AQP9 ELISA kit
- Known as:
- AQP9 Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- DL-AQP9-Hu
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- WDSTD
- Gene target:
- AQP9 ELISA kit
Related genes to: AQP9 ELISA kit
- Gene:
- AQP7 NIH gene
- Name:
- aquaporin 7
- Previous symbol:
- AQP7L
- Synonyms:
- AQP9, AQPap
- Chromosome:
- 9p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-04-10
- Date modifiied:
- 2016-10-05
- Gene:
- AQP9 NIH gene
- Name:
- aquaporin 9
- Previous symbol:
- -
- Synonyms:
- SSC1, HsT17287
- Chromosome:
- 15q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-28
- Date modifiied:
- 2016-10-05
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- The aquaporin genes (aqps) are widely distributed among vertebrates. In cartilaginous fish, aqp3 and aqp10 are duplicated, whereas many species have lost aqp8. While the solute permeability of aquaglyceroporins and Aqp8 exhibits significant diversity, systematic evaluations of their activity within species are limited. Consequently, we conducted a comprehensive analysis of the aqps in various cartilaginous fish genome databases. Our analysis revealed that the sharpnose sevengill shark (Heptranchias perlo) and North Pacific spiny dogfish (Squalus suckleyi) possess all aqp genes found in cartilaginous fish, rendering them suitable for comparative analysis of Aqp activity. The activity of all aquaglyceroporins and Aqp8 in the sharpnose sevengill shark was analyzed using Xenopus oocyte swelling assays. The water permeability of Aqp3c2, Aqp8, Aqp9, Aqp10c1, and Aqp10c2; the glycerol permeability of Aqp3c2, Aqp9, and Aqp10c2; the urea permeability of Aqp3c2, Aqp8, Aqp9, and Aqp10c2; and the boric acid permeability of Aqp8 and Aqp9 were determined. The urea and boric acid permeabilities of Aqp9 were higher than those of other Aqps. Our results provide genomic evidence for the loss of aqp7 and further elucidate the diversification of aqp8 in cartilaginous fishes. Moreover, the urea permeability of Aqp9 suggests a functional role in their unique urea-based osmoregulation strategy. - Source: PubMed
Hidaka ShinichiroNagashima AyumiKato Akira - Aquaporins (AQPs) are transmembrane channel proteins that transport water and small solutes. Their dysregulation in cancer reveals functions beyond maintaining osmotic balance. This review summarizes that AQPs drive tumor progression through three core mechanisms: metabolic reprogramming, enhanced motility, and remodeling of the immune microenvironment. Specifically, AQP3, AQP7, and AQP9 serve as metabolic hubs for glycerol, while AQP3 and AQP8 help maintain redox homeostasis. AQP1 and AQP4 facilitate cell migration via hydrodynamic mechanisms, and AQP5 promotes invasion through signaling pathways such as Ras/NF-κB. In immune regulation, AQP9 and AQP3 modulate immune cell function by transporting metabolites, and AQP1 influences angiogenesis. Other isoforms, including AQP0, AQP2, AQP6, AQP10, and AQP11, also play roles in malignancy. Collectively, AQPs form a multifunctional network linking tumor metabolism, physical properties, and immunity, offering insights for novel diagnostic and therapeutic strategies. However, tissue-specific functions, complex regulatory mechanisms, and challenges in developing targeted therapies remain significant hurdles in translational medicine. - Source: PubMed
Publication date: 2026/03/26
Qu KexinWang RuiBi YingweiLiu YuxinYi BolinWang Jianbo - Zingerone (ZO) found in Zingiber officinale, belonging to methoxyphenol family and its related derivatives, has been reported to ameliorate nonalcoholic fatty liver disease (NAFLD) by enhancing lipid metabolism and exerting hepatoprotective effects. However, the effect of ZO on hepatic AQP9 expression, along with the underlying mechanisms driving its hepatoprotective potential, remains largely unexplored. This study aims to investigate the modulatory effect of ZO on AQP9 expression in a steatosis cell model through experimental and in silico analyses, providing insights that could contribute to therapeutic interventions for NAFLD. Oleate-palmitate (OA-PA) and free fatty acids (FFA) induced hepatic steatosis was established in Hepa 1-6 cells as in vitro model of NAFLD. Cell cytotoxicity and lipid accumulation were evaluated by MTT assay and Oil-RedO staining, respectively. ZO pretreatment significantly attenuated intracellular lipid accumulation and altered the expression of aquaporins, resulting in downregulation of AQP9 and upregulation of AQP3 and AQP7, as demonstrated by qRT-PCR analysis. These findings suggest that ZO ameliorates OA-PA induced hepatic steatosis primarily by inhibiting lipid accumulation and selectively modulating aquaporin expression. Molecular docking analysis revealed that ZO forms a complex with AQP9 with the minimum binding energy of -6.2 kcal/mol. The molecular dynamics simulations showed that this complex stays stable across time with consistent RMSD and low RMSF values. In summary, pre-treatment with ZO has beneficial health effects by inhibiting lipid accumulation and selectively modulating aquaporin expression, highlighting its potential in preventing fatty liver disease. - Source: PubMed
Publication date: 2026/03/12
Mate Payal SA T Fathima JasminRani SumanNagpal AnjuAshutosh Meena Sunita - 1. The objective of this study was to evaluate the effects of dietary electrolyte balance (DEB) concentrations on growth performance, heat sensitivity biomarkers and water and ion metabolism of meat ducks under heat stress (HS).2. A total of 400, 28-d-old Cherry Valley male meat ducks were randomly divided into five treatment groups (eight pens per treatment with 10 birds/pen), with dietary different DEB values, 120, 160, 200, 240 and 280 mmol/kg.3. Ducks in the 240-mmol/kg DEB group had a tendency ( = 0.098) for increased body weight at 41 d of age. The 240-mmol/kg DEB group displayed the numerically highest daily gain, the best FCR and lowest mortality among all treatment groups. Serum corticosterone (CORT) concentration in ducks from the 240-mmol/kg DEB group was significantly lower than that in the 280-mmol/kg DEB group ( < 0.05) and chlorine concentration had a tendency to fall ( = 0.083).4. The 240-mmol/kg DEB group significantly upregulated the expression of aquaporins () in the small intestine ( and ), kidney (, , ) and thenasal salt gland ( and ). In addition, it upregulated the expression of ion transporter ( cotransporter and /) in the small intestine, kidney and nasal salt gland.5. Based on the overall benefits in growth performance, biochemical measures, tissue AQP and expression of ion transporters, an optimal level of DEB in diets for heat stressed ducks was 240 mmol/kg. - Source: PubMed
Publication date: 2026/01/12
Liu HTian GZhang KDing XBai SWang JLiu YXuan YLi SZeng Q - The aquaporin (AQP) gene family plays a critical role in water balance and osmotic regulation, yet its function and regulatory mechanisms in plateau reptiles remain poorly understood. In this study, we systematically identified 10 AQP genes in the Qinghai toad-headed agama () based on whole-genome data, and conducted a comprehensive analysis of their physicochemical properties, phylogenetic relationships, conserved domains, gene structures, and expression patterns. The results showed that the AQP genes of are predicted to localize to the plasma membrane and exhibit significant tissue-specific expression, with the highest levels detected in the kidney and liver. Under low-temperature stress, multiple AQP genes displayed dynamic expression patterns during the stress and recovery phases. Specifically, , , and were persistently downregulated in the liver, kidney, and brain, whereas , , and were initially upregulated during early cold exposure but significantly downregulated during recovery, suggesting their coordinated roles in energy metabolism and water conservation. This study provides evidence supporting the involvement of the AQP gene family in the adaptation of to the cold and arid plateau environment, providing new insights into the regulatory mechanisms of water metabolism in reptiles. - Source: PubMed
Publication date: 2025/12/07
Zhang YurongYang PingLi XinyangWang Jia