Rabbit anti phospho ripk3

Manufactured by Cell Signaling Technology

Rabbit anti-phospho RIPK3 is a primary antibody that recognizes the phosphorylated form of the receptor-interacting serine/threonine-protein kinase 3 (RIPK3). RIPK3 is a key mediator of necroptosis, a form of programmed cell death. This antibody can be used to detect and study the activation of RIPK3 in various cellular and biological systems.

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Lab products found in correlation

Rabbit anti phospho mlkl, by Cell Signaling Technology (2 mentions) Mouse anti ripk1, by BD (2 mentions) Rabbit anti ciap2, by Cell Signaling Technology (1 mentions) Mouse anti gapdh, by Biotrend (1 mentions) Mouse anti ciap1, by Santa Cruz Biotechnology (1 mentions) Mouse anti caspase 8, by Enzo Life Sciences (1 mentions) Goat anti rabbit igg, by Abcam (1 mentions) Goat anti mouse igg, by Abcam (1 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 mouse cleaved caspase 8, by Cell Signaling Technology (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)

2 protocols using rabbit anti phospho ripk3

Comprehensive Western Blot Analysis of Cell Death Regulators

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Western blot analysis was performed as described previously [29] (link), using the following antibodies: rabbit anti-MLKL, rabbit anti-RIPK3, rabbit anti-phospho MLKL, rabbit anti-phospho RIKP1, rabbit anti-phospho RIPK3, rabbit anti-TNFR1, rabbit anti-cIAP2 (all from Cell Signaling), mouse anti-RIPK1 (BD Bioscience), mouse anti-GAPDH (BioTrend), rabbit anti-TRAIL-R1 (Abcam), rabbit anti-TRAIL-R2 (Millipore), rabbit anti-FasR, mouse anti-cIAP1 (all from Santa Cruz), mouse anti-Caspase-8 (Enzo). For detection, secondary antibodies goat anti-mouse IgG and goat anti-rabbit IgG (Abcam) conjugated to horseradish peroxidase and enhanced chemiluminescence were used (Amersham Bioscience).

Koch A., Jeiler B., Roedig J., van Wijk S.J., Dolgikh N, & Fulda S. (2021). Smac mimetics and TRAIL cooperate to induce MLKL-dependent necroptosis in Burkitt's lymphoma cell lines. Neoplasia (New York, N.Y.), 23(5), 539-550.

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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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