ATP1b1 ELISA kit
- Known as:
- ATP1b1 Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- DL-ATP1b1-Mu
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- WDSTD
- Gene target:
- ATP1b1 ELISA kit
Related genes to: ATP1b1 ELISA kit
- Gene:
- ATP1B1 NIH gene
- Name:
- ATPase Na+/K+ transporting subunit beta 1
- Previous symbol:
- ATP1B
- Synonyms:
- -
- Chromosome:
- 1q24.2
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2016-02-10
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- Microplastics have been established as a novel environmental contaminant, while bisphenol A represents a common endocrine-disrupting chemical. However, the combined toxicity of both pollutants on the gills of marine crustaceans remains underexplored. This study investigated the possible risks associated with co-exposure to MPs and BPA on the gills of Portunus trituberculatus. Crabs were exposed to 100 μg/L BPA, 10 mg/L MPs, and a combination of 100 μg/L BPA + 10 mg/L MPs for 21 days. Histological analysis revealed that both MPs and BPA significantly compromised gill architecture. Transcriptomic analysis identified 1766 differentially expressed transcripts under varying exposure conditions, which were implicated in biological processes associated with oxidative stress, ion regulation, and apoptosis. The presence of MPs, BPA, and their co-exposure resulted in a reduction of sodium/potassium-transporting ATPase subunit beta-1 expression levels, ATPase activities, ATP content, and ion concentrations in the gills when compared to the control group. Notably, MPs, BPA and their combined treatment induced ROS and HO accumulation, and the upregulation of catalase and superoxide dismutase activities, which could potentially impact cell apoptosis. These results suggest that MPs and BPA may adversely affect oxidative damage, ion content, ion regulatory proteins, ion transport ATPase activity, apoptosis and their related gene expression in the gills of P. trituberculatus. Besides, integrated biomarker response values indicated that co-treatment resulted in greater gill toxicity. This comprehensive understanding highlights the imperative for preemptive measures to mitigate the adverse effects of environmental pollutants on ecological health, while providing valuable insights into the relevant molecular pathways. - Source: PubMed
Publication date: 2026/02/02
Wang XiaotianWei ZhengjiaHuo XunjieGe XueruiRen JiayuanChen XiaocongZhang Tao - The development of ice crystals during the freezing process can be detrimental to the viability and fertilization capacity of frozen-thawed spermatozoa. The unique properties of antifreeze proteins allow them to inhibit the formation of ice crystals during cell cryopreservation. - Source: PubMed
Publication date: 2026/01/23
Ibrahim SaddahAbdou MohamedYu Il-Jeoung - NRG1 fusions are unique oncogenic drivers that activate the HER3/HER2/PI3K pathway. The FDA granted Accelerated Approval to a HER2/HER3 antibody, zenocutuzumab, for treatment of NRG1 fusion-positive (NRG1+) non-small-cell lung and pancreatic cancer (PDAC). The optimal detection methods and clinicopathologic features of patients with NRG1+ cancer have not been systematically studied. We review NRG1+ cancer and focus on outcomes in PDAC. - Source: PubMed
Publication date: 2025/12/13
Schram Alison MYang Soo-RyumKahn GenessaVelasco RogelioRepetto MatteoKinh Gian Do RichardDiNapoli SaraSukhadia PurvilTroxel MeganOzcan KeremTarcan ZeynepLadanyi MarcHarding James JDrilon AlexanderBasturk OlcaO'Reilly Eileen M - Eggs represent an accessible and nutrient-dense source of high-quality animal protein, and decades of selective breeding have markedly elevated reproductive output in commercial laying hens. However, sustaining elevated productivity while improving eggshell integrity presents a critical challenge, as the molecular mechanisms of eggshell strength remain unclear. In this study, phenotypic assessment of eggshell strength was combined with single-cell transcriptomic profiling of the uterus from high- and low-strength groups, transcriptomic analysis of multiple tissues, and quantitative proteomic analysis of uterine fluid. Serum calcium and phosphorus levels did not differ significantly between groups. A single-cell atlas of the Rhode Island Red uterus was successfully generated for the first time, identifying nine distinct cell populations encompassing smooth muscle, epithelial, endothelial, and immune subsets. Integration of transcriptomic and proteomic datasets revealed that genes encoding collagens ( / , / , , and / / ), solute carriers ( / , , / , and ), ATPases ( , , / , / , and ), calcium voltage-gated channels ( , , and ), annexins ( and ), and integrins ( and ) were key molecular determinants associated with variation in eggshell strength. These genes were primarily enriched in signaling cascades involved in focal adhesion, actin cytoskeleton regulation, extracellular matrix (ECM)-receptor interactions, and calcium signaling. Notably, collagen family genes were predominantly localized to smooth muscle cells, consistent with the tissue remodeling and uterine inversion that occur during shell calcification, which may enhance spatial proximity between calcium ions and matrix proteins. These findings establish a multi-omics framework for understanding the uterine regulatory mechanisms underlying eggshell formation and offer a molecular foundation for breeding strategies aimed at prolonging laying cycles while preserving shell quality. - Source: PubMed
Zhang Xiao-KeChen Ji-LanSun Yan-YanLi QinMa Peng-YunDu Hong-FengYang Han-HanLi Xin-YiXu Xin-YingMa HuiYuan Jing-WeiLi Yun-Lei - Porcine reproductive and respiratory syndrome virus (PRRSV) is an immune-suppressive pathogen that poses a significant challenge to the global swine industry. The mechanism by which PRRSV regulating host inflammation to evade innate immunity remains unclear. Here, Na /K-ATPase beta1 subunit (ATP1B1), a pivotal antiviral protein, was shown to interact with PRRSV nsp6, a tiny viral protein encoded by ORF1a. ATP1B1 stabilized the protein level of TRAF6 by downregulating K48-linked ubiquitination of TRAF6, thus triggering NF-κB signaling and inflammatory response. Moreover, PRRSV nsp6 competetively interacted with ATP1B1 via the site of Leu 3 and impaired the formation of ATP1B1-TRAF6 complex, leading to TRAF6 proteasomal degradation and compromised inflammatory response. PRRSV with the corresponding mutation in nsp6 L3S was successfully rescued but presented defective virus growth in the late stage of infection, especially under the inflammation condition induced by either ATP1B1 overexpression or poly (I:C) stimulation. In addition, the halt in PRRSV replication was induced by treatment with autophagy inhibitor BafA1 during virus passage. L3S mutant virus impaired the recovery of virus growth even after the removal of BafA1, indicating the key role of nsp6 in sustaining virus vitality under innate immunity. Taken together, these results elucidate the functional mechanism by which PRRSV alleviates the inflammatory response to promote successful virus proliferation and growth recovery from the host innate immune response. - Source: PubMed
Publication date: 2025/11/13
Yang HaotianGu HanQiu HeLi BichengXu JidongCao TongLiuyang DuLi XiaoliangHe Fang