Rabbit anti mouse cleaved caspase 8

Manufactured by Cell Signaling Technology

Rabbit anti-mouse cleaved caspase-8 is a primary antibody that recognizes the cleaved form of caspase-8, a key enzyme involved in the apoptosis (programmed cell death) pathway. This antibody can be used to detect and study the activation of caspase-8 in mouse model systems.

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Lab products found in correlation

Lsm 710, by Zeiss (2 mentions) Supersignal west pico plus chemiluminescent substrate, by Thermo Fisher Scientific (1 mentions) Rabbit anti caspase 1 p10, by Santa Cruz Biotechnology (1 mentions) Mouse anti caspase 1, by Santa Cruz Biotechnology (1 mentions) Rabbit anti cleaved caspase 1, by Cell Signaling Technology (1 mentions) Rabbit anti gasdermin d, by Cell Signaling Technology (1 mentions) Rabbit anti phospho mlkl, by Cell Signaling Technology (1 mentions) Rabbit anti phospho ripk3, by Cell Signaling Technology (1 mentions) Mouse anti ripk1, by BD (1 mentions) Mouse anti β actin, by Santa Cruz Biotechnology (1 mentions) Goat anti mouse igg hrp, by Bio-Rad (1 mentions) Chemidoc mp imager, by Bio-Rad (1 mentions) β mercaptoethanol, by Thermo Fisher Scientific (1 mentions) Goat anti rabbit igg hrp, by Merck Group (1 mentions) Rabbit anti ripk3, by ProSci (1 mentions) Ab179515, by Abcam (1 mentions) Ab196436, by Abcam (1 mentions) Ab187091, by Abcam (1 mentions) Ab215203, by Abcam (1 mentions) Enhanced chemiluminescence luminescence reagent, by Meilun (1 mentions)

3 protocols using rabbit anti mouse cleaved caspase 8

Western Blot Analysis of Cell Apoptosis

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Cell lysates were obtained by lysing cells in 1% SDS lysis buffer containing 1% β-mercaptoethanol (Gibco). The lysates were immediately boiled for 10 min to minimize protein degradation. Supernatants were diluted in SDS buffer and boiled for 10 min prior to loading. Western blot analysis was performed using the following antibodies: rabbit anti-cleaved caspase-1 (89332S; Cell Signaling Technology), rabbit anti-gasdermin D (39754S; Cell Signaling Technology), rabbit anti-mouse cleaved caspase-8 (8592P; Cell Signaling Technology), mouse anti-RipK1 (610459; BD Biosciences), rabbit anti-RipK3 (2283; ProSci Inc), rabbit anti-phospho RipK3 (91702S; Cell Signaling Technology), rabbit anti-phospho MLKL (37333S; Cell Signaling Technology), rabbit anti-caspase-1 p10 (SC-514; Santa Cruz Biotechnology), mouse anti-caspase-1 (sc-56036; Santa Cruz Biotechnology), mouse anti-β-actin (SC-81178; Santa Cruz Biotechnology), goat anti-mouse IgG HRP (172-1011; Bio-Rad Laboratories Inc), and goat anti-rabbit IgG HRP (A6154; MilliporeSigma). The blots were subsequently detected by chemiluminescence with SuperSignal West Pico PLUS Chemiluminescent Substrate (Thermo Fisher Scientific Inc) on a ChemiDoc MP imager (Bio-Rad Laboratories Inc).

Cai D., Brickey W.J., Ting J.P, & Sad S. (2021). Isolates of Salmonella typhimurium circumvent NLRP3 inflammasome recognition in macrophages during the chronic phase of infection. The Journal of Biological Chemistry, 298(1), 101461.

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Western Blot Analysis of Apoptosis Markers

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Protein extracts were separated on 8–15% polyacrylamide gels and then transferred onto polyvinylidene difluoride (PVDF) membranes (MilliporeSigma, Burlington, MA, USA). After blocking nonspecific binding with 5% nonfat dry milk (Sangon Biotech Shanghai Co., Ltd.) membranes were probed with primary antibodies overnight at 4°C and incubated with ppropriate HRP-labeled secondary antibodies at room temperature for 1 h. Membranes were then visualized with an enhanced chemiluminescence luminescence reagent (Meilunbio). The intensities of the bands were determined by ImageJ Launcher broken symmetry software program (NIH, Bethesda, MD, USA). Following antibodies were used: rabbit anti-mouse cleaved caspase-8 (#8592; Cell Signaling Technology), rabbit anti caspase-8 (AC056; Beyotime), Phospho-RSK2 (Ser227) Rabbit mAb (#3556S; Cell Signaling Technology), PDK1 (D37A7) Rabbit mAb (#5662S; Cell Signaling Technology), Caspase-3 (D3R6Y) Rabbit mAb (#14220S; Cell Signaling Technology), Caspase-1 (D7F10) Rabbit mAb (#3866S; Cell Signaling Technology), Anti-MLKL (phospho S345) (ab196436; Abcam), Anti-MLKL (phospho S358) (ab187091; Abcam), Anti-pro Caspase-1 + p10 + p12 (ab179515; Abcam), Anti-GSDMD antibody (ab209845; Abcam), Anti-GSDMD antibody (ab225867; Abcam), Anti-cleaved N-terminal GSDMD (ab215203; Abcam), anti-beta-actin (bs-0061 R; Bioss).

Yuan H., Zhou L., Chen Y., You J., Hu H., Li Y., Huang R, & Wu S. (2023). Salmonella effector SopF regulates PANoptosis of intestinal epithelial cells to aggravate systemic infection. Gut Microbes, 15(1), 2180315.

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Histological Analyses of Intestinal Tissue

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For hematoxylin and eosin stainings, intact intestinal tissue was fixed for 24h in methacarn to preserve mucus and epithelial cells trapped inside the mucus. Tissue was paraffin embedded in a water free procedure, cut to 5μm and stained. For analysis of cleaved Caspase 8, GFP, propidium iodide and actin, intestinal tissue was sliced open and fixed in PLP buffer (0.05 M phosphate buffer containing 0.1 M L-lysine, pH 7.4, 2 mg/ml NaIO4 and 1%PFA). After fixation overnight, tissue was washed in phosphate buffer and immersed in 30% sucrose overnight. Tissue was frozen in OCT, cut and stained with 100nM actistain 488 phalloidin (cytoskeleton) followed by DAPI. For cleaved Caspase 8 staining, slides were blocked using 10% normal donkey serum in 0.1% Tween20, 100mMTrisHCl, 150mMNaCl, 0.5% blocking reagent (Perkin Elmer) for 30 minutes. Slides were stained with 1:400 rabbit anti-mouse cleaved caspase-8 (no. 8592; Cell Signaling Technology) for 60 followed by donkey anti rabbit alexa fluor 488 (JacksonImmunoReasearch) for 30 minutes, followed by DAPI. Slides were analyzed on a Zeiss LSM710 and GFP intensity was measured using imageJ software.

Rauch I., Deets K.A., Ji D.X., von Moltke J., Tenthorey J.L., Lee A.Y., Philip N.H., Ayres J.S., Brodsky I.E., Gronert K, & Vance R.E. (2017). NAIP-NLRC4 inflammasomes coordinate intestinal epithelial cell expulsion with eicosanoid and IL-18 release via activation of Caspase-1 and -8. Immunity, 46(4), 649-659.

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