RIPK1 antibody
- Known as:
- RIPK1 (anti-)
- Catalog number:
- orb31978
- 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
- PANoptosis is a distinct inflammatory and lytic cell death pathway, orchestrated by the PANoptosome and executed through caspases and receptor-interacting protein kinases (RIPKs). Unlike other forms of programmed cell death, PANoptosis integrates components from multiple death signaling cascades. To date, several PANoptosome complexes - such as those nucleated by ZBP1, AIM2, RIPK1, and NLRP12 - have been characterized. These supramolecular assemblies form via domain-domain interactions upon detection of pathogen-associated or damage-associated signals. By eliminating infected and compromised cells, this coordinated pathway helps maintain tissue homeostasis, while its synchronized release of inflammatory cytokines and damage-associated molecular patterns (DAMPs) enhances innate immune responses, resulting in more effective pathogen clearance compared to any single cell death mechanism. Growing evidence underscores the relevance of PANoptosis across a spectrum of pathological conditions, including neurological disorders, infections, inflammatory diseases, cancer, and homeostatic imbalances, often mediated by PANoptosis-associated proteins. In neurological contexts - such as stroke, Parkinson's disease, Alzheimer's disease, and traumatic brain injury - PANoptosis activation correlates with disease progression and prognosis, highlighting its potential as a therapeutic target. In this review, we systematically outline the molecular foundations of PANoptosis, examine its role in neurological diseases, and summarize current pharmacological and methodological strategies for its modulation. A deeper understanding of PANoptosis may inform the identification of novel therapeutic targets for neurological disorders. - Source: PubMed
Publication date: 2026/07/10
Tang QiongyanXu MinminXiao XuemeiCao JingYang Weimin - Acute liver injury (ALI) is characterized by massive hepatocyte necrosis and rapid deterioration of liver function, which is closely associated with a cytokine storm mediated by the excessive activation of macrophages. Currently, there is a lack of effective targeted drugs in clinical practice. This study aimed to investigate the protective effects and mechanisms of protocatechualdehyde (PCA) against ALI. PCA exerts its biological effects by inhibiting macrophage-driven inflammation. The protective effects and mechanisms of PCA were experimentally validated using both in vivo and in vitro assays. In vivo, mice with ALI induced by lipopolysaccharide (LPS), acetaminophen (APAP), or carbon tetrachloride (CCl₄) showed reduced liver tissue damage, decreased serum transaminase levels, and downregulated inflammatory cytokine levels after PCA treatment, indicating that PCA protects against ALI induced by multiple causes. In vitro experiments further demonstrated that, within a safe concentration range, PCA significantly inhibit the expression of inflammatory cytokines in LPS-induced RAW264.7 cells and suppress necroptosis. Mechanistically, PCA functions through multiple pathways. It directly binds to RIPK1 to inhibit necroptosis in macrophages. Furthermore, it downregulates IFN-γ, subsequently blocking the JAK1/STAT1 signaling pathway and reducing the release of IL-17a and Ccl20. A reduction in these cytokines diminishes the infiltration of neutrophils and T cells, thereby improving the inflammatory milieu in ALI. In conclusion, PCA synergistically attenuates macrophage-driven inflammatory injury by inhibiting RIPK1-mediated necroptosis and regulating the IFN-γ/JAK1/STAT1 signaling axis, providing experimental evidence of its potential as a therapeutic agent for ALI. - Source: PubMed
Publication date: 2026/07/09
Hu ChuchuMiao YijiaYan WenjingJia MengyiZhang XiaoyaLi MengjuanSun XiaolongLiu ZiyiLi JunLi HaidiYang Yaru - Proteolysis-targeting chimeras (PROTACs) represent a revolutionary therapeutic strategy that achieves selective protein degradation through the ubiquitin-proteasome system, offering transformative potential for modulating programmed cell death (PCD) pathways. This review comprehensively examines the central role of PROTACs in regulating critical PCD mechanisms, including ferroptosis induction via GPX4 degradation, pyroptosis regulation through stimulator of interferon genes (STING) targeting, necroptosis modulation by MLKL/RIPK1 degradation, apoptosis activation