Anti_Mouse, mab TNFRSF10B Source Rat
- Known as:
- Anti_Mouse, mab TNFRSF10B Source Rat
- Catalog number:
- 103-M478
- Product Quantity:
- 100 µg
- Category:
- -
- Supplier:
- Reliatech
- Gene target:
- Anti_Mouse mab TNFRSF10B Source Rat
Related genes to: Anti_Mouse, mab TNFRSF10B Source Rat
- Gene:
- TNFRSF10B NIH gene
- Name:
- TNF receptor superfamily member 10b
- Previous symbol:
- -
- Synonyms:
- DR5, KILLER, TRICK2A, TRAIL-R2, TRICKB, CD262, TRAILR2
- Chromosome:
- 8p21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-04
- Date modifiied:
- 2018-01-25
Related products to: Anti_Mouse, mab TNFRSF10B Source Rat
Related articles to: Anti_Mouse, mab TNFRSF10B Source Rat
- Ulcerative colitis (UC) is a type of inflammatory bowel disease without curative therapeutics. Recent studies demonstrate that exerts mitigating effects on UC, but the underlying mechanisms remain unclear. In this study, we isolated a strain of , designated NND9, from the feces of DSS-induced ulcerative colitis model mice and investigated its effects on UC of the mouse model. NND9 significantly alleviated UC severity in the mice by restoring gut barrier integrity through improving colonic mucus layer thickness, mitigating goblet cell depletion, and halting epithelial cell death. Mechanistically, NND9 suppressed the expression of the gene encoding death receptor 5 (DR5) on the surface of colonic epithelial cells. Additionally, NND9 inhibited the phosphorylation of kinase 3 (RIPK3) and the pseudokinase mixed-lineage kinase domain-like protein (MLKL) associated with the necrotic apoptosis pathway, thereby reducing gut epithelial cell death. NND9 also markedly ameliorated the gut microbiome of the colitis mice. Untargeted metabolomics analysis demonstrated that NND9 modulated both tryptophan and bile acid metabolism. In conclusion, NND9 exhibits curative effects on UC by resolving inflammatory reactions of the gut mucosa through the DR5-RIPK3/p-RIPK3-MLKL/p-MLKL pathway and redressing gut dysbiosis. This study provides valuable information for the development of innovative therapeutic strategies for the treatment of UC. - Source: PubMed
Publication date: 2026/04/29
Gao Xin-YuWang YanWang Yu-HuiYu HaoLiu LiangZhang Xing-HuaXu Hong-TaoMeng YaoJohnston Randal NLiu Gui-RongLiu Shu-Lin - HexaBody-DR5/DR5 (GEN1029) is a death receptor 5 (DR5) agonist composed of two humanized immunoglobulin G1 (IgG1) antibodies, Hx-DR5-01 and Hx-DR5-05, that bind non-overlapping DR5 epitopes with nanomolar affinity. HexaBody-DR5/DR5 is designed to activate the TRAIL pathway through DR5 clustering. This phase 1/2a, open-label, multi-center study aimed to determine the safety, pharmacokinetics (PK), pharmacodynamics, and preliminary antitumor activity of HexaBody-DR5/DR5 in patients with advanced solid tumors. In the study, 46 patients received biweekly intravenous injections of HexaBody-DR5/DR5 at doses ranging from 0.1 to 3.0 mg/kg, including patients with colorectal, gastric, non-small-cell lung, pancreatic, and triple-negative breast cancer. Safety evaluations revealed that 76.1% of patients experienced at least one grade (G) ≥ 3 treatment-emergent adverse event (TEAE), and 45.7% had drug-related G ≥ 3 events. The most frequent G ≥ 3 drug-related TEAEs were elevations of liver transaminases and diarrhea. According to RECIST criteria, 32.6% of patients showed stable disease. No patients achieved a partial or complete response. Exploratory assessments of cleaved cytokeratin 18 (cCK18) plasma levels indicated apoptotic pathway activation upon treatment. Reductions in circulating tumor DNA (ctDNA) levels and tumor metabolic activity according to PERCIST criteria suggested tumor-targeted biological activity. Nonclinical studies in vitro using human liver models demonstrated that HexaBody-DR5/DR5 directly inhibits viability of hepatocytes, but not Kupffer cells. The non-clinical liver toxicity was driven by dual epitope binding and hexamerization features, independent of FcγR-mediated crosslinking. Overall, these findings suggest that the TRAIL pathway has potential as a target for cancer therapy, provided tumor-specificity is sufficiently high to achieve an acceptable therapeutic index. - Source: PubMed
