LASS2 antibody - N-terminal region (ARP31922_P050)
- Known as:
- LASS2 (anti-) - N-terminal region (ARP31922_P050)
- Catalog number:
- arp31922_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- LASS2 antibody - N-terminal region (ARP31922_P050)
Related genes to: LASS2 antibody - N-terminal region (ARP31922_P050)
- Gene:
- CERS2 NIH gene
- Name:
- ceramide synthase 2
- Previous symbol:
- LASS2
- Synonyms:
- SP260, FLJ10243
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-09-10
- Date modifiied:
- 2015-08-24
Related products to: LASS2 antibody - N-terminal region (ARP31922_P050)
Related articles to: LASS2 antibody - N-terminal region (ARP31922_P050)
- The gut microbiome is a critical regulator of host health, but how it mediates the therapeutic effects of drugs targeting neurodegenerative diseases like diabetic cognitive impairment (DCI) is unclear. Here, we investigated whether the neuroprotective effects of the GLP-1 agonist semaglutide (SE) are linked to its modulation of the gut-brain axis. - Source: PubMed
Publication date: 2026/03/26
Qi LiqinKang HuiminLi XiaofenWang LijingLin YinchenZhan MenglanZeng FeihuiXiao ZhiwenLiu XiaoyingChen ZhouLiu Libin - Sirtuin 1 (Sirt1), a member of the sirtuin family, is integral to the regulation of energy homeostasis, cellular metabolism, and stress responses. While Sirt1 has been intensively studied in mammals, studies on this gene in aquatic animals, especially turbot, is relatively limited. In this study, the sirt1 gene was cloned. The open reading frame (ORF) of the Sirt1 consists of 2187 base pairs, encoding a 728-amino-acid protein that contains a SIR2 domain. Compared with the siRNA-NC group, Sirt1 knockdown resulted in a significant downregulation of mRNA expression levels of the tight junction proteins occludin, tricellulin, claudin3, and zo1, as well as protein levels of Occludin and ZO1, within the intestinal tissue of turbot. Concurrently, it markedly inhibited the expression of genes associated with ceramide synthesis (sptlc2, kdsr, cers1, cers2, cers3, smpdl3a, smpdl3b, neu1, glb1, gba1, and sgpp2) and ceramide catabolism (sgms1a, ugcg, b4galt, and sphk1) in the same tissue. Conversely, compared to the pcDNA3.1 group, Sirt1 overexpression significantly enhanced the mRNA expression levels of occludin, tricellulin, claudin3, claudin7, and zo1, along with the protein level of Occludin. Furthermore, Sirt1 overexpression significantly elevated the expression of genes involved in ceramide synthesis (cers2, cers3, smpd3, smpdl3b, neu1, glb1, gba1, sgpp2) and ceramide catabolism (sgms1a, galt, b4galt, and sphk1). These results suggest that Sirt1 may influence the intestinal mechanical barrier by acting on the metabolic balance of ceramide and altering the expression of intestinal tight junction proteins, thus playing a crucial role in maintaining the intestinal health of turbot. - Source: PubMed
Publication date: 2026/03/18
Ma XiuhuaLiu QianhuiMai KangsenZhang Yanjiao - The lung, a key organ for oxygen exchange, is particularly susceptible to high-altitude hypoxic stress. Hypoxia induces vascular impairment, which is characterized by vascular inflammatory responses and aging-like changes. Lipid metabolism has been shown to be closely associated with cellular homeostasis and membrane balance. However, the alterations in pulmonary lipid metabolism in response to high-altitude hypoxia are not fully characterized. In this study, model mice were subjected to a hypobaric chamber at an altitude of 5500 m for 3 days, and pulmonary microvascular endothelial cells (PMVECs) were cultured under 1% oxygen for 18 h to simulate the effects of acute severe hypoxia. High-altitude hypoxia significantly disrupted lung sphingolipid metabolism, accompanied by inflammation and aging-like changes in mice. Moreover, C24-Ceramide (Cer) and its synthase (CERS2) were significantly increased in PMVECs. C24-Cer was identified to bind to voltage-dependent anion channel 1 (VDAC1) (a mitochondrial outer membrane protein), which promoted mitochondrial DNA (mtDNA) release and subsequently induced the inflammation and aging-like changes by activating the cyclic guanosine monophosphate-adenosine monophosphate synthase-stimulator of interferon genes (cGAS-STING) pathway. Inhibition of C24-Cer or VDAC1 oligomerization by si-Cers2 or VBIT-4 could significantly reduce mtDNA release and alleviate inflammation and aging-like changes in the PMVECs and lung tissue under hypoxia. Our present work provides a novel and potential therapeutic target for high-altitude hypoxia-related vascular diseases. - Source: PubMed
Publication date: 2026/03/03
Xu JinGe YiLingZhang BinHe SiYuanCao QingLinLi PeiJieBu YingRuiBai YunGangZhang LinTan GuoDongMa JinXie ManJiang - - Source: PubMed
Publication date: 2026/02/19
Sun HuanMo LuyueCao MingjunTian YanlinMo LesongNi ZhenZhang ShaohuaHuang XiaheWang YingchunLam Sin ManShui Guanghou - Cuproptosis has been linked to Parkinson's disease (PD), but underlying genetic mechanisms remain unclear. We integrated multi-omic QTL data (methylation, gene expression, protein) with GWAS data of PD (discovery: GWAS Catalog; replication: UK Biobank/FinnGen/IEU). Integrated summary-data Mendelian randomization (SMR) with colocalization analyses revealed regulatory relationships involving 4 candidate genes (ISCA1, PDE6B, PTGES, and CERS2). Replication analyses demonstrated consistent CERS2/PDE6B methylation effects across cohorts. Experimental validation in MPTP-treated mice demonstrated that the copper chelator tetrathiomolybdate (TTM) robustly rescued motor deficits and prevented dopaminergic neurodegeneration. Mechanistically, TTM reversed core features of cuproptosis, including striatal copper accumulation and the destabilization of lipoylated TCA cycle proteins. TTM also normalized the expression of all four candidate genes, confirming a copper-dependent regulatory axis predicted by our SMR analysis. This study provides a functional link between cuproptosis-related genes and PD pathogenesis, highlighting copper dyshomeostasis as a key pathogenic driver and a potential therapeutic target. - Source: PubMed
Publication date: 2026/01/15
Zhang TingWang Yuwen