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
- 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 - - Source: PubMed
Publication date: 2026/10/05
Chen XiaoshiZou Chengyu - Receptor-interacting protein kinase 1 (RIPK1) mediates cell survival, inflammation, and cell death, and its kinase-independent scaffolding function drives tumor progression and therapeutic resistance, which cannot be eliminated by conventional RIPK1 kinase inhibitors. To overcome this limitation, we adopted proteolysis-targeting chimera (PROTAC) technology to achieve complete RIPK1 protein depletion. Through linker structural optimization with a rigid phenyl ring incorporation, we successfully identified a potent RIPK1 degrader, compound B11. In A375 and B16F10 melanoma cells, B11 exhibited robust RIPK1 degradation activity, with DC values of 4.48 nM and 4.61 nM, respectively, and a maximum degradation efficiency of 98% in both cell lines. Mechanistically, B11 induced VHL E3 ligase-dependent ubiquitination and proteasomal degradation of RIPK1, which ablated the kinase-independent scaffolding function and markedly sensitized melanoma cells to TNF-α-triggered cell death. In vivo studies verified that B11 significantly enhanced the efficacy of anti-PD-1 immunotherapy. Moreover, combined treatment with B11 and a STING agonist further improved antitumor efficacy. This work demonstrates that PROTAC-mediated RIPK1 degradation is a viable strategy to target undruggable scaffolding functions of RIPK1, providing a novel lead compound B11, encoded with KWGS-B11, and design paradigm for RIPK1-targeted anticancer drug development. - Source: PubMed
Publication date: 2026/09/29
Guo ShunxinTang MingzeYu PeiYang JingLin RuohuiZheng LongLuo ZhongwenJiang YuhanGuo XiaoWei FangyanWang XiaobingKong Lingyi