Caspase 1

Manufactured by Genentech

Sourced in Switzerland

Caspase-1 is a laboratory enzyme that plays a key role in the process of programmed cell death, known as apoptosis. It functions as a cysteine protease, which means it can cleave and activate other proteins involved in the apoptotic pathway. Caspase-1 is an important tool for researchers studying cell death mechanisms and their implications in various biological processes and diseases.

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Lab products found in correlation

Alexa fluor 488 anti rabbit igg, by Thermo Fisher Scientific (2 mentions) F4 80 pe, by Thermo Fisher Scientific (2 mentions) B220 apc, by Thermo Fisher Scientific (2 mentions) Cd3 bv605, by BioLegend (2 mentions) Cd206 pe cy7, by BioLegend (2 mentions) Nf kb, by Cell Signaling Technology (2 mentions) Pnfkb, by Cell Signaling Technology (2 mentions) Tyrosine hydroxylase, by Cell Signaling Technology (2 mentions) Cd11b percp cy5, by Thermo Fisher Scientific (2 mentions) Cd11c apc efluor780, by Thermo Fisher Scientific (2 mentions) Fixable viability dye aqua cd45 bv711, by BD (2 mentions) F4 80 eflour450 f4 80 pe, by BD (2 mentions) Mhcii alexa fluor 700, by Thermo Fisher Scientific (2 mentions) Tubb3 alexafluor488, by BioLegend (2 mentions) Anti rabbit igg apc, by Thermo Fisher Scientific (2 mentions) Pvdf membrane, by Bio-Rad (1 mentions) Protease inhibitor cocktail, by Roche (1 mentions) Caspase 11, by Merck Group (1 mentions) Phospho cofilin, by Cell Signaling Technology (1 mentions) Calreticulin, by Stressgen (1 mentions)

Spelling variants of this product

Anti-caspase-1 (5 citations) Caspase 1 p20 (2 citations) Mouse caspase-1 (clone 4B4, (2 citations)

8 protocols using caspase 1

Western Blot Analysis of Apoptosis Signaling

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Cell lysates were prepared with an isotonic buffer (10 mM HEPES, 5 mM MgCl₂, 1 mM EGTA, 142 mM KCl with NP-40), in the presence of complete, EDTA-free, protease inhibitor cocktail (Roche). Samples were clarified, denatured with SDS buffer, and boiled. Proteins were separated by SDS-PAGE and then transferred to a polyvinylidene fluoride (PVDF) membrane (Biorad). Blots were probed with antibodies against caspase-11 (Sigma), caspase-1 (Genentech), phospho-cofilin, cofilin, Rac/Cdc42, and phospho-Rac (Cell Signaling), actin (Abcam), calreticulin (Stressgen). Detection was achieved using appropriate secondary antibodies conjugated with horseradish peroxidase (HRP), as previously described12 (link)14 (link)22 (link)79 (link).

Caution K., Gavrilin M.A., Tazi M., Kanneganti A., Layman D., Hoque S., Krause K, & Amer A.O. (2015). Caspase-11 and caspase-1 differentially modulate actin polymerization via RhoA and Slingshot proteins to promote bacterial clearance. Scientific Reports, 5, 18479.

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Genetically Modified Mouse Strains

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C57BL/6J and Rag1^−/− mice were purchased from the Biological Resource Center (Agency for Science, Technology and Research, A^*STAR, Singapore). B6.SJL-PtprcaPepcb/BoyJ (CD45.1⁺) mice were purchased from The Jackson Laboratory (USA). Nlrp3^tm1Tsc (Nlrp3^−/−) mice were provided by the University of Lausanne (Switzerland), Pycard^tm1Vmd (Asc^−/−) and Caspase1^−/− (Casp-1^−/−) mice were obtained from V. M. Dixit (Genentech). Age-matched and gender-matched wild-type mice were used in all experiments. All animals were congenic on a C57BL/6J background and were maintained at the Biological Resource Center (A^*STAR) under specific pathogen-free conditions. All experimental procedures were approved by the Institutional Animal Care and Use Committee (IACUC) of the Biological Resource Center (BRC), A^*STAR in compliance with their Guidelines for Animal Experiments.

