RIPK1 antibody
- Known as:
- RIPK1 (anti-)
- Catalog number:
- orb75271
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- 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
- Tumor Necrosis Factor (TNF) is a key pro-inflammatory cytokine whose sensing by TNFR1 triggers gene activation or cell death induction. While TNF cytotoxicity can be beneficial during infections by supporting effective immune responses, its chronic or excessive induction is harmful and promotes inflammatory pathologies. Protective brakes, known as cell death checkpoints, normally repress TNF cytotoxicity and therefore constitute crucial safeguards against these diseases. Death by TNF mainly proceeds upon inactivation of a checkpoint by microbial effector proteins or pathological mutations. We previously identified lysosomal turnover of TNFR1 Complex II by TAX1BP1-mediated selective macro-autophagy as a brake on TNF cytotoxicity. Here, we propose an alternative mechanism that prevents TNF-induced RIPK1 kinase-independent apoptosis. We found that inhibiting the ESCRT machinery, HSC70 or TAX1BP1 interferes with the TNF-dependent targeting of activated CASPASE-8 into endosomal intralumenal vesicles (ILVs) and is associated with apoptosis induction. Furthermore, we identified TAX1BP1 and TNFR1 Complex II components as TNF-induced cargoes of extracellular vesicles, suggesting that exosomal release of TNFR1 Complex II serves as a parallel detoxification pathway to lysosomal turnover. Finally, we show that Salmonella Typhimurium and Mycobacterium tuberculosis effector proteins activate TNF cytotoxicity by inhibiting components of the ESCRT machinery involved in this detoxification process. - Source: PubMed
Publication date: 2026/08/25
Huyghe JonPriem DarioHaems AnneloreLippens LienDe Meyer MargauxDelanghe TomDondelinger YvesBruggeman IngeVandenabeele PeterEyckerman SvenHendrix AnBertrand Mathieu Jm - Alzheimer's disease is a multifactorial neurodegenerative disorder in which amyloid-β accumulation, tau pathology, neuroinflammation, synaptic dysfunction, vascular injury, and neuronal loss interact across multiple cellular compartments. Although amyloid and tau remain central to disease definition and biomarker staging, growing evidence indicates that inflammatory and regulated cell-death pathways actively shape disease progression. Receptor-interacting protein kinase 1 (RIPK1) has emerged as a context-dependent signaling checkpoint that links inflammatory signaling to cell-fate decisions. In its scaffold and ubiquitinated forms, RIPK1 supports TNFR1-associated NF-κB and MAPK signaling, whereas RIPK1 kinase activation can promote apoptosis and RIPK1-RIPK3-MLKL-dependent necroptosis when regulatory checkpoints fail. In Alzheimer's disease, RIPK1 signaling has been implicated in disease-associated microglial responses, impaired amyloid-β handling, astrocyte reactivity, tau-associated neuronal stress, neurovascular dysfunction, and necroptotic cell death. Here, we review the molecular regulation of RIPK1; evaluate evidence from human tissue, experimental models, and cellular systems; and discuss how RIPK1 may function as a convergence and amplification node linking amyloid-β, tau, neuroinflammation, and regulated cell death. We also examine the therapeutic rationale for targeting RIPK1, including CNS-penetrant inhibitors, biomarker challenges, timing of intervention, patient selection, and safety considerations. We propose that RIPK1 is an understudied pathway in Alzheimer's disease pathogenesis and that defining its cell-type-specific and stage-dependent functions will be essential to determine whether RIPK1 inhibition can be developed as a disease-modifying therapeutic strategy. - Source: PubMed
Publication date: 2026/09/18
Caccamo AntonellaLanza MarikaCasili GiovannaOddo Salvatore - Necroptosis is a regulated form of lytic cell death that plays important roles in inflammation, host defense, and disease. Central to this pathway is mixed lineage kinase domain-like protein (MLKL), the terminal effector responsible for membrane disruption. Upon phosphorylation by receptor-interacting protein kinase 3 (RIPK3), MLKL undergoes conformational changes, oligomerizes, and translocates to cellular membranes. Despite extensive study, however, the detailed molecular mechanism by which MLKL mediates necroptosis remains incompletely understood. Multiple models have been proposed, including pore formation, cation channel activity, and higher-order or amyloid-like assemblies, yet each is supported by limited and often indirect evidence. Notably, high-resolution structures of membrane-associated, active MLKL assemblies are still lacking, hindering a unified mechanistic understanding. In addition, emerging studies suggest that membrane permeabilization and terminal membrane rupture may be mechanistically distinct processes, potentially involving additional effectors such as SIGLEC12. In this review, we summarize current structural and mechanistic insights into MLKL, including its domain architecture, activation mechanisms, and species-specific divergence. We then evaluate competing models of MLKL-mediated membrane disruption and highlight key challenges and future directions. We emphasize the need to directly visualize the active, oligomeric MLKL assemblies in the membrane-bound state and to integrate structural, biochemical, and cellular approaches for a comprehensive understanding of MLKL-mediated membrane permeabilization. Resolving these questions will be essential for understanding necroptosis and for developing therapeutic strategies targeting MLKL-mediated cell death. - Source: PubMed
Publication date: 2026/09/23
Dreyer BrookeRuan Jianbin - Current pharmacotherapies for chronic kidney disease (CKD) are limited by adverse effects and a "one-target-one-drug" paradigm. Necroptosis is a key driver of renal deterioration, yet its regulatory network remains poorly defined. Modified Da-Huang-Fu-Zi Decoction (DHFZ) has shown clinical efficacy, although its underlying mechanism, particularly in relation to necroptosis, requires further clarification. - Source: PubMed
Publication date: 2026/09/20
Zhang SitengZhu WeikunHuang GuofangDai DinghuiHe ShiweiZhang Xikui - The therapeutic efficacy of ischemic stroke (IS) treatment is severely limited by insufficient accumulation of therapeutic agents within ischemic lesions and persistent secondary injury after ischemia-reperfusion. Herein, we report a cRGD-functionalized exosome-based nanoplatform that enhances ischemic lesion-associated accumulation and antioxidative neuroprotection for the treatment of IS. Neural stem cell-derived exosomes were functionalized with cyclic RGD peptides (cRGD) and subsequently loaded with Mn₃O₄ nanoparticles to construct a hybrid nanosystem (cRGD-Exo@Mn₃O₄). The engineered exosomes preserve intrinsic brain tropism, while cRGD modification promotes preferential accumulation in ischemic regions, potentially through interaction with αβ integrin that is upregulated in ischemic lesions. The incorporated Mn₃O₄ nanoparticles confer robust reactive oxygen species (ROS) scavenging capability, thereby mitigating oxidative stress in ischemic microenvironments. In vitro and in vivo studies demonstrate that cRGD-Exo@Mn₃O₄ exhibits enhanced accumulation in ischemic regions compared with non-modified counterparts. The nanosystem effectively attenuates oxidative stress and neuroinflammation, leading to reduced infarct volume, alleviation of cerebral edema, and improved neurological function in MCAO/R mice. Mechanistically, transcriptomic analysis suggests that the therapeutic effects are associated with modulation of inflammation-and cell death-related pathways, including suppression of the RIPK1/RIPK3/MLKL signaling cascade. Collectively, this study presents a rationally designed exosome-based nanoplatform integrating ischemic lesion-associated accumulation with ROS-scavenging capability. - Source: PubMed
Publication date: 2026/08/13
Deng XuXie XixiangZhou XingJiang LanfangZhu TaoSu RixiangChen ChunmeiChen WanChen Chunxia