Polyclonal Rabbit NFE2L1 Antibody
- Known as:
- Polyclonal Rabbit NFE2L1 Antibody
- Catalog number:
- abx25990
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- Polyclonal Rabbit NFE2L1 Antibody
Related genes to: Polyclonal Rabbit 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: Polyclonal Rabbit NFE2L1 Antibody
Related articles to: Polyclonal Rabbit NFE2L1 Antibody
- Nfe2l1 is a transcription factor that is highly conserved and is encoded by the Nuclear Factor Erythroid 2 Like 1 (Nfe2l1) gene, which responds to oxidative stress, proteotoxic stress, and endoplasmic reticulum stress in cells; However, its specific role in the context of acute kidney injury (AKI) is not fully understood. - Source: PubMed
Publication date: 2026/05/03
Hu JianqiangZhang YueweiZhang YanZhang YanminCi Xinxin - Aortic valve disease (AVD) is a cardiovascular disorder highly prevalent in the elderly population. Aortic valve leaflets suffer hardening due to extracellular matrix (ECM) remodeling and subsequent calcification, leading to impaired blood flow and aortic valve stenosis. Valve interstitial cells (VICs) are fibroblast-like cells that can undergo myofibroblast activation and osteogenic transformation, contributing to disease progression. - Source: PubMed
Publication date: 2026/04/07
Macarie Răzvan DȚucureanu Monica MCiortan LetițiaPreda Mihai BogdanMânduțeanu IleanaButoi Elena - Proteolytic stress frequently arises during disease and aging, particularly in long-lived, post-mitotic cells such as cardiomyocytes. To maintain proteostasis, cardiomyocytes depend on coordinated protein quality control pathways, including the ubiquitin-proteasome system and autophagy. Mechanisms that activate these pathways hold therapeutic potential for heart disease. Here, we demonstrate that transient activation of nuclear factor erythroid 2-like 1 (Nfe2l1, also known as Nrf1), a transcriptional regulator of proteasome activity, in cardiomyocytes during ischemia/reperfusion injury improves cardiac function. In addition to regulating the proteasome, we identify a critical role for Nrf1 in activating autophagy, which is essential for its cardioprotective effects. Through multi-omics analyses, we define both transcriptional and post-transcriptional functions of Nrf1 that underlie its cardioprotective activity. Loss-of-function studies in mice demonstrate that Nrf1, but not its homolog Nrf2, is required for autophagy and baseline cardiac function. Together, our findings establish a dual function of Nrf1 in promoting cardiac proteostasis by regulating both proteasomal and autophagic protein quality control pathways. Activating Nrf1 thus offers a therapeutic strategy for treating ischemic heart disease. - Source: PubMed
Publication date: 2026/04/17
Kankanamge Lakindu PAn HyunjiGuo QinProndzynski MaksymillianKwon Soon HoBonde Durgesh AnilPu William TOlson Eric NCui Miao - The cytosolic peptide:N-glycanase (PNGase, NGLY1 in mammals) is an enzyme that removes N-glycans from misfolded glycoproteins. NGLY1 contributes to cytosolic glycan degradation (non-lysosomal glycan degradation) and is one of the quality control systems for newly synthesized proteins, i.e., ER-associated degradation (ERAD). NGLY1 is also responsible for the activation of a transcription factor, NFE2L1, which participates in several stress responses, including regulation of proteasome subunit expression and oxidative stress. In 2012, NGLY1 deficiency, a human genetic disorder caused by the biallelic mutations in the NGLY1 gene, was discovered. Since then, research on the physiological functions of NGLY1 and the pathogenic mechanism of NGLY1 deficiency has expanded rapidly. Here, we will briefly overview the early history of NGLY1 research and then introduce its versatile functions. We will also provide mechanistic insights into the pathogenesis of NGLY1 deficiency based on studies using model animals, such as worms, flies, and rodents. - Source: PubMed
Fujihira HaruhikoSuzuki Tadashi - As multiple sclerosis (MS) progresses, myelin repair becomes inefficient. To gain insight into the underlying causes, we RNA-sequenced postmortem brain tissues from 4 and 6 patients, comparing remyelinating versus chronically active MS lesions. We identified the transcription factor FoxF2 as highly expressed within remyelinating lesions. Immunohistochemistry and in situ hybridization showed FoxF2 co-expression in GFAP-positive astrocytes, suggesting a subpopulation of astrocytes with a potential role in repair. To investigate how FoxF2 may influence repair, we examined cuprizone (CPZ)-induced de- and remyelination in CreERT2 FoxF2 conditional knockout (FoxF2 KO) mice. In the absence of FoxF2, RNA sequencing of the isolated corpus callosum (CC) showed high gene activation during demyelination and reduced gene activation during remyelination. Upregulated genes in FoxF2 KO mice were related to immune functions and metabolism. Specifically, upregulation of MHC-II and TNF-associated pathway genes, while astrocyte-specific FoxF2 deletion significantly reduced Tgfb2 and Tgfbr2 expression, implicating disrupted TGF-β signaling. The FoxF2 KO mice exhibited upregulation of ribosomal and sphingolipid metabolism genes during demyelination, while structurally related genes, including Mog expression, were impaired in the FoxF2 KO mice. Using network analysis to group highly correlated genes in the CC transcriptome, we identified gene regulatory network (GRN) changes. GRN analysis revealed the loss of FoxF2-associated modules (e.g., Foxf2-Bach2, Nfe2l1-Mafg), indicating impaired coordination of anti-inflammatory and regenerative pathways. In conclusion, analysis of MS white matter (WM) lesions and subsequent experimental data demonstrates that FoxF2 plays a role in regulating repair and gene networks associated with immune regulation, metabolism, and structural remodeling. - Source: PubMed
Publication date: 2026/02/26
Damsbo KarinaReyahi AzadehNik Ali MOubounyt MhanedWeber AnnaHyrlov Kirsten HKingo ChristinaFoged Maria LWaede MieBaumbach JanReynolds RichardCarlsson PeterIlles ZsoltElkjaer Maria L