PCR-Tubes 0,2 ml flat cap (transparent, thin walled, free of PCR-inhibitors)
- Known as:
- PCR test kit-Tubes 0,2 milliliter flat cap (clear, walled, free PCR test kit-inhibitors)
- Catalog number:
- a22203
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- GeneON
- Gene target:
- PCR-Tubes 2 flat cap (transparent thin walled free PCR-inhibitors)
Related genes to: PCR-Tubes 0,2 ml flat cap (transparent, thin walled, free of PCR-inhibitors)
- Gene:
- TMEM159 NIH gene
- Name:
- transmembrane protein 159
- Previous symbol:
- -
- Synonyms:
- promethin
- Chromosome:
- 16p12.3
- Locus Type:
- gene with protein product
- Date approved:
- 2006-06-14
- Date modifiied:
- 2016-10-05
Related products to: PCR-Tubes 0,2 ml flat cap (transparent, thin walled, free of PCR-inhibitors)
Related articles to: PCR-Tubes 0,2 ml flat cap (transparent, thin walled, free of PCR-inhibitors)
- The Seipin protein is a conserved key component in the biogenesis of lipid droplets (LDs). Recently, a cooperation between human Seipin and the Lipid droplet assembly factor 1 (LDAF1) was described. LDAF1 physically interacts with Seipin and the holocomplex safeguards regular LD biogenesis. The function of LDAF1 proteins outside mammals is less clear. In yeast, the lipid droplet organization (LDO) proteins, which also cooperate with Seipin, are the putative homologs of LDAF1. While certain functional aspects are shared between the LDO and mammalian LDAF1 proteins, the relationship between the proteins is under debate. Here, we identify the Drosophila melanogaster protein CG32803, which we re-named to dmLDAF1, as an insect member of this protein family. dmLDAF1 decorates LDs in cultured cells and in vivo and the protein is linked to the fly and mouse Seipin proteins. Altering the dmLDAF1 abundance affects LD size, number and overall lipid storage amounts. Our results suggest that the LDAF1 proteins thus fulfill an evolutionarily conserved function in the biogenesis and biology of LDs. - Source: PubMed
Publication date: 2020/12/09
Chartschenko EugeniaHugenroth MarieAkhtar IrfanDroste AndreaKolkhof PetraBohnert MariaBeller Mathias - Lipids act as building blocks for all cellular membranes and as key energy carriers. Neutral storage lipids are packaged into specialized organelles termed Lipid Droplets (LDs). LDs dynamically respond to the metabolic state of the cell, and undergo cycles of de novo biogenesis, growth, shrinkage, and consumption. How these processes are mediated on a molecular level is a key objective of the LD field. The yeast Lipid Droplet Organization (LDO) proteins and the human promethin/TMEM159/LDAF1 are newly identified molecular players involved in different aspects of the life cycle of LDs. These factors show remote homology to each other, and are physically and functionally linked to seipin, a central component in LD formation and adipogenesis. - Source: PubMed
Publication date: 2020/05/08
Bohnert Maria - Lipid droplets (LDs) originate from the endoplasmic reticulum (ER) to store triacylglycerol (TG) and cholesterol esters. The ER protein seipin was shown to localize to ER-LD contacts soon after LDs form, but what determines the sites of initial LD biogenesis in the ER is unknown. Here, we identify TMEM159, now re-named lipid droplet assembly factor 1 (LDAF1), as an interaction partner of seipin. Together, LDAF1 and seipin form an ∼600 kDa oligomeric complex that copurifies with TG. LDs form at LDAF1-seipin complexes, and re-localization of LDAF1 to the plasma membrane co-recruits seipin and redirects LD formation to these sites. Once LDs form, LDAF1 dissociates from seipin and moves to the LD surface. In the absence of LDAF1, LDs form only at significantly higher cellular TG concentrations. Our data suggest that the LDAF1-seipin complex is the core protein machinery that facilitates LD biogenesis and determines the sites of their formation in the ER. - Source: PubMed
Publication date: 2019/11/07
Chung JeeyunWu XudongLambert Talley JLai Zon WengWalther Tobias CFarese Robert V - Seipin (BSCL2/SPG17) is a key factor in lipid droplet (LD) biology, and its dysfunction results in severe pathologies, including the fat storage disease Berardinelli-Seip congenital lipodystrophy type 2, as well as several neurological seipinopathies. Despite its importance for human health, the molecular role of seipin is still enigmatic. Seipin is evolutionarily conserved from yeast to humans. In yeast, seipin was recently found to cooperate with the lipid droplet organization (LDO) proteins, Ldo16 and Ldo45, two structurally-related proteins involved in LD function and identity that display remote homology to the human protein promethin/TMEM159. In this study, we show that promethin is indeed an LD-associated protein that forms a complex with seipin, and its localization to the LD surface can be modulated by seipin expression levels. We thus identify promethin as a novel seipin partner protein. - Source: PubMed
Publication date: 2019/03/21
Castro Inês GEisenberg-Bord MichalPersiani ElisaRochford Justin JSchuldiner MayaBohnert Maria - Arousal affects cognition, emotion, and behavior and has been implicated in the etiology of psychiatric disorders. Although environmental conditions substantially contribute to the level of arousal, stable interindividual characteristics are well-established and a genetic basis has been suggested. Here we investigated the molecular genetics of brain arousal in the resting state by conducting a genome-wide association study (GWAS). We selected N = 1877 participants from the population-based LIFE-Adult cohort. Participants underwent a 20-min eyes-closed resting state EEG, which was analyzed using the computerized VIGALL 2.1 (Vigilance Algorithm Leipzig). At the SNP-level, GWAS analyses revealed no genome-wide significant locus (p < 5E-8), although seven loci were suggestive (p < 1E-6). The strongest hit was an expression quantitative trait locus (eQTL) of TMEM159 (lead-SNP: rs79472635, p = 5.49E-8). Importantly, at the gene-level, GWAS analyses revealed significant evidence for TMEM159 (p = 0.013, Bonferroni-corrected). By mapping our SNPs to the GWAS results from the Psychiatric Genomics Consortium, we found that all corresponding markers of TMEM159 showed nominally significant associations with Major Depressive Disorder (MDD; 0.006 ≤ p ≤ 0.011). More specifically, variants associated with high arousal levels have previously been linked to an increased risk for MDD. In line with this, the MetaXcan database suggests increased expression levels of TMEM159 in MDD, as well as Autism Spectrum Disorder, and Alzheimer's Disease. Furthermore, our pathway analyses provided evidence for a role of sodium/calcium exchangers in resting state arousal. In conclusion, the present GWAS identifies TMEM159 as a novel candidate gene which may modulate the risk for psychiatric disorders through arousal mechanisms. Our results also encourage the elaboration of the previously reported interrelations between ion-channel modulators, sleep-wake behavior, and psychiatric disorders. - Source: PubMed
Publication date: 2018/04/27
Jawinski PhilippeKirsten HolgerSander ChristianSpada JanekUlke ChristineHuang JueBurkhardt RalphScholz MarkusHensch TilmanHegerl Ulrich