RIPK1 antibody
- Known as:
- RIPK1 (anti-)
- Catalog number:
- orb99213
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- RIPK1 antibody
Related genes to: RIPK1 antibody
- Gene:
- RIPK1 NIH gene
- Name:
- receptor interacting serine/threonine kinase 1
- Previous symbol:
- -
- Synonyms:
- RIP
- Chromosome:
- 6p25.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-07
- Date modifiied:
- 2015-11-17
Related products to: RIPK1 antibody
Related articles to: RIPK1 antibody
- Necroptosis is a regulated form of cell death that relies on receptor-interacting serine/threonine-protein kinase 3 (RIPK3) -mediated phosphorylation of mixed-lineage kinase domain-like pseudokinase (MLKL). This phosphorylation drives MLKL oligomerization and membrane translocation, eventually leading to plasma membrane rupture and the release of damage-associated molecular patterns (DAMPs). Here, we outline methods to induce necroptosis by activating signaling pathways through the tumour necrosis factor receptor 1, Toll-like receptors (TLR3/4), and the interferon receptor. All pathways converge on the core event of RIPK3 activation, which further phosphorylates the effector MLKL to execute cell death. Furthermore, we describe key techniques and optimized protocols for detecting necroptotic activity and validating it with specific inhibitors, providing a comprehensive overview of both induction and evaluation strategies in necroptosis research. - Source: PubMed
Publication date: 2026/05/02
Lu JieLu HaohaoHe Sudan - Z-DNA-binding protein 1 (ZBP1) senses Z-form nucleic acids to trigger cell death and inflammation via RHIM domain-mediated interactions with RIPK1 and RIPK3. Here we show that compared to mouse ZBP1 (mZBP1), human ZBP1 (hZBP1) possesses a heightened sensitivity for inducing cell death in cells across different species and potent tumor-killing effects in vivo. In contrast to mZBP1, which signals primarily through RIPK3, hZBP1-induced cell death depends on RIPK1 in a RIPK3-independent manner. Specifically, while the scaffold function of RIPK1 is required for hZBP1-mediated apoptosis, its kinase activity is indispensable for the execution of necroptosis. Unlike mZBP1, which primarily uses only its RHIM1 domain, hZBP1 requires all three RHIM domains (RHIM1, RHIM2, and RHIM3) to trigger cell death. We further identify the C-terminal RHIM2 and RHIM3 regions as the key determinant that confers hZBP1 high sensitivity and confirm that endogenous hZBP1 promotes RIPK1-dependent cell death under pathological conditions. Together, our findings reveal an intrinsic mechanistic divergence between human and murine ZBP1 signaling and highlight the limitations of translating preclinical findings in animal models to human therapeutic strategies targeting this pathway. - Source: PubMed
Publication date: 2026/07/11
Lu FeiTang LinghuanTian ZichaoTian JialiangFu YinghaoGao AnminDong HengChen JianxiangLu HuasongKim ChunLai DengmingZhou ChunHe JianfengTou JinfaLin JuanJiao Huipeng - Necroptosis is a lytic form of programmed cell death that requires activation of the RIPK1/3-MLKL complex and results in plasma membrane permeabilization. Although the protein components governing necroptosis are well defined, the lipid determinants of this process remain poorly understood. Here, we combined lipidomics, pharmacological perturbations of sphingolipid metabolism and functional assays to identify sphingolipid pathways that contribute to necroptotic cell death. Using a panel of small molecule inhibitors, we found that inhibition of acid sphingomyelinase (ASMase) with ARC39 restored cell viability and membrane integrity during necroptosis without altering canonical necroptotic signaling. Lipidomic analysis revealed that ARC39 treatment prevented ceramide accumulation in necroptosis, linking reduced ceramide levels to decreased membrane permeability. Interestingly, ARC39 treatment did not reduce total cellular levels of phosphorylated MLKL (pMLKL) nor its membrane association, suggesting that the observed decrease in membrane permeability arises downstream of MLKL activation. Instead, our findings support a model in which the reduction of ceramide levels impairs productive membrane interactions by pMLKL. Consistent with this interpretation, genetic knockdown of ASMase similarly resulted in increased cell viability, decreased membrane permeabilization, and decreased ceramide levels during necroptosis, further linking ceramide homeostasis to necroptotic membrane damage. Together, these results indicate that ASMase-derived ceramides are important for efficient MLKL-mediated membrane permeabilization in necroptosis. - Source: PubMed
Publication date: 2026/07/02
Pilapil Luis Agustin EChitkara ShwetaAtilla-Gokcumen G Ekin - Depression, a prevalent mental health disorder, has attracted increasing attention owing to its association with neuroinflammation. Receptor-interacting serine/threonine-protein kinase 1 (RIPK1) plays a crucial role in maintaining cellular and tissue homeostasis by regulating inflammatory responses and cell death signalling pathways, both of which are closely linked to various physiological and pathological processes. Accordingly, RIPK1 functions as an upstream kinase that modulates inflammation and cell death. Tumour necrosis factor-α (TNF-α), a key pro-inflammatory cytokine implicated in the pathogenesis of various human diseases, acts as a principal upstream activator of RIPK1. Accumulating evidence further indicates that RIPK1 may contribute to a detrimental neuroinflammatory environment in mental disorders such as depression. However, its specific regulatory role and underlying mechanisms in depression remain incompletely understood. This review first summarises current advances in understanding the molecular structure and biological functions of RIPK1, with particular emphasis on multiple cellular pathways associated with depression. Subsequently, it discusses the mechanisms by which RIPK1 participates in the pathological process of depression, including its role in neuroinflammation and synaptic plasticity. Finally, we outline the effects of RIPK1 inhibitors in animal models, which have been shown to prevent neuronal cell death and reduce neuroinflammation. Collectively, these findings suggest that targeting RIPK1 may represent a promising therapeutic strategy with potential for clinical translation, highlighting its value as a potential therapeutic target in depression. However, further work is still needed to bridge the gap between preclinical mechanisms related to the RIPK1 inflammatory pathway and their actual clinical efficacy. - Source: PubMed
Publication date: 2026/07/10
Chen Xiao-QunZhuang Yu-ChiGuan Wei - Necrostatin-1 (Nec-1), a widely used RIPK1 inhibitor and necroptosis probe, also suppresses ferroptosis, complicating distinction between these cell death pathways. Here, we show that the thiohydantoin moiety of Nec-1 reacts with hydroperoxides to form a sulfenic acid intermediate capable of trapping peroxyl radicals and inhibiting the lipid peroxidation (LPO) that drives ferroptosis. To investigate this mechanism, several analogs were synthesized and evaluated in the FENIX cell-free LPO assay. Anti-LPO activity was enhanced by increasing steric bulk or nucleophilicity around the thiocarbonyl, relocating the thiohydantoin methyl group, or introducing a fully conjugated linker between the thiohydantoin and indole rings. The fully conjugated analog of Nec-1 (dsaturated Nec-1 or dsNec-1) was isolated as a stable species from preparative reactions of Nec-1 and a hydroperoxide, suggesting it mediates Nec-1's antiferroptotic effects. Desaturated derivatives were, however, inactive against necroptosis, indicating that the Nec-1 scaffold is unsuitable for dual-pathway inhibitor development. - Source: PubMed
Publication date: 2026/07/10
Al-Farhan AmrNayal Onkar SPratt Derek A