Overdijk Marije BStrumane KristinPlummer RuthLoRusso PatriciaRodon Ahnert JordiBanerji UdaiGarralda ElenaCalvo EmilianoSi HanHoevenaars NaomiMortensen Jens ThingBosgra SietoMalmberg AndersEllekilde-Pedersen MereteRamirez-Andersen TeresaDiamantopoulou Reiter PanagiotaFavaro ElenaForssmann UlfBreij Esther C WJure-Kunkel Maria - Heart failure (HF) is a major global public health challenge, with obesity being one of its key risk factors. Although several HF risk prediction models have been developed in the general population, few are specifically tailored to individuals with obesity. This underscores the urgent need for precise biomarkers to improve individual risk stratification and enable personalized prevention strategies. We aimed to develop and validate a plasma proteomics-based protein risk score (PRS) to predict incident HF among individuals with obesity. - Source: PubMed
Publication date: 2026/05/21
Li MaohuaHe XiaoHu BinGu FengLi XinShu ChangZhu ZhaoweiLi Jiehua - Diabetic foot ulcers are a major cause of morbidity in patients with diabetes mellitus and remain challenging to treat despite advances in wound care. Growing evidence suggests that impaired axonal regeneration, along with chronic inflammation, impaired angiogenesis, and altered extracellular remodeling, is an important mechanism contributing to the chronic, nonhealing nature of cutaneous wounds. However, the mediators involved and the mechanisms by which they impair wound healing in the presence of hyperglycemia are poorly understood. Peripheral nerves coordinate inflammation, angiogenesis, and extracellular matrix remodeling during repair, and their dysfunction in diabetes disrupts these processes. This review examines how hyperglycemia and oxidative stress impair neuroregeneration ( mainly axonal and nerve regeneration), highlighting the downstream consequences for vascular and structural repair. Particular attention is given to the altered expression of activin A (associated with nerve growth and neural inflammation), TNFRSF10B (associated with neuronal damage and apoptosis, and synaptophysin (a marker of synaptic vesicles and involved in nerve regeneration, particularly in the early stages of axonal regrowth) as representative mediators linking neuronal injury to defective wound healing. By integrating findings across neural, vascular, and inflammatory pathways, this review supports impaired neuronal regeneration as an important contributor to nonhealing diabetic foot ulcer pathogenesis to identify potential molecular targets that may improve healing outcomes. - Source: PubMed
Publication date: 2026/05/13
Patel JaylanRai Vikrant - Chronic infection with hepatitis B virus (HBV) remains a global health issue, leading to liver diseases such as chronic hepatitis B, cirrhosis, and hepatocellular carcinoma. The HBV X protein (HBx) promotes viral replication and disease progression by interacting with various host proteins. One of its functions involves binding to microtubule-associated protein 1 light chain 3B (LC3B), which mediates selective autophagy and facilitates the removal of the immune-related protein TNFRSF10B (tumor necrosis factor receptor superfamily 10B). However, even the mechanism by which HBx interacts with LC3B remained unclear. In this study, we focused on the HBx-LC3B interaction as a first step and identified a conserved LC3-interacting region motif (Trp120-X-X-Leu123) within the Bcl-2 homology 3 (BH3)-like domain of HBx that directly binds to LC3B. This interaction was characterized using isothermal titration calorimetry and nuclear magnetic resonance (NMR) spectroscopy. We present the first NMR structure of LC3B in complex with the HBx BH3-like peptide, revealing that it adopts an extended conformation upon binding and that Trp120 and Leu123 are essential for LC3B recognition. Notably, the same portion forms an α-helix when binding to B-cell lymphoma 2 (Bcl-2) and B-cell lymphoma extra-large (Bcl-x), suggesting that HBx uses different conformations to interact with distinct targets. This structural plasticity may underlie the multifunctional roles of HBx. - Source: PubMed
Publication date: 2026/05/06
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