CD95 _ FAS
- Known as:
- CD95 _ Fas Cell Surface Death Receptor
- Catalog number:
- AM05203AC-N
- Product Quantity:
- 100 Tests
- Category:
- -
- Supplier:
- ACR
- Gene target:
- CD95 _ FAS
Ask about this productRelated genes to: CD95 _ FAS
- Gene:
- FAS NIH gene
- Name:
- Fas cell surface death receptor
- Previous symbol:
- FAS1, APT1, TNFRSF6
- Synonyms:
- CD95, APO-1
- Chromosome:
- 10q23.31
- Locus Type:
- gene with protein product
- Date approved:
- 1992-06-25
- Date modifiied:
- 2019-04-23
Related products to: CD95 _ FAS
Related articles to: CD95 _ FAS
- Sulfur is a vital macroelement for soil fertility and crop growth, and its bioavailability is converted with electron flux. To determine the effect of biological electron transfer on the sulfur cycle in soil, a microbial electrochemical system (MES) was established to amplify the efficiency of extracellular electron transfer. Results showed that biocurrent obviously promoted the reduction of water-soluble SO to S, and afterward reoxidised to fulvic acid sulfur (FAS, 32% increment) instead of humic acid sulfur (HAS, 77% decrement). The δFAS values (12‰ to 24‰) were consistent with the typical isotopic signatures of dissimilatory sulfate reduction, while the δHAS values (-40‰ to -60‰) matched the assimilatory sulfate reduction. Meanwhile, the assimilatory SO reduction to cysteine improved with a 30%-33% increase for the NAD/NADH and secretion of cytochrome c to support robust redox. Essentially, the precursor-product pairs of desulfonation were enhanced by 26%-93%. Compared to a 6% contribution of HAS, the formation of cysteine accounted for 55% of the electron transport flux. According to screening 32 sulfur-transforming genes, 609 genera were identified, especially 31%-84% proliferation for Desulfatitalea. This study reveals ways of organic sulfur conversion mediated by electron transfer, which can assist the biological amendment of sulfur bioavailability in soil. - Source: PubMed
Sun JialuYang YueweiYu XinZhang XiaolinYang PinpinLiu BingyangChen YaliWang DejunPeng XinhongLi Xiaojing - - Source: PubMed
Publication date: 2026/05/04
Nguyen Tan VANPoyarkov Nikolay ATran Thinh GiaKennedy-Gold Stevie ROhler Annemarie - We here report the immature stages and novel host plant records for six species in the nymphalid subtribe Euptychiina, which are documented based on populations found in the Madre de Dios department, Peru: (Butler, 1867), (Möschler, 1876), (Butler, 1867), (Stoll, 1780), (Butler, 1867), Lamas & Nakahara, 2022. We also report new host plant records for two euptychiine species: (Linnaeus, 1767) and (C. Felder & R. Felder, 1867). A total of eight euptychiine species are discussed in the present study and the majority of new host plant records for them belong to the family Poaceae except for which was found feeding on seedlings of (Arecaceae). We provide photos of documented immature stages and host plants for species discussed herein, as well as DNA barcode data for selected taxa. - Source: PubMed
Publication date: 2026/01/13
Nakahara ShinichiVega YeisonCorahua-Espinoza ThaliaKabir JamalMaclure CalumDuerr NathanGallice GeoffreyCervantes-Martinez JoselinArteaga Zunilda EscalanteTejeira RafaelCcahuana RodrigoBaine Quinlyn - A recent study sheds light on the question of how separate tissues come together to build functional organ systems with connected luminal chambers. - Source: PubMed
Gredler Marissa L - FatB acyl-ACP thioesterases play an important role in plant fatty acid metabolism, determining the chain length and saturation of acyl groups that feed both storage oil and membrane lipid biosynthesis. In sunflower (Helianthus annuus L.), only one isoform, HaFatB1, has been characterized to date. Here, we report the identification and functional characterization of a novel sunflower plastidial thioesterase, HaFatB2, which exhibits low expression in developing seeds but is relatively abundant in leaves, suggesting a metabolic role beyond oil biosynthesis. Structural modelling and molecular docking predicted efficient accommodation of palmitoyl- and oleoyl-ACPs, a preference confirmed by in vitro assays and kinetic studies. When expressed in Escherichia coli, HaFatB2 markedly modified the fatty acid profile, leading to the unexpected accumulation of 4-hydroxymyristic acid (23% of total FAs), a rare fatty acid with potential industrial relevance. In contrast, expression in the photosynthetic cyanobacterium Anabaena sp. PCC 7120 and in Nicotiana benthamiana leaves did not significantly alter fatty acid composition, likely due to differences in substrate availability and endogenous regulatory mechanisms. Altogether, these findings identify HaFatB2 as a thioesterase with high preference for the export of palmitic and oleic fatty acids and highlight its biotechnological potential for producing uncommon hydroxylated fatty acids in heterologous systems. - Source: PubMed
Publication date: 2026/07/02
Martins-Noguerol RaquelSánchez RosarioMoreno-Pérez Antonio JMuro-Pastor Alicia MVenegas-Calerón MónicaMartínez-Force EnriqueSalas Joaquín J