AOC3 ELISA kit
- Known as:
- AOC3 Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- DL-AOC3-Mu
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- WDSTD
- Gene target:
- AOC3 ELISA kit
Related genes to: AOC3 ELISA kit
- Gene:
- AOC3 NIH gene
- Name:
- amine oxidase copper containing 3
- Previous symbol:
- -
- Synonyms:
- VAP1, HPAO, VAP-1
- Chromosome:
- 17q21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-03
- Date modifiied:
- 2019-01-18
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- Human primary amine oxidase (AOC3) is a membrane-anchored protein expressed on the luminal surface of the vascular endothelium at sites of inflammation. It binds via protein-protein interactions to the CE-loops of the C2 domain in Siglec-9 and Siglec-10, but the exact mechanism of interaction is unknown on an atomic level. The AOC3 binding to a radiolabeled Siglec-9 peptide can be used to image inflammation by positron emission tomography (PET). In the present study, a combination of computational and wet lab experiments is used to map the binding of the original and designed shorter Siglec-derived peptides to AOC3, to determine what features in the CE-loop are important for the interaction. To select the peptides for wet lab studies, docking and molecular dynamics simulations were first conducted to predict the binding mode of the peptides in the AOC3 active site channel, and MMGBSA calculations to predict binding energies. Selected peptides were further analyzed through microscale thermophoresis to affirm binding and saturation transfer difference NMR (STD-NMR) to determine the binding epitope to AOC3. Our results unveil that the shorter cyclic Siglec-9 and Siglec-10 peptides derived from the CE-loop bind to AOC3. Our results summarize that a tryptophan and an arginine in both peptides are important for the AOC3 interactions, but their binding mode differs slightly. Our results suggest that the designed shorter Siglec-9 peptide could be advantageous in PET imaging of inflammation and the binding properties of the Siglec-10 peptides hint a biological role for the CE-loop of the C2 domains in Siglec-10. - Source: PubMed
Publication date: 2026/08/05
Alix MarionLonden MikaelGuédez GabrielaGrosso Ana SofiaMarcelo FilipaCabrita EuricoSalminen Tiina Annamaria - Resveratrol and its glycoside polydatin are high-value stilbene metabolites with broad pharmacological potential, but their natural accumulation in plants is usually limited. Endophytic fungal elicitation may provide a useful approach for improving the accumulation of these compounds. In this study, three crude elicitors prepared from the endophytic fungus Plectosphaerella sp. J-G was evaluated for its effects on seedling growth and stilbene accumulation in Rumex gmelinii Turcz. ex Ledeb. sterile seedlings. Among the tested elicitor types, concentrations, and treatment durations, the mycelial homogenate elicitor at 250 mg·L⁻¹ for 10 days showed a relatively strong induction effect. Under this condition, the total content of resveratrol and polydatin in roots increased by 272.50% compared with the time-matched 10-day sterile water control, from 750.60 to 2795.97 µg·g⁻¹. This treatment was also accompanied by 22.02% higher plant height and 165.63% greater root fresh weight. Transcriptome sequencing and real-time quantitative PCR validation were used to examine transcriptional changes associated with this response. Eight upregulated genes, including IAA, CYP73A/C4H, LDH, SAUR, STS, AOC3, ADH1, and POD, were potentially associated with precursor supply, stilbene/phenylpropanoid biosynthesis, defense response, and auxin-related growth regulation. Several transcription factor families, such as MYB, AP2/ERF, and WRKY, may also be related to the transcriptional response under J-G crude elicitor treatment. These results suggest that J-G crude elicitor treatment may be a useful induction strategy for increasing resveratrol and polydatin accumulation in RGT sterile seedlings and provide candidate genes for future functional validation. - Source: PubMed
Publication date: 2026/07/31
Liang JingruZhang YangLi XintaoXu RuiyunDing Changhong - Dopa decarboxylase (DDC) is a candidate biomarker in Parkinson's disease (PD), but its levels are influenced by dopamine replacement therapy (DRT), complicating interpretation. We used high-throughput proteomics to analyze serum and CSF samples from PD patients, individuals with idiopathic REM-sleep behaviour disorder, and controls to assess DRT effects. In serum, DDC increased and prolactin and AOC3 decreased with higher levodopa equivalent daily doses, showing drug class-specific associations. Longitudinally, serum DDC and prolactin levels changed with DRT, while AOC3 remained stable. In CSF, DDC was elevated regardless of treatment, while prolactin was reduced only in treated PD. These results indicate that serum changes in DDC, prolactin, and AOC3 primarily reflect treatment exposure rather than disease biology. Our findings highlight the need to account for medication effects in proteomic studies, identify AOC3 as a novel DRT-sensitive protein, and support the potential of treatment-responsive proteins as pharmacodynamic markers in PD. - Source: PubMed
Publication date: 2026/07/04
van Hillegondsberg LudoAhmad ShahzadZerenner TanjaLawton MichaelGroenewald KarolienFletcher MicahIanniello AyanBen-Shlomo YoavWade-Martins RichardPiazza PaoloTaylor AvigailThompson Alexander GHu Michele T - Studies have shown that dysregulation of the gut microbiota (GM) plays a crucial role in the development of endometriosis (EMs). Study aimed to investigate the potential of protective GM metabolites in treating EM through network pharmacology and Mendelian randomization (MR), opening new avenues for targeted therapeutic strategies. - Source: PubMed
Publication date: 2026/06/11
Zhou JunShan TiehuLi YanZhang Guangmei - Assessing disease activity in giant cell arteritis (GCA) remains challenging, as existing clinical, laboratory and imaging biomarkers lack specificity. This proof-of-concept study explored the diagnostic potential of vascular adhesion protein-1 (VAP-1) targeting [Ga]Ga-(1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid) DOTA-sialic acid-binding immunoglobulin-like lectin-9 (Siglec-9) positron emission tomography-CT (PET/CT) as an inflammation-specific molecular imaging biomarker in newly diagnosed and relapsing GCA. - Source: PubMed
Publication date: 2026/06/11
Petzinna Simon MKüppers JimSchemmer BenediktJamin Raul NKirch Sophie-MarieBauer Claus-JürgenGheitasi RezaKernder Anna LGinzburg DanielBaerlecken Niklas TJung Gustav BAdamson Maike SEssler MarkusSchäfer Valentin S