NRF1 EMSA Kit
- Known as:
- NRF1 EMSA Kit
- Catalog number:
- AY1224
- Product Quantity:
- 25 rxn
- Category:
- -
- Supplier:
- Panomics
- Gene target:
- NRF1 EMSA Kit
Related genes to: NRF1 EMSA Kit
- 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
- Gene:
- NRF1 NIH gene
- Name:
- nuclear respiratory factor 1
- Previous symbol:
- -
- Synonyms:
- EWG, ALPHA-PAL
- Chromosome:
- 7q32.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-11-01
- Date modifiied:
- 2016-10-05
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- 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 proteasome is essential for cellular protein homeostasis through selective destruction of damaged and misfolded proteins. Failure of proteasome-dependent turnover accompanied by accumulation and aggregation of aberrant proteins is a hallmark of aging and late-onset neurodegenerative diseases. SKN-1A/Nrf1, a member of the NFE2L/Nrf family of transcription factors, is a master regulator of proteasome biogenesis. Through transcriptional control of proteasome subunit gene expression, SKN-1A/Nrf1 controls homoeostatic and stress-responsive upregulation of proteasome levels in adaptation to proteasome dysfunction or protein misfolding. SKN-1A/Nrf1 acts in concert with another Nrf family transcription factor, SKN-1C/Nrf2, to regulate many aspects of physiology including stress responses, redox balance, immunity, and metabolism. Here, we demonstrate that a small deletion in the promoter of the pbs-5 gene, which encodes an essential proteasome subunit, uncouples its expression from transcriptional regulation by SKN-1A/Nrf1. This disruption leads to compensatory SKN-1A/Nrf1-dependent upregulation of other proteasome subunit genes, resulting in a homeostatic imbalance in proteasomal gene expression. This pbs-5 regulatory mutation phenocopies some, but not all, aspects of SKN-1A/Nrf1 inactivation, providing evidence that coordinated regulation of proteasomal subunit gene expression underlies a subset of SKN-1A/Nrf1's physiological roles. In comparing the effects of the pbs-5 promoter deletion with isoform-specific inactivation of SKN-1A or SKN-1C, we show that the pbs-5 promoter mutation completely abrogates multiple lifespan extension paradigms. These results reveal that coordinated homeostatic regulation of proteasome subunit gene expression is critical for longevity and healthy aging. - Source: PubMed
Publication date: 2026/02/17
Topalidou IriniLehrbach Nicolas - - Source: PubMed
Publication date: 2026/01/26
Sokolov MaximTaniguchi HiroakiWeber Jonasz Jeremiasz - Fasting-mimicking diet (FMD) is a safe and effective strategy in clinical oncology via metabolically restricting tumour growth and remodelling the immunity. To date, few studies have investigated the impact of on tumour-associated macrophages (TAMs), which are a crucial component of immune cells in the tumour microenvironment. Fasting can induce the ubiquitin-proteasome system (UPS) to regulate intracellular protein turnover homoeostasis, while Nuclear Factor Erythroid 2-like 1 (NRF1; encoded by the gene Nfe2l1), which controls proteasome gene transcription, may potentially be induced by fasting. However, whether NRF1 is induced by FMD/fasting, and how NRF1-mediated protein turnover works on TAMs remain unknown. This study investigated the hypothesis that FMD activates the anti-tumour immunity of TAMs by ubiquitinated protein metabolism. - Source: PubMed
Publication date: 2026/01/29
Li JiakunJiang WenjiaoTu GuoweiZhong ZiwenLuo ZheHorng TiffanyMiao Changhong - Nuclear factor erythroid 2-like 1 (NFE2L1/Nrf1), an endoplasmic reticulum (ER)-associated transcription factor, is responsible for the coordinated expression of proteasome subunit genes upon proteasomal dysfunction. -glycosylated proteins undergo protein sequence editing by peptide:-glycanase (NGLY1)-mediated conversion of -glycosylated asparagine residues to aspartic acid. Nrf proteins are the only transcription factors that undergo sequence editing for transcriptional activation. However, the mechanism via which sequence editing regulates the transcriptional activity of Nrf1 has remained unclear. Here, we demonstrated that sequence editing of the ninth -glycosylation site (Asn574) in human Nrf1 is required for proteasome gene expression in HeLa cells. Editing of Asn574 is essential for interaction with host cell factor C1 and -GlcNAc transferase, which is required for Nrf1 chromatin binding and sufficient proteasome expression. Furthermore, sequence editing of -glycosylation sites other than Asn574 is required for the interaction with the coactivator CREBBP/EP300, thereby enhancing Nrf1's transcriptional activity. Unexpectedly, the expression of Nrf1 mutants that mimic proteolytic processing by DNA-damage-inducible 1 homolog 2 and sequence editing by NGLY1 markedly diminished the growth rate in HeLa cells, suggesting that the constitutive activation of Nrf1 exhibits cytotoxicity. Collectively, our study explains the strategy of on-demand Nrf1 activation for survival benefits. Nrf1 is synthesized as a proteasome-targeting protein and is highly glycosylated in the ER. Nrf1 is activated via sequence editing-dependent coactivator complex formation only when the proteasome needs to be compensated for. - Source: PubMed
Publication date: 2025/12/30
Yoshida YukikoOkada MeariArai NaokoAndo ChikaraKinoshita DaikiNishito YasumasaKametani FuyukiHasegawa MasatoTanaka KeijiEndo Akinori