germany
IL-1β is a cytokine that plays a crucial role in the inflammatory response. It functions as a mediator of the innate immune system.

More about "Caspase 1"

Caspase 1, also known as IL-1β-converting enzyme (ICE), is a crucial player in the innate immune response and inflammation.
As a cysteine protease enzyme, it is responsible for the proteolytic activation of the proinflammatory cytokines interleukin-1 beta (IL-1β) and interleukin-18 (IL-18), which are central to the body's defense against microbial infections and the pathogenesis of various inflammatory and autoimmune disorders.
Caspase-1 is involved in the process of pyroptosis, a form of programmed cell death distinct from apoptosis.
This process is characterized by the rapid lysis of the cell, leading to the release of the cell contents and the subsequent activation of the immune response.
The NLRP3 (NLR family pyrin domain containing 3) inflammasome is a key regulator of Caspase-1 activation.
When the NLRP3 inflammasome is triggered by various stimuli, such as pathogen-associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs), it leads to the activation of Caspase-1, which in turn processes and releases IL-1β and IL-18.
Researchers studying Caspase-1 often utilize PVDF (polyvinylidene fluoride) membranes for Western blotting experiments to detect and quantify Caspase-1 protein levels.
Additionally, the TRIzol reagent is commonly used for RNA extraction, and RIPA lysis buffer is employed for protein extraction and purification.
The housekeeping gene GAPDH (glyceraldehyde 3-phosphate dehydrogenase) is frequently used as a loading control in these experiments.
Optimizing Caspase-1 research with PubCompare.ai's AI-driven protocol comparison can help researchers easily locate the best protocols from literature, preprints, and patents, ensuring reproducible and accurate results.
Leverageing AI to identify the optimal products and methodologies for Caspase-1 experiments can improve research outcomes and advance our understanding of this important enzyme.