NFE2L1 Antibody
- Known as:
- NFE2L1 Antibody
- Catalog number:
- GWB-MM722B
- Product Quantity:
- 50ug
- Category:
- -
- Supplier:
- GenWay
- Gene target:
- NFE2L1 Antibody
Related genes to: NFE2L1 Antibody
- Gene:
- NFE2L1 NIH gene
- Name:
- nuclear factor, erythroid 2 like 1
- Previous symbol:
- TCF11
- Synonyms:
- NRF1, LCR-F1, FLJ00380
- Chromosome:
- 17q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1994-03-24
- Date modifiied:
- 2015-11-18
Related products to: NFE2L1 Antibody
Related articles to: NFE2L1 Antibody
- The mechanisms by which cancer cells survive and adapt under high levels of reactive oxygen species (ROS) remain poorly understood, especially in the context of redox homeostasis. This study reveals increased oxidative stress in esophageal squamous cell carcinoma (ESCC), with serine/arginine-rich splicing factor 6 (SRSF6) playing a crucial role in maintaining redox homeostasis. SRSF6 binds to the exonic splicing enhancer (ESE) motif in nuclear factor erythroid 2-related factor 1 (NFE2L1 Exon 4, preventing exon skipping and promoting the production of specific isoforms that promote ESCC cell proliferation. This interaction enhances cellular antioxidant capacity, thereby influencing redox balance. Moreover, reducing SRSF6 increases the levels of NFE2L1-S, the isoform produced by exon 4 skipping in the gene, which elevates ROS levels and induces apoptosis and ferroptosis. Notably, SRSF6 and NFE2L1 form a positive feedback loop: NFE2L1 serves as the transcription factor for SRSF6, while SRSF6 acts as the splicing factor for NFE2L1. Antisense oligonucleotides (ASOs) targeting SRSF6 significantly suppress ESCC cell growth. Importantly, inhibiting this feedback loop also enhances cisplatin (CDDP) sensitivity, increasing the therapeutic efficacy of CDDP. Our findings highlight the critical role of the SRSF6-NFE2L1 axis in redox homeostasis and tumor progression, positioning SRSF6 as a distinctive therapeutic target to improve treatment outcomes in ESCC. - Source: PubMed
Publication date: 2026/06/10
He XinyuXu JialuoDuan LinaMa JingGao DanXie YifeiZhao DengyunLiu JialinZhao JiminLiu FangfangLee Mee-HyunKim Myoung OkDong ZigangJiang YananLiu Kangdong - In diabetic nephropathy (DN), oxidative stress disrupts normal metabolic processes, contributing to progressive kidney injury. Although Nfe2l1 (also known as Nrf1) is known to regulate oxidative stress and metabolism, its specific role in DN remains poorly understood. This study investigated how changes in Nrf1 expression influence DN-associated renal fibrosis. - Source: PubMed
Publication date: 2026/06/12
Qiu ZiyingZhang YanminZhu LaiyuZhao XuanruiLi XinyaGong XiaokeCi Xinxin - Endometriosis (EMs) is a chronic inflammatory disease characterized by ectopic growth of endometrial-like tissues. N-methyladenosine (mA) modification regulates diverse cellular processes, yet its role in EMs remains unclear. Here, we show that the mA reader YTHDF2 is downregulated in ectopic tissue and endometrial stromal cells. Overexpression of YTHDF2 in HESCs suppresses proliferation and migration while promoting apoptosis, whereas its knockdown exerts opposite effects. In vivo, AAV9-mediated Ythdf2 delivery inhibits lesion growth, while inhibition of YTHDF2 accelerates disease progression. Mechanistically, hypoxia induces HDAC11 via HIF-1α, reducing acetylation of the YTHDF2 promoter and leading to transcriptional silencing. RNA-seq reveals that YTHDF2 loss activates NF-κB signaling. Integrative MeRIP-seq, RIP-seq, and scRNA-seq analyses identify NFE2L1 as a direct downstream target whose mRNA stability is enhanced upon YTHDF2 depletion in an mA-dependent manner. Elevated NFE2L1 activates STAT3 and CARD11, potent NF-κB inducers. Collectively, our study uncovers a mechanism whereby epigenetic silencing of YTHDF2 drives EMs progression through the NFE2L1-NF-κB axis, suggesting YTHDF2 as a potential therapeutic target. - Source: PubMed
Publication date: 2026/05/19
Wang TaoPeng XiaotongYang PushengJi MeMiao YaxinZhang JiaxinLiu WenwenZhu YipingTang MingSun Jing - Migraine, a prevalent and debilitating neurovascular disorder, frequently co-occurs with functional dyspepsia. Emerging evidence suggests that infection may contribute to both conditions via neuroimmune pathways, though the molecular basis for this association has yet to be fully elucidated. - Source: PubMed
Publication date: 2026/04/28
Sun NengjinWang KaileGou JianliLi PanpanFu XiaoyanShi WenjingLi JingXiang MiaoSun ShenglinSun ZihanLiang ShujuanZhang YuyingWang Hongyan - Proteasome inhibitor drugs are currently used in the clinic to treat multiple myeloma and mantle cell lymphoma. These inhibitors cause accumulation of undegraded proteins, thus inducing proteotoxic stress and consequent cell death. However, cancer cells counteract this effect by activating an adaptive response through the transcription factor nuclear factor erythroid 2-related factor 1 (NRF1, also known as NFE2L1). NRF1 induces transcriptional upregulation of proteasome and autophagy/lysosomal genes, thereby reducing proteotoxic stress and diminishing the effectiveness of proteasome inhibition. While suppressing this protective autophagy response is one potential strategy, here we investigated whether this heightened autophagy could instead be leveraged therapeutically. To this end, we designed an autophagy-targeting chimera (AUTAC) compound to selectively degrade the anti-apoptotic protein Mcl1 via the lysosome. Our results show that this lysosome-mediated targeted degradation is significantly amplified in the presence of proteasome inhibition, in a NRF1-dependent manner. Mechanistically, AUTAC-driven Mcl1 clearance requires K63-linked ubiquitination by UBC13 and TRAF6 and recognition by the cargo receptor p62/SQSTM1. The combination of the proteasome inhibitor carfilzomib and Mcl1 AUTAC synergistically promoted cell death in both in vitro models, including wild-type and proteasome inhibitor-resistant multiple myeloma and lung cancer cells, and in mouse tumor xenografts. Thus, our work offers a novel strategy for enhancing proteasome inhibitor efficacy by exploiting the adaptive autophagy response. More broadly, our study establishes a framework for amplifying lysosome-mediated targeted protein degradation, with potential applications in cancer therapeutics and beyond. - Source: PubMed
Publication date: 2026/05/11
Elshazly Ahmed MHosseini NayyerehalsadatVangala JanakiramShen ShanweiNeely VictoriaHu XiaoyanPagare Piyusha PHarada HisashiGrant StevenRadhakrishnan Senthil K