Javanmard Khameneh H., Leong K.W., Mencarelli A., Vacca M., Mambwe B., Neo K., Tay A., Zolezzi F., Lee B, & Mortellaro A. (2019). The Inflammasome Adaptor ASC Intrinsically Limits CD4+ T-Cell Proliferation to Help Maintain Intestinal Homeostasis. Frontiers in Immunology, 10, 1566.

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Comprehensive Immunophenotyping of Adipose Tissue

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For flow cytometry analysis, the following antibodies were used: Fixable Viability Dye Aqua; CD45-BV711 (30F11: cat#563709) (BDBioscience); F4/80-eFlour450; F4/80-PE (BM8; cat#48-4801-82 & 12-4801-82); CD11b-PerCPCy5.5 (M1/70; cat#45-0112-82); CD11c-APC-eFluor780 (N418; cat#47-0114-82); B220-APC (RA3-6B2; cat#17-0452-82); MHCII-Alexa Fluor 700 (M5/114.15.2; cat#56-5321-82) (eBioscience) and CD3-BV605 (17A2; cat#100237); CD206-PECy7 (C068C2; cat#141709) (Biolegend). For western blot analysis, the following antibodies were used: pHSL (Ser660; cat#4126), pHSL (Ser563; cat#4139), HSL (cat#4107), ATGL (cat#2439), Actin (cat#4967), UCP-1 (cat#14670), p NFkB (cat#3033), NFkB (cat#8242), (Cell Signaling), Caspase-1 (Genentech). For whole mount staining: F4/80-PE (BM8; 12-4801-82; eBioscience), TUBB3-AlexaFluor488 (TUJ1; cat#801203; Biolegend), Tyrosine hydroxylase (cat#2792; Cell Signaling), B220-APC (RA3-6B2; cat#17-0452-82; eBioscience), anti-rabbit IgG-APC (Jackson; cat# 111-136-144), anti-rabbit IgG-AlexaFluor 488 (cat#A11008; Life Technologies).

Camell C.D., Sander J., Spadaro O., Lee A., Nguyen K.Y., Wing A., Goldberg E.L., Youm Y.H., Brown C.W., Elsworth J., Rodeheffer M.S., Schultze J.L, & Dixit V.D. (2017). Inflammasome-driven catecholamine catabolism in macrophages blunts lipolysis in the aged. Nature, 550(7674), 119-123.

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Comprehensive Immunophenotyping of Adipose Tissue

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Antibody-Mediated Analysis of Cellular Signaling

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Antibodies specific for CD11b were from BD Biosciences; p-rpS6, rpS6, p-Akt^S473, p-Akt^T308, Akt, p-AMPK, AMPK, tubulin, mTOR, LC3A, p-cofilin, cofilin, caspase-11, and FLAG (Cell Signaling); caspase-1 (Genentech); HA (Abcam); CD40, CD80, and anti-rabbit IgG (Biolegend Pharmaceuticals); anti-goat and -rabbit (Alexa 647) IgG (Molecular Probes); Concanamycin A (Sigma-Aldrich); LimKi 3 and Jasplakinolide (EMD Calbiochem); Torin1(Tocris); rapamycin (Cell Signaling); IRDye680- and IRDy800-conjugated antibodies (anti-rabbit, anti-mouse) (LI-COR Biosciences); phalloidin and LysoSensor Yellow/Blue dextran (ThermoFisher); Streptavidin (PE) (Jackson ImmunoResearch); and FAM-FLICA caspase-1 assay kit (ImmunoChemistry Technologies). Antibodies specific to nucleosome (PL2-3), Smith (2.12.3), and CD16/32 (2.4G2) and L-cell media (LCM) for BMMφ differentiation were generated as previously described (13 (link)).

Monteith A.J., Vincent H.A., Kang S., Li P., Claiborne T.M., Rajfur Z., Jacobson K., Moorman N.J, & Vilen B.J. (2018). mTORC2 activity disrupts lysosome acidification in systemic lupus erythematosus by impairing caspase-1 cleavage of Rab39a. Journal of immunology (Baltimore, Md. : 1950), 201(2), 371-382.

