RIPK1 Antibody (C_term) Blocking Peptide
- Known as:
- RIPK1 Antibody (C_term) Blocking Peptide
- Catalog number:
- BP7817b
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- RIPK1 Antibody (C_term) Blocking Peptide
Related genes to: RIPK1 Antibody (C_term) Blocking Peptide
- 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 (C_term) Blocking Peptide
Related articles to: RIPK1 Antibody (C_term) Blocking Peptide
- Lipopolysaccharide (LPS)-induced sepsis causes widespread inflammation and liver dysfunction, driven by oxidative stress and necroptosis. Remifentanil (REM), a short-acting μ-opioid receptor (MOR) agonist, has demonstrated anti-inflammatory and antioxidant effects. This study aimed to assess its potential hepatoprotective role in an LPS-induced rat model of liver injury. Female Wistar rats were allocated into four groups: Control, LPS (5 mg/kg, intraperitoneally), LPS + REM (LPS plus 0.04 mg/kg total dose of REM via IV infusion over 40 min), and REM alone. Liver tissues were analyzed histologically and immunohistochemically for tumor necrosis factor-alpha (TNF-α), alkaline phosphatase (ALP), and hypoxia-inducible factor-1 alpha (HIF-1α). Biochemical analyses included aspartate transaminase (AST), alanine transaminase (ALT), total oxidant status (TOS), total antioxidant status (TAS), and oxidative stress index (OSI). Expression levels of nuclear factor erythroid 2-related factor 2 (NRF2), heme oxygenase-1 (HO-1), receptor-interacting serine/threonine-protein kinase 1 (RIPK1), receptor-interacting protein kinase 3 (RIPK3), and mixed lineage kinase domain-like protein (MLKL) were assessed by qRT-PCR. LPS induced significant liver damage, as evidenced by higher histopathological scores, elevated liver enzymes, oxidative imbalance, and upregulated necroptotic gene expression. REM significantly reduced inflammation, necrosis, and hemorrhage. ALP expression remained comparable to the control group, whereas HIF-1α and TNF-α were markedly reduced. REM showed a non-significant decreasing trend in AST, ALT, TOS, and OSI levels. In contrast, REM significantly restored NRF2 and HO-1 mRNA expression and reduced the mRNA expression of RIPK1, RIPK3, and MLKL. REM attenuated LPS-induced hepatic injury, and this effect was found to be associated with modulation of oxidative stress responses, inflammatory alterations, and necroptosis-related gene expression. These findings suggest that REM may have potential as an adjunctive pharmacological agent in sepsis-associated hepatic dysfunction; however, further protein-level and pathway-specific validation studies are required. - Source: PubMed
Publication date: 2026/08/12
Savran MehtapAsci HalilOzmen OzlemGulal AbdurrahmanBalci CagriTepebasi Muhammet YusufIlhan Ilter - Adenosine monophosphate-activated protein kinase (AMPK) is an evolutionarily conserved serine/threonine kinase that links cellular energy stress with metabolic adaptation, autophagy, redox homeostasis, and cell fate decisions. Necroptosis is a regulated lytic form of cell death driven by receptor-interacting serine/threonine kinases 1 and 3 (RIPK1 and RIPK3), with mixed lineage kinase domain-like protein (MLKL) serving as the terminal executor. Increasing evidence suggests that AMPK modulates necroptosis through multiple interconnected mechanisms. AMPK directly phosphorylates RIPK1, thereby influencing necroptotic signaling in a context- and time-dependent manner. Through the AMPK-mTOR axis, AMPK also regulates autophagy and mitophagy, affecting inhibitory control of RIPK1 and autophagic turnover of RIPK3. In parallel, AMPK suppresses necroptosis through SIRT1- and PGAM5-related pathways, limiting necrosome assembly, mitochondrial dysfunction, and Drp1-dependent mitochondrial fission. AMPK further shapes reactive oxygen species (ROS)-associated necroptotic responses through downstream effectors, including mTOR and Nrf2. In this review, we summarize recent advances in the mechanisms by which AMPK regulates necroptosis and highlight unresolved questions, including the cell-type-specific roles of AMPK subunits, the contribution of additional autophagy regulators, the balance between mTORC1-dependent protective signaling and RIPK3 stability, and the in vivo relevance of the AMPK-SIRT1-PGAM5 axis. Clarifying this regulatory network may facilitate the development of therapeutic strategies for necroptosis-related diseases, including metabolic disorders, ischemia-reperfusion injury, and neurodegeneration. Collectively, the available evidence indicates that AMPK acts as a context-dependent regulator of necroptosis rather than a universally protective kinase. - Source: PubMed
