Ask about this productRelated genes to: NOX2 antibody
- Gene:
- CYBB NIH gene
- Name:
- cytochrome b-245 beta chain
- Previous symbol:
- CGD
- Synonyms:
- GP91-PHOX, NOX2
- Chromosome:
- Xp21.1-p11.4
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2019-04-23
- Gene:
- DUOX2 NIH gene
- Name:
- dual oxidase 2
- Previous symbol:
- -
- Synonyms:
- P138-TOX, P138(TOX), THOX2, LNOX2
- Chromosome:
- 15q21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-11-09
- Date modifiied:
- 2016-10-05
Related products to: NOX2 antibody
Related articles to: NOX2 antibody
- Very early onset inflammatory bowel disease (VEO-IBD) is a rare, severe condition with over 80 monogenic causes. These often resist conventional therapies, necessitating targeted treatments such as biologics and hematopoietic stem cell transplantation (HSCT). This study aimed to systematically review therapeutic outcomes. - Source: PubMed
Publication date: 2026/01/16
Abhari Amir ParsaRezvanian ParasteshSohrabi ElikaHosseini KavehAttauabi MohamedGupta RasheeNajafi Kimia - The precise role of neutrophil-derived reactive oxygen species (ROS) in combating bacterial uropathogens during urinary tract infections (UTI) remains largely unexplored. In this study, we elucidate the antimicrobial significance of NADPH oxidase 2 (NOX2)-derived ROS, as opposed to mitochondrial ROS, in facilitating neutrophil-mediated eradication of uropathogenic Escherichia coli (UPEC), the primary causative agent of UTI. Furthermore, NOX2-derived ROS regulate NF-κB-mediated inflammatory responses in neutrophils against UPEC by inducing the release of nuclear factor erythroid 2-related factor 2 (Nrf2) from its inhibitor, Kelch-like ECH-associated protein 1 (Keap1). Consistently, the absence of NOX2 (Cybb) in mice led to uncontrolled bacterial infection associated with increased NF-κB signaling, heightened neutrophilic inflammation, and increased bladder pathology during cystitis. These findings underscore a dual role for neutrophil NOX2 in both eradicating UPEC and mitigating neutrophil-mediated inflammation in the urinary tract, revealing a previously unrecognized effector and regulatory mechanism in the control of UTI. - Source: PubMed
Publication date: 2024/12/20
Cotzomi-Ortega IsraelRosowski Emily EWang XinSanchez-Zamora Yuriko ILopez-Torres Jeimy MSanchez-Orellana GamalielHan RachelVásquez-Martínez GabrielaAndrade Gabriel MayoralBallash GregoryCortado HannaLi BirongAli YusufRascon RaulRobledo-Avila FrankPartida-Sanchez SantiagoPérez-Campos EduardoOlofsson-Sahl PeterZepeda-Orozco DianaSpencer John DavidBecknell BrianRuiz-Rosado Juan de Dios - Acute myeloid leukaemia (AML) is a highly heterogeneous malignancy, with a poor 5-year overall survival rate of approximately 30%. Consequently, the search for novel therapeutic strategies is ongoing, and the identification of new vulnerabilities could accelerate progress. Oxidative stress and metabolic rewiring are established hallmarks of cancer, and recent evidence suggests that NADPH oxidases may regulate metabolism, potentially linking these two processes. Increasing research highlights the importance of NOX2 in AML, particularly its role in metabolic regulation. In this study, we investigated the effects of simultaneously inhibiting NOX2 and glycolysis in AML cells. Dual inhibition of NOX2 and glycolysis-by targeting hexokinase or lactate dehydrogenase (LDH)-significantly reduced cell proliferation, markedly impaired clonogenic potential, and induced extensive cell death in a broad panel of AML cell lines. Importantly, these findings were further validated in primary bone marrow samples derived from AML patients, where combined inhibition triggered similar potent anti-leukemic effects. Furthermore, the combined inhibition of NOX2 and LDH enhanced the efficacy of cytarabine (AraC), suggesting this approach could boost the effectiveness of conventional therapies. In an in vivo AML model, targeting NOX2 and LDH in myeloid progenitor cells delayed the onset of leukaemia and extended survival. In conclusion, our findings propose a novel therapeutic strategy for AML through the dual targeting of NOX2 and glycolysis. - Source: PubMed
Publication date: 2024/10/29
Ijurko CarlaRomo-González MartaPrieto-Bermejo RodrigoDíez-Campelo MaríaVidriales María-BelénMuntión SandraSánchez-Guijo FermínSánchez-Yagüe JesúsHernández-Hernández Ángel - Lenvatinib resistance causes less than 40% of the objective response rate. Therefore, it is urgent to explore new therapeutic targets to reverse the lenvatinib resistance for HCC. HAND2-AS1 is a critical tumor suppressor gene in various cancers. - Source: PubMed
Song ZhengZhang YuLuo WeiSun ChaoLv CaihongWang SihaoHe QuanweiXu RanBai ZhaofangChang XiujuanYang Yongping - The actin cytoskeleton and reactive oxygen species (ROS) both play crucial roles in various cellular processes. Previous research indicated a direct interaction between two key components of these systems: the WAVE1 subunit of the WAVE regulatory complex (WRC), which promotes actin polymerization and the p47 subunit of the NADPH oxidase 2 complex (NOX2), which produces ROS. Here, using carefully characterized recombinant proteins, we find that activated p47 uses its dual Src homology 3 domains to bind to multiple regions within the WAVE1 and Abi2 subunits of the WRC, without altering WRC's activity in promoting Arp2/3-mediated actin polymerization. Notably, contrary to previous findings, p47 uses the same binding pocket to interact with both the WRC and the p22 subunit of NOX2, albeit in a mutually exclusive manner. This observation suggests that when activated, p47 may separately participate in two distinct processes: assembling into NOX2 to promote ROS production and engaging with WRC to regulate the actin cytoskeleton. - Source: PubMed
Publication date: 2024/03/01
Kuihon Simon V N PSevart Brodrick JAbbey Colette ABayless Kayla JChen Baoyu