ATF6 ELISA kit
- Known as:
- ATF6 Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- DL-ATF6-Mu
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- WDSTD
- Gene target:
- ATF6 ELISA kit
Related genes to: ATF6 ELISA kit
- Gene:
- ATF6 NIH gene
- Name:
- activating transcription factor 6
- Previous symbol:
- -
- Synonyms:
- ATF6A
- Chromosome:
- 1q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-12-15
- Date modifiied:
- 2015-09-11
Related products to: ATF6 ELISA kit
Human ELC ELISA KIT 96 TEST
OxiSelect In Vitro ROS/RNS Assay Kit (Green Fluorescence), Trial Size
OxiSelect Methylglyoxal (MG) Competitive ELISA Kit
OxiSelect Methylglyoxal (MG) Competitive ELISA Kit
OxiSelect TBARS Assay Kit (MDA Quantitation), Trial Size
OxiSelect Total Antioxidant Capacity (TAC) Assay Kit, Trial Size
OxiSelect™ In Vitro ROS RNS Assay Kit (Green Fluorescence), Trial Size(1-3)-beta-D-glucan Sandwich ELISA, Double Antibody(1-Kit )11,12-EET DHET Immunoassay Kit(1-Kit )11,12-EET_DHET Immunoassay Kit(1-Kit) 11,12-DHET Immunoassay Kit(1-Kit) 14,15-DHET Human Urine ELISA Kit(1-Kit) 14,15-DHET Hypertension ELISA Kit(1-Kit) 14,15-DHET sEH activity ELISA Kit(1-Kit) 14,15-EET DHET Hypertension ELISA Kit Related articles to: ATF6 ELISA kit
- Fuchs endothelial corneal dystrophy (FECD) is a progressive degenerative disease of the corneal endothelium and remains a leading indication for corneal transplantation worldwide. FECD is characterized by excessive extracellular matrix (ECM) deposition, disruption of proteostasis with endoplasmic reticulum (ER) stress, and progressive endothelial cell loss; however, no pharmacological therapy is currently available. Given that FECD involves multiple interacting pathogenic pathways, we asked whether a structure-based polypharmacology approach could identify a single small molecule capable of modulating distinct disease-relevant targets. We performed virtual screening of 1,178 FDA-approved compounds against transforming growth factor-β receptor type II (TGF-βR2) and p38 mitogen-activated protein kinase (p38 MAPK), which contribute to ECM dysregulation and stress-induced apoptosis. VX-809 was the only compound predicted to bind both targets, with docking scores of - 8.5 kcal/mol for TGF-βR2 and - 10.7 kcal/mol for p38 MAPK; molecular dynamics simulations further supported stable protein-ligand interactions. In patient-derived FECD corneal endothelial cells, VX-809 attenuated TGF-β2-induced apoptosis, suppressed activation of Smad2/3 and p38 MAPK signaling, and reduced ECM overproduction and global protein synthesis. VX-809 also decreased aggresome formation and dampened activation of the PERK, IRE1α, and ATF6 arms of the unfolded protein response, consistent with improved protein homeostasis under stress conditions. Together, these findings show that structure-based screening can reveal previously unrecognized multi-target activities in existing drugs and identify candidate modulators of converging pathogenic pathways in FECD. This study provides proof of concept for docking-based polypharmacology strategies to accelerate early-stage discovery for multifactorial ocular diseases. - Source: PubMed
Publication date: 2026/05/02
Noda ShunsukeImai KotaOkino TaiseiNumao TaisukeTourtas TheofilosSchlötzer-Schrehardt UrsulaKruse FriedrichKoizumi NorikoOkumura Naoki - Drug-induced liver injury (DILI) remains a leading cause of acute liver failure; however, current clinical strategies lack reliable biomarkers, predictors of susceptibility, and effective therapeutic interventions. Among these etiologies, acetaminophen (APAP) overdose is the most common cause of DILI worldwide. Heat shock proteins (HSPs), particularly members of the HSP40 family, are central regulators of cellular stress responses, yet the specific role of DNAJB4/HLJ1 in APAP-induced hepatotoxicity remains poorly defined. To address this gap, we employed DNAJB4/HLJ1-deficient mice (Dnajb4) to investigate the function of DNAJB4/HLJ1 in APAP-induced liver injury. Following APAP administration (> 400 mg/kg), Dnajb4exhibited exacerbated hepatic necrosis, elevated liver enzymes, and enhanced c-jun/JNK activation compared with Dnajb4 controls. Metabolic profiling revealed altered APAP metabolism, with reduced detoxification products and excessive oxidative metabolites, and pronounced glutathione (GSH) depletion. Transcriptomic analysis implicated DNAJB4/HLJ1 in metabolism, protein folding, and endoplasmic reticulum (ER) stress via interaction with HSP70. Consistently, ATF6, XBP1, and CHOP expression confirmed aggravated ER stress in Dnajb4 livers. AlphaFold-Multimer modeling and co-immunoprecipitation validated physical interaction between DNAJB4/HLJ1 and HSP70. Restoration of DNAJB4/HLJ1 expression attenuated ER stress, c-jun/JNK activation, and liver injury, while pharmacological inhibition of ER stress confirmed its mechanistic involvement. Collectively, these findings identify DNAJB4/HLJ1 as a previously unrecognized regulator of stress signaling in APAP-induced hepatotoxicity. By modulating ER stress within the integrated cellular stress network, DNAJB4/HLJ1 limits injury progression and promotes hepatocellular resilience, highlighting its potential as a novel therapeutic target for preventing or mitigating DILI. - Source: PubMed
