RIPK1 antibody
- Known as:
- RIPK1 (anti-)
- Catalog number:
- orb31978
- Product Quantity:
- 5 ug(Trial size)
- 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
- To investigate the role of the RIPK1 inhibitor GFH312 in ischemic stroke and identify its potential mechanisms. - Source: PubMed
Liu ZeWu ShengjuSuo QianLiu ChangShi RubingYe JingKhan HaroonZhang Jing-YangTang YaohuiZhang ZhijunLi WanluZhou Fu-ShengYang Guo-Yuan - The innate immune system is the first line of defense against infection, using pattern recognition receptors to sense pathogens and abnormal host-derived nucleic acids. Among these, Z-DNA-binding protein 1 (ZBP1) and interferon gamma-inducible protein 16 (IFI16) are two important nuclear and cytosolic nucleic acid sensors attracting recent attention. These sensors play key roles in detecting abnormal nucleic acids from viruses, bacteria, and damaged host cells. They trigger downstream innate immune responses to regulate inflammation. Despite much progress, key questions remain about how they are exactly activated under infection stress, the complexity of their signaling networks, and their dual roles in protective immunity and pathological inflammation. This review summarizes the structural features of ZBP1 and IFI16, how they recognize ligands, and their interactions with key signaling molecules (including RIPK1, RIPK3, MLKL, and caspase-1). We then emphasize cell fate decisions mediated by these sensors. Especially, ZBP1 is the core upstream regulator of PANoptosis (an integrated form of programmed cell death combining pyroptosis, apoptosis, and necroptosis via the PANoptosome complex), alongside classical cell death pathways. In addition, we review recent advances to highlight functional roles of ZBP1 and IFI16 in herpesvirus, influenza virus, and bacterial infections, and their dysregulation in autoimmune diseases. For IFI16, human studies and murine homolog-based evidence are analyzed. Further we review unique and overlapping functions, including a comparison with other canonical nucleic acid sensors (e.g., cGAS, AIM2, RIG-I) and analyze the ADAR1-ZBP1 axis in self-nonself nucleic acid discrimination. We cover the therapeutic potential of targeting ZBP1- and IFI16-mediated pathways for anti-inflammatory and anti-infective strategies and provide a balanced analysis of developmental challenges, potential toxicity, and risks of impaired immune surveillance. - Source: PubMed
Publication date: 2026/09/22
Lu ChengbinXu BenmoXiong Yu - Cognitive decline in Parkinson's disease (PD), progressing from mild cognitive impairment (PD-MCI) to severe dementia (PD-D), is a debilitating core feature driven by complex neuropathological interactions. While α-synuclein accumulation is the disease's hallmark, co-pathologies involving amyloid-β and tau, alongside chronic neuroinflammation, are critical accelerators of cognitive collapse. This review positions the receptor for advanced glycation end products (RAGE) as a key molecular orchestrator bridging these disparate pathological events. Functioning as a multi-ligand sensor, RAGE binds proteotoxic aggregates (α-synuclein, amyloid-β, and tau) and damage-associated molecular patterns like HMGB1. We discuss how RAGE can drive early synaptic failure through four interconnected mechanisms: (1) triggering a "two-hit" hyperinflammatory microglial response along with TLRs; (2) initiating non-canonical intracellular neuroinflammation through RAGE-RIPK1 complex; (3) acting as a neurovascular gateway to actively transport peripheral amyloid-β and recruit circulating monocytes into the central nervous system; and (4) directly blocking long-term potentiation (LTP) and degrading dendritic spines prior to overt neuronal death. Furthermore, clinical evidence highlights the depletion of protective soluble RAGE (sRAGE) in dementia, reinforcing the prognostic value of the RAGE axis. By reframing RAGE as a convergence point for proteinopathy, neurovascular breakdown, and synaptic dysfunction, this review highlights its valuable translational potential. We conclude by exploring how selective interventions-such as RAGE-RIPK1 uncoupling peptides and sRAGE modulation-could effectively intercept the molecular cascades that precipitate dementia in prodromal PD cohorts. - Source: PubMed
Publication date: 2026/10/06
Peixoto Daniel OppermannGasparotto JucianoOjo Olajide RaymondAro Olayemi PhilemonGodswill Umin-Awaji Sundayde Abreu Luiza FrancoLopes Luana CarneiroMoreira José Claudio FonsecaGelain Daniel Pens - Receptor-interacting protein kinase 1 (RIPK1) plays a pivotal role in regulating cell survival and death, thereby exerting complex and multifaceted functions in the initiation and progression of cancer. Its expression is frequently dysregulated across diverse malignancies and correlates strongly with poor prognosis, highlighting its significance in the tumor microenvironment. The precise mechanisms through which RIPK1 modulates oncogenic processes, including cell death pathways, immune evasion, proliferation, migration, and drug resistance, remain incompletely elucidated, presenting both a challenge and an opportunity. This review summarizes the molecular mechanisms orchestrated by RIPK1, discusses its expression profiles across human cancers, and analyzes relevant regulatory networks. We also highlight recent advances in targeting RIPK1 therapeutically, focusing on emerging strategies such as small-molecule inhibitors and proteolysis-targeting chimera (PROTAC). We evaluate the translational potential of these agents, particularly in immunotherapy and chemosensitization. By synthesizing the multifaceted roles of RIPK1 in malignancy, this article hopes to identify novel therapeutic vulnerabilities for precision oncology. - Source: PubMed
Publication date: 2026/10/06
Luo JingyuSong ShuyaLi ZekunLiu TingtingCao KunGao FuLi XinDeng YuYang YanyongXu Ying - Triple-negative breast cancer (TNBC) cells face metabolic, proteotoxic and treatment-associated stress, but the mechanisms that determine how stressed cells dispose of intracellular cargo remain incompletely defined. We hypothesize that lysosomal stress shifts part of the autophagy-associated cargo burden from intracellular degradation towards extracellular release in small extracellular vesicle (sEV)-enriched fractions. The rationale integrates general evidence linking autophagy with EV biology with two model-specific observations: RIP1 involvement in Manzamine A-induced secretory autophagy in breast cancer cells and RASAL2-dependent modulation of Rab27a activity and autophagy-associated sEV release in MDA-MB-231 cells. These observations motivate the hypothesis but do not establish its generality across TNBC backgrounds or forms of lysosomal stress. We therefore regard RIPK1 as a candidate regulator whose role may depend on the stress context, whereas the RASAL2-Rab27a module is functionally supported but mechanistically unresolved. The model predicts that perturbing these components will alter time-resolved paired intracellular and extracellular measurements. A coordinated sequence of lysosomal and autophagic changes preceding vesicle-associated export, together with exclusion of cell-death-associated particle release, would support the model; stressor-restricted, arm-specific or injury-associated outcomes would require its revision. - Source: PubMed
Publication date: 2026/09/21
Liu YuanpengQi GuocuiWang AnjunHu Fengxiao