RIPK1 Antibody
- Known as:
- RIPK1 Antibody
- Catalog number:
- XW-7754
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- 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
- Chronic kidney disease (CKD) is a prevalent global health concern with a high worldwide prevalence rate. It is defined by a steady deterioration in renal function, which causes toxins and metabolic waste to build up and cause systemic problems and multi-organ failure. The development and progression of CKD are influenced by a number of pathogenic factors, such as diabetes mellitus, hypertension, glomerulonephritis, and exposure to nephrotoxic chemicals. However, the precise underlying mechanisms remain incompletely understood. Necroptosis, a well-studied form of regulated cell death, is primarily mediated by the receptor-interacting protein kinase 1 (RIPK1) and receptor-interacting protein kinase 3 (RIPK3) signaling complex. Understanding necroptosis provides new avenues for therapeutic modulation of cillnehronic kidney disease, linking regulated cell death to fibrosis and inflammation. RIPK3 expression is upregulated up to five-fold in experimental CKD models, underscoring its pathogenic significance. The definition, key molecular mechanisms, and most current advancements in pharmacological research pertaining to necroptosis are all comprehensively summarized in this article. This review provides mechanistic insights into necroptosis in CKD and highlights therapeutic targets for future translational research. - Source: PubMed
Publication date: 2026/04/27
Lu JiaweiWang YingCheng YalinZhou ShuyuanLiao YunqiangZeng JiqiangZhang ShanrongTang Yang - RIPK1 regulates the pathways in programmed cell death, and is closely associated with inflammatory and immune diseases. Based on the pharmacophore-based virtual screening, compound 15, a tetrahydropyrrolo[3,4-c]pyrrole-1,3-dione derivative, was identified as a hit of RIPK1 inhibitor with an IC value of 6.42 μM. Furthermore, a similarity searching was carried out to get more potent RIPK1 inhibitors. Among them, compound 21 showed obvious improvement in RIPK1 inhibitory activity with an IC value of 2.21 μM, accompanied with moderate anti-necroptosis activity in HT-29 cells (IC = 15.32 μM). Molecular dynamics (MD) simulations indicated that it probably functioned as a type III kinase inhibitor. - Source: PubMed
Zeng XinYu YanzhenWu YifanChen GengSheng Rong - Receptor-interacting protein kinase 1 (RIPK1) is a critical regulator of programmed cell death and is implicated in various pathological conditions, particularly in mediating tumor resistance to immune checkpoint inhibitors (ICBs). In this study, we have pioneered the development of a novel cereblon (CRBN)-recruiting RIPK1 degrader, , through systematic optimization of linker and CRBN ligand portion. demonstrates potent and selective RIPK1 degradation across cell lines, with rapid kinetics and sustained degradation over 72h post-washout. Functionally, RIPK1 degradation by significantly sensitized Jurkat cells to TNFα-induced apoptosis. Furthermore, exhibited favorable pharmacokinetics, including metabolic stability and an extended half-life. Strikingly, , a single dose of achieved durable RIPK1 degradation in xenograft tumors over 6 days. These findings underscore the potential of as a chemical probe for studying RIPK1 biology and a promising candidate for cancer treatment. - Source: PubMed
Publication date: 2026/04/14
Lu DongYu XinLin HanfengCheng RanZhang MinYang BinChen JingjingLi FengQi XiaoliWang Jin - Pulmonary fibrosis (PF) is a life-threatening interstitial lung disease characterized by scarring and inflammation in lung tissues. Aberrant activation of the JAK/STAT and NF-κB signaling pathways is critical in initiating and sustaining the inflammatory processes that drive fibrotic progression. In this study, we identify a novel small-molecule compound, T4015, a 4-indolyl-2-phenylaminopyrimidine derivative, as a dual-pathway inhibitor targeting both JAK/STAT and NF-κB signaling. Dual-luciferase reporter assays demonstrate the potent inhibitory activity of T4015 against these pathways. T4015 effectively suppresses the phosphorylation of STAT3, JAK1, and TYK2 induced by IL-6 and IFN-β, while suppressing LPS-induced NF-κB activation in macrophages. Transcriptome sequencing and pathway enrichment analyses further confirm that T4015 downregulates multiple inflammation-related signaling cascades, including the JAK/STAT, NF-κB, TNF, IL-17, and Toll-like receptor pathways. In a mouse model of bleomycin-induced PF, T4015 treatment significantly improves survival, attenuates collagen deposition, and reduces the expression of pro-inflammatory and profibrotic markers such as IL-6, CCL2, and COL1. Molecular docking and target prediction analyses suggest that T4015 exhibits strong binding affinity for multiple kinases within the JAK/STAT and NF-κB networks, including JAK1, TYK2, JAK2, JAK3, RIPK1, IRAK1/4, TAB1, and ZAP70. Collectively, these results highlight T4015 as a promising therapeutic candidate for PF through its simultaneous inhibition of the JAK/STAT and NF-κB signaling pathways. - Source: PubMed
Publication date: 2026/04/25
Zhang MinghuiXu HangLiu ShanXu XiaohanYin JiayiZhang XinxinZhang XiaonanYang XiaopingLiu XiaochunYin BinZhou MingmingWang LeweiZhang MengLiu HuiyingJiang WenqingSong QiaolingYang Jinbo - Recent studies have shown that cardiac glycosides can induce protective autophagy, but the precise mechanism is unclear. Our research focused on Toxicarioside H (ToxH), a newly discovered cardiac glycoside, to explore its ability to induce cytoprotective autophagy in triple-negative breast cancer (TNBC) cell lines and investigate the underlying mechanism. Cell growth and proliferation were measured using CCK-8 and EdU assays, while cell death was evaluated by flow cytometry and lactate dehydrogenase release assay. Autophagy and necroptosis markers were detected by Western blotting, and immunofluorescence was conducted for the autophagy marker LC3B and phosphorylated RIPK3 complex. Immunoprecipitation was used to detect the RIPK1/RIPK3 complex. Additionally, a mouse TNBC tumor model was established to assess the therapeutic effect of ToxH combined with CQ and the occurrence of autophagy and necroptosis. Our research showed that ToxH inhibited cell growth, increased cell death, and caused full autophagic flux in three TNBC cell lines. Co-treatment with CQ augmented ToxH's cytotoxicity both in vitro and in vivo. Autophagic degradation of the necroptosis-related proteins was observed in the TNBC cells treated with ToxH, as evidenced by the reduction of RIPK1/RIPK3 necrosomes and phosphorylated MLKL oligomers. This was restored by co-treatment with CQ. Autophagy and inhibition of necroptosis were also observed in TNBC tumor tissues. Our findings point to the conclusion that ToxH induces cytoprotective autophagy, leading to the breakdown of necrosomes and suppression of necroptosis in TNBC cells. Thus, a combination therapy involving ToxH and an autophagy inhibitor may be a potential treatment option for TNBC. - Source: PubMed
Publication date: 2026/04/23
Xiong WeiTan Guang-HongChen HengyuChen Ming-HuiWu Ri-HongDai Shu-ZhenSong TaoHe Gui-ShengZheng Wu-PingHuang Feng-Ying