Publication date: 2026/08/12
Song WenjingKe Zhifei - To investigate the effects and mechanism of a synthetic LXR agonist, T0901317, on neuronal necroptosis-related signaling pathways in NSC-34 mouse neuronal cells transfected with the TDP-43-A315T plasmid, TDP-43-A315T transgenic mice of amyotrophic lateral sclerosis (ALS). SWATH proteinomics analysis was used to compare ALS patients with cognitive impairment (CI) and non-cognitive impairment (NOCI). TDP-43 abnormal aggregation and necroptosis-related protein expression were assessed with immunofluorescence and western blotting, while apoptosis and inflammatory cytokines were measured through TUNEL assay and ELISA, muscle and motor neuron degeneration were examined with H&E and Toluidine Blue staining. Additionally, the Y-maze and Rotarod tests were used to evaluate cognitive and motor functions. Our study indicates that the LXR pathway was more downregulated in the ALS patients with cognitive impairment. RIPK1, p-RIPK3, and p-MLKL protein levels were upregulated in the TDP-43-A315T plasmid-transfected neuron cells and the TDP-43-A315T transgenic mouse model. The LXR agonist T0901317 reduced the abnormal aggregation of TDP-43 protein and downregulated the protein levels of RIPK1, p-RIPK3, and p-MLKL in vivo and in vitro. Furthermore, T0901317 attenuated motor neuron death and ameliorated muscle degeneration in TDP-43-A315T mice. T0901317 significantly prolonged survival, ameliorated cognitive and motor deficits, and shifted microglial activation marker profiles. The beneficial effects of T0901317 were abolished by LXR antagonist GSK 2033, accompanied by upregulation of necroptotic signaling. The neuroprotective effects of activating LXR may involve the regulation of the RIPK1-RIPK3-MLKL axis and TDP-43 aggregation. - Source: PubMed
Publication date: 2026/08/11
Zhang XiaojieZhang LirenChen LiYu WeibinZhao YuwuHuang YinhuiXu Zhouwei - To elucidate the role of Sirtuin 3 (SIRT3) / isocitrate dehydrogenase 2 (IDH2) axis in T-2 toxin-induced energy metabolism disorders and necroptosis in chondrocytes. Enrichment analysis was performed on differentially expressed genes in the articular cartilage and serum of Kashin-Beck disease patients. Sprague-Dawley rats were randomly divided into control (equal volume of normal saline), low T-2 toxin (100 ng/g·bw/day), and high T-2 toxin (200 ng/g·bw/day) groups. Human SW1353 cells were used to construct T-2 toxin exposed and SIRT3 intervened models in vitro. Enrichment analysis results indicated involvement of the tricarboxylic acid (TCA) cycle and oxidative phosphorylation (OXPHOS) in T-2 toxin-induced cartilage damage. The articular cartilage pathological changes including attenuated matrix staining, thinning of the cartilage layer, and blurred or disrupted marginal lines were observed in rats exposed to T-2 toxin. Western blot revealed that T-2 toxin downregulated SIRT3 expression and reduced the SIRT3-IDH2 interaction in chondrocyte. Immunoprecipitation confirmed decreased IDH2 deacetylation of chondrocyte induced by T-2 toxin. Additionally, the dose-dependently increased isocitrate content, while decreasing α-ketoglutarate and NADH levels of chondrocyte exposure to T-2 toxin. T-2 toxin also reduced activities of mitochondrial complexes II, III, and IV, inhibited oxygen consumption rate, and decreased adenosine triphosphate production of chondrocyte. Additionally, T-2 toxin upregulated necroptosis markers RIPK1, RIPK3, and MLKL, an effect reversed by a SIRT3 activator. In conclusion, T-2 toxin inhibited SIRT3 expression in chondrocytes, reduced IDH2 deacetylation, blocked the TCA cycle and OXPHOS, and ultimately led to energy metabolism disorder and necrosis of chondrocyte. - Source: PubMed
Publication date: 2026/08/11
Yu Fang-FangDou Yan-JieSha Tong-TongZhang Huan-XiaLi YaoLi QianDong Zai-ChaoKou Guang-Ning - - Source: PubMed