Publication date: 2026/05/01
Lu Chih-YunHsieh Tsung-HsuanChien Min-HuiHsu Wei-LunLuo Wei-JiaChang Jung-HsuanLee Chia-IChen Yi-ChunFang Cheng-HaoKuo Ching-HuaYu Sung-LiangSu Kang-Yi - The endoplasmic reticulum (ER) plays a central role in protein homeostasis by facilitating the folding, modification, and quality control of secretory and membrane proteins. Disruption of ER function results in protein misfolding and ER stress, which activate the unfolded protein response (UPR). While the three canonical UPR branches, inositol-requiring enzyme 1 (IRE1), protein kinase RNA-like endoplasmic reticulum kinase (PERK), and activating transcription factor 6 (ATF6), have been extensively studied, the mechanisms that coordinate their activities and ultimately dictate survival or death remain poorly understood. Transmembrane P24 trafficking protein 9 (TMED9), a cargo receptor that cycles between the ER and Golgi, has been implicated in protein quality control under pathological conditions, but its physiological role in ER proteostasis and UPR signaling is unclear. - Source: PubMed
Publication date: 2026/04/30
Lenchisky ChenMuhammad Majadly AreenBronshtein Berger IrenaBiton DanielleDaoud Sarsour AlaaArbeli NarkisCohen TamarAmos NaamaKinstlinger SaraCohen OrtalHorwitz EladDvela-Levitt Moran - Although Doxorubicin (Dox) is an effective anticancer drug, it can cause severe cardiotoxicity. While several mechanisms have been proposed to explain Dox-induced cardiomyopathy (DIC), strategies to prevent it remain limited. In previous research on isolated cardiomyocytes, we identified that Empagliflozin (EMPA), an antidiabetic drug, mitigated Dox-induced ER stress and apoptosis. In this in vivo study using rats, we further investigated EMPA's potential in preventing and treating DIC. Rats administered a cumulative dose of 15 mg/kg Dox exhibited significant cardiovascular damage, including left ventricular cavity dilation, decreased left ventricular ejection fraction (LVEF), ER dilation, mitochondrial defects and vacuole formation. These structural changes were linked to the activation of ER-stress pathways (PERK, IRE1 and ATF6) and upregulation of apoptotic proteins initiated by ER stress. When EMPA (10 mg/kg/day) was administered either prophylactically or concurrently with Dox, it significantly attenuated adverse LV remodelling and preserved LVEF. Additionally, EMPA prevented ER stress and subsequent apoptosis in the myocardium of the Dox + EMPA-treated group. These findings suggest that EMPA offers cardioprotective benefits in DIC, likely through the inhibition of ER-stress-induced myocardial injury. - Source: PubMed
Malik AkshiCheung David C YLedingham D AllisonDesautels DanielleHerrmann JoergSingal Pawan KJassal Davinder S - Mitochondrial dysfunction and the corresponding metabolic reprogramming have been established as critical drivers of tumor progression; nevertheless, the specific molecular mechanisms have not yet been fully elucidated. In this study, we reveal that ablation of inner mitochondrial membrane protein (IMMT), a key architectural component of mitochondrial cristae, induces concurrent mitochondrial and endoplasmic reticulum stress (ERS), which selectively activates the ATF6-mediated unfolded protein response (UPR) to drive breast cancer (BC) cell proliferation. Mechanistically, IMMT loss promotes ATF6α-ATF6β heterodimer formation, whereby ATF6α stabilizes ATF6β protein, enabling ATF6β to engage PPARγ through direct physical interaction and orchestrate redox homeostasis remodeling that sustains tumor cell proliferation. Notably, we discovered that this compensatory stress adaptation is context-dependent, manifesting specifically in TP53-mutant tumors, but not in their wild-type counterparts, and targeted disruption of the ATF6β-PPARγ signaling axis effectively abrogates the oncogenic effects induced by IMMT-KO. Our work uncovers a previously unrecognized adaptive axis linking chronic mitochondrial dysfunction to redox control in BC and establishes ATF6β as a critical effector that partners with PPARγ under stress-a functional role distinct from its classical regulatory relationship with ATF6α. These findings provide a theoretical foundation for precision therapeutic strategies targeting vulnerabilities in the stress adaptation pathway of BC. - Source: PubMed
Publication date: 2026/04/28
Liu LiLi DanHou ZeyuHuang YiWang JinjingPu ChaoruiZhao QingqingYu YunyanChen Rui