through BCL-2/MDM2 elimination, and autophagy regulation via dual ubiquitin-proteasome and lysosomal pathways. These approaches effectively address the limitations of traditionally "undruggable" targets while demonstrating unique mechanistic properties and clinical promise. Currently, over 30 PROTAC candidates have entered clinical trials, including the estrogen receptor (ER) degrader ARV-471 for breast cancer and the IRAK4 degrader KT-474 for inflammatory diseases, both showing remarkable efficacy in overcoming drug resistance. While challenges remain in delivery systems, E3 ligase selectivity, and toxicity management, innovative technologies, such as nanocarriers, covalent PROTACs, and novel E3 ligases (e.g., RNF114) are advancing PROTAC applications in oncology, neurodegenerative disorders, and immune-related diseases. Future research will focus on optimizing molecular design, expanding the E3 ligase repertoire, and developing combination therapies. These efforts will establish PROTACs as groundbreaking solutions for intractable diseases, with their precise control of PCD pathways opening new therapeutic avenues. The technology's ability to selectively modulate cell death mechanisms positions it as a transformative approach in precision medicine. - Source: PubMed
Publication date: 2026/03/28
Huang HangqiDeng AoliPan FeifanLu YajuanChen LuluCao JinghaoTang QinLiu YingchaoWu YunyiDu JingLi YanchunTong Xiangmin - Proteolysis-targeting chimeras (PROTACs) have emerged as a transformative approach for targeted protein degradation (TPD). However, their therapeutic potential is limited by the scarcity of diverse E3 ligase ligands. Only a small fraction of more than 600 human E3 ligases are currently amenable to functional PROTAC development. To expand the E3 ligase toolbox, we developed RIPK1-Mediated Targeting Chimeras (RIMTAC). Rather than directly inhibiting VHL, RIMTAC employs a RIPK1 inhibitor to hijack the endogenous RIPK1-VHL complex, recruiting VHL indirectly for TPD. As a proof of concept, we designed RIMTACs targeting BRD4, AKT, and JAK1. These molecules induced potent, concentration- and time-dependent degradation of their targets. Mechanistically, degradation was confirmed to be UPS-dependent and required a quaternary complex of VHL, RIPK1, the target protein, and the RIMTAC molecule. RIMTAC expands the TPD toolbox and offers a promising synergistic strategy for anti-inflammatory therapy. - Source: PubMed
Publication date: 2026/07/08
Shen ChangSun HanyinLi RuiningMutyala RaghupathiTian XinjianHuang ChaoqunHu JingleiAn JieLi LinZhang TaoYu XufenZhao BoZhu MingyanShen Yudao - Chronic periodontitis (CP) is a chronic infectious disease. Ubiquitin-specific protease 5 (USP5), a member of the deubiquitinase family, has garnered significant attention due to its crucial biological functions. In this study, we aimed to explore the function of USP5 in CP development. Human periodontal ligament mesenchymal stromal cells (hPDL-MSCs) were stimulated with LPS. qRT-PCR and western blot assay were performed to determine the expression of USP5, receptor-interacting protein kinase 1 (RIPK1), osteogenic markers, and macrophage polarization markers. Alkaline phosphatase (ALP) and Alizarin red S (ARS) staining assays were used to examine ALP activity and ARS quantification. Flow cytometry analysis was used to analyze cell apoptosis. Commercial kits were used to evaluated the levels of oxidative stress indicators. ELISA was performed for the concentrations of inflammatory factors. Co-immunoprecipitation (Co-IP) assay, GST pull-down assay and Ubiquitination assay were applied to analyze the relation between USP5 and RIPK1. USP5 was upregulated in the PDL tissues of CP patients and LPS-triggered hPDL-MSCs. Knockdown of USP5 contributed to the osteogenic differentiation of LPS-treated hPDL-MSCs and repressed the apoptosis, oxidative stress, inflammation, and M1-like macrophage polarization in LPS-treated hPDL-MSCs. Mechanically, USP5 was demonstrated to regulate RIPK1 expression through deubiquitination. Moreover, overexpression of RIPK1 restored the effects of USP5 knockdown on the osteogenic differentiation, apoptosis, oxidative stress injury, and macrophage polarization direction in LPS-treated hPDL-MSCs. USP5 deubiquitinated and stabilized RIPK1 to regulate the osteogenic differentiation, oxidative stress injury and macrophage polarization in CP. - Source: PubMed
Publication date: 2026/07/06
Mao JinghongQin Ming