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Comprehensive Cell Death Pathway Analysis

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Human recombinant TNF, BV6, GNE684, and GSK583 were all synthesized at Genentech. Emricasan was purchased from Selleck Chemicals (S7775), zVAD from ABclonal and LPS from InvivoGen (tlrl-3peLPS). The primary antibodies used were directed against: RIP1 (610459, BD Biosciences), pRIP1 S166 (#31122, Cell Signaling Technology (CST)), RIP3 (#15828, CST), pRIP3 (#91702, CST), MLKL (#MABc604, Millipore), pMLKL (#37333, CST), FADD (#05-486, Millipore), RIP2 (#22763, Santa Cruz), XIAP (M044-3, MBL, 66800-1-Ig, Proteintech), c-IAP2 (Genentech), c-IAP1/2 (#3400, R&D), caspase-1(Genentech), caspase-3 (#9661, 9662, CST), caspase-7(#9491, CST), caspase-8 (#8592, 9429, 4927, CST), caspase-11(#14340, CST), GSDMD (#50928, CST), IL-1b (AF-401-NA, R&D), JNK(#9252, CST), pJNK (#4668, CST), p65(#8242, CST), p-p65(#3033, CST), IkBa (#9242, CST), p-IkBa (#2859, CST), p38 (#9212, CST), p-p38 (#9211, CST), ERK (#4695, CST), p-ERK (#4370, CST), actin (A3853, Sigma), GapDH (#2118, CST), HSP90 (#4877, CST).

Witt A., Goncharov T., Lee Y.M., Kist M., Dohse M., Eastham J., Dugger D., Newton K., Webster J.D, & Vucic D. (2023). XIAP deletion sensitizes mice to TNF-induced and RIP1-mediated death. Cell Death & Disease, 14(4), 262.

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Genetically Engineered Mice for Immunology

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Wild-type C57BL/6 mice were obtained from Charles River UK. Conventional knockout mice were bred in-house at the animal facilities of the University of Cambridge (Home Office Project License No. 80/2572). Nlrp3^−/−, Pycard^−/−, and Caspase1/11^−/− mice on a C57BL/6 background were produced by Millennium Pharmaceuticals and obtained from Kate Fitzgerald, University of Massachusetts, Worcester, MA. Caspase1^−/− and Caspase11^−/− mice on a C57BL/6 background were provided by Genentech. TLR2/4^−/− mice on a C57BL/6 background were provided by Shizuo Akira, Osaka University, Osaka, Japan. Mice were backcrossed on a C57BL/6 background at least eight generations. All mice strains were bred independently and routinely genotyped to ensure maintenance of the correct genotype.

Barone D.G., Carnicer-Lombarte A., Tourlomousis P., Hamilton R.S., Prater M., Rutz A.L., Dimov I.B., Malliaras G.G., Lacour S.P., Robertson A.A., Franze K., Fawcett J.W, & Bryant C.E. (2022). Prevention of the foreign body response to implantable medical devices by inflammasome inhibition. Proceedings of the National Academy of Sciences of the United States of America, 119(12), e2115857119.

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Genetically Modified Mouse Lines

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All mice were on a C57BL/6 background. C57BL/6 WT mice, ASC-Citrine (B6.Cg-Gt(ROSA)26Sor^{tm1.1(CAG-Pycard/mCitrine}*^,-CD2*^)Dtg/J), caspase-1/11^−/− (B6N.129S2-Casp1^tm1Flv/J), TNF^−/− (B6;129S-Tnf^tm1Gkl/J), and IL-1R^−/− (B6.129S7-il1r1^tmlmx/J) mice were obtained from the Jackson laboratories (Bar Harbor, ME). TNF/IL-1R^−/− mice were generated by crossing the TNF^−/− with the IL-1R^−/− mice. IL-1β^−/− mice were previously generated and provided by Y. Iwakura (University of Tokyo). ASC^−/−, GSDMD^−/−, caspase-1^−/−, and caspase-11^−/− mice were previously generated and provided by Genentech. All mice were bred and maintained under specific pathogen-free conditions at an animal facility accredited by the American Association for the Accreditation of Laboratory Animal Care at Johns Hopkins and housed according to procedures described in the Guide for the Care and Use of Laboratory Animals (56 ).

Alphonse M.P., Rubens J.H., Ortines R.V., Orlando N.A., Patel A.M., Dikeman D., Wang Y., Vuong I., Joyce D.P., Zhang J., Mumtaz M., Liu H., Liu Q., Youn C., Patrick G.J., Ravipati A., Miller R.J., Archer N.K, & Miller L.S. (2021). Pan-caspase inhibition as a potential host-directed immunotherapy against MRSA and other bacterial skin infections. Science translational medicine, 13(601), eabe9887.

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