Npas2 antibody - N-terminal region (ARP37865_P050)
- Known as:
- Npas2 (anti-) - N-terminal region (ARP37865_P050)
- Catalog number:
- arp37865_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- Npas2 antibody - N-terminal region (ARP37865_P050)
Related genes to: Npas2 antibody - N-terminal region (ARP37865_P050)
- Gene:
- NPAS2 NIH gene
- Name:
- neuronal PAS domain protein 2
- Previous symbol:
- -
- Synonyms:
- MOP4, PASD4, bHLHe9
- Chromosome:
- 2q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-05-29
- Date modifiied:
- 2015-08-25
Related products to: Npas2 antibody - N-terminal region (ARP37865_P050)
Related articles to: Npas2 antibody - N-terminal region (ARP37865_P050)
- Huntington's disease (HD) involves progressive corticostriatal dysfunction, yet the temporal dynamics and cell type-specific vulnerability patterns remain incompletely understood. While recent single-cell studies in rapidly progressing models have revealed early developmental and regional changes, temporal profiling distinguishing pathogenic mechanisms from normal aging in full-length HTT models remains lacking. Resolving stage-specific temporal dynamics across interconnected striatal and cortical neuronal populations over protracted time is essential for identifying drivers of cellular dysfunction. - Source: PubMed
Publication date: 2026/05/28
Robbins Ashley BRanum Paul THuerta-Ocampo IcneliaKuckyr MichaelDavidson Beverly L - Polystyrene nanoparticles (PS-NPs) present significant risks to respiratory health, contributing to lung fibrosis. Current therapeutic strategies for PS-NP exposure injuries are limited and often ineffective. One promising solution is immunological training. This study explores the novel role of in immune training to alleviate PS-NP-induced fibrosis. Our findings demonstrate that enhances immune responses in a unique way, advancing current frameworks of trained immunity and offering new therapeutic approaches for health issues related to environmental pollutants. We conducted experiments using male BALB/c mice exposed to 80 nm PS-NPs via posterior pharyngeal drip. Prior to exposure, the mice received an intravenous injection of low-dose to induce immunological training. To evaluate the protective effects of , we assessed survival rates, pulmonary histopathology, and gene expression profiles. The results indicated that while 100% of the control group exposed to PS-NPs did not survive, the group pre-treated with exhibited complete survival. Histopathological analysis revealed preserved lung architecture and a significant reduction in collagen deposition in the + PS-NPs group compared to the PS-NPs only group. Additionally, RNA sequencing analysis identified a total of 415 differentially expressed genes, including five upregulated circadian rhythm genes (: 1.93-fold, : 1.69-fold, : 2.01-fold, : 2.55-fold, : 2.73-fold) and one downregulated circadian rhythm gene (: 0.42-fold) in the + PS-NPs group compared to the PS-NPs group. -based immune training reduces lung fibrosis and enhances survival after PS-NP exposure, suggesting a promising therapeutic strategy. - Source: PubMed
Publication date: 2026/05/07
Zhu ZhuyunZhou YifanZheng DongnanXu ZeminChen YuqingWang FengxuZhao XinyuanMa Yuanyuan - The heterodimeric transcription factor CLOCK-BMAL1 functions as the central activator of the mammalian circadian clock. By integrating basic helix-loop-helix (bHLH) and PAS-domain interaction surfaces, it binds E-box DNA elements and drives rhythmic transcriptional programs that underlie 24-hour physiological and behavioral cycles. - Source: PubMed
Publication date: 2026/05/26
Kamel Emadeldin MKhadrawy Sally MostafaAllam Ahmed AAhmed Noha AAlkhayl Faris F AbaLamsabhi Al Mokhtar - This study investigated the relationship between periodontitis and metabolic dysfunction-associated steatotic liver disease (MASLD), with a specific focus on the role of Porphyromonas gingivalis peptidylarginine deiminase (PPAD) carried by P. gingivalis-derived outer membrane vesicles (OMVs) in hepatic lipid metabolism. Clinical analyses revealed a positive correlation between periodontal disease severity and the fatty liver index (OR = 6.18, 95% CI: 2.36-16.13), a predictor of MASLD. In an obese mouse model of periodontitis, P. gingivalis-induced periodontitis accelerated MASLD progression, promoted hepatic lipid accumulation and increased inflammation. Since P. gingivalis OMVs had the advantage of traveling through the blood to the liver, we found that they demonstrated liver-specific accumulation, impairing fatty acid oxidation and increasing lipid deposition in hepatocytes, when injected into MASLD model mice via the tail vein. The critical role of PPAD was confirmed using the P. gingivalis and P. gingivalis strains, from which OMVs were isolated. The results of the in vivo and in vitro experiments indicated that PPAD-enriched OMVs mediated hepatic metabolic dysregulation via suppression of the circadian regulator NPAS2 and downstream inhibition of CYP4A10 expression, revealing a previously unrecognized PPAD-liver communication pathway. These findings highlight the urgent need for effective PPAD inhibitors and a deeper understanding of the interactions of PPAD with host proteins implicated in systemic diseases, underscoring the broader health impacts of periodontal disease. - Source: PubMed
Publication date: 2026/05/09
Liu YanqingXue XiaomengLi ZhaorongGe ZimingJiang MuzhouLiu JingboPan YapingLin Li - BMAL1 is a bHLH-PAS transcription factor complex that utilizes its bHLH (basic helix-loop-helix) domains to bind E-box motifs in DNA and tandem PAS (PER-ARNT-SIM) domains to heterodimerize and interact with regulatory proteins to generate circadian rhythms. PAS domains are evolutionarily conserved modules that frequently bind small molecule ligands within buried cavities to perform sensory and signal transduction functions. CLOCK and BMAL1 PAS domains have cavities that could be leveraged to regulate the transcription factor, and consequently, the circadian clock. Using NMR spectroscopy, we identified small molecules that bind within a cavity inside the PAS-A domain of CLOCK and its paralog NPAS2, which sits at an important flexible junction in the structured core of the heterodimer. We identified a gatekeeping mutant in the core of CLOCK PAS-A that significantly decreased ligand binding affinity. High-pressure NMR studies showed that ligand binding or the gatekeeping mutant significantly stabilized the domain. Finally, we showed that ligands induced dose-dependent displacement of CLOCK:BMAL1 from DNA . Together, these data demonstrate that small molecules can regulate DNA binding by the circadian transcription factor CLOCK:BMAL1 through occupancy of a PAS domain cavity. - Source: PubMed
Publication date: 2026/04/14
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