EasySep™小鼠TIL（CD45）正选试剂盒
产品号 #05796_C
无血清神经生理基础培养基，改善神经元活细胞成像和功能
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总览
"BrainPhys™成像专用培养基是一种无血清的神经元基础培养基（基于Cedric Bardy和Fred H. Gage发布的BrainPhys™配方），经过优化，适用于成像应用。BrainPhys™成像专用培养基的应用包括活细胞荧光成像（如钙成像和光遗传学）和神经元培养。该配方不仅去除了酚红，还对配方进行了改良，以减少背景荧光并增加反复暴露在光下的稳定性（M Zabolocki等）。Nat Comm, 2020)。"
分类
专用培养基
细胞类型
神经细胞，PSC衍生，神经元，多能干细胞
种属
人，小鼠，非人灵长类，其他物种，大鼠
应用
细胞培养，功能学筛选，免疫荧光，类器官培养
品牌
BrainPhys
研究领域
疾病建模，药物发现和毒理检测，神经科学，类器官
制剂类别
化学成分明确，无血清
实验数据
产品说明书及文档
请在《产品说明书》中查找相关支持信息和使用说明，或浏览下方更多实验方案。
应用领域
本产品专为以下研究领域设计，适用于工作流程中的高亮阶段。探索这些工作流程，了解更多我们为各研究领域提供的其他配套产品。
相关材料与文献
技术资料 (16)
文献 (4)
CFAP300 Loss-of-Function Mutations with Primary Ciliary Dyskinesia: Evidence from Ex Vivo and ALI Cultures
International Journal of Molecular Sciences 2025 Aug
Abstract
Primary ciliary dyskinesia (PCD) is a genetically heterogeneous disorder characterized by impaired mucociliary clearance due to defects in motile cilia. This study investigates the impact of loss-of-function mutations in the CFAP300 gene on the ciliary structure and function in three PCD patients. Using a multimodal approach, we integrated molecular genetic testing, transmission electron microscopy, the high-speed video microscopy assay and immunofluorescence staining to analyze ciliary motility and protein expression in both ex vivo and in vitro-obtained ciliary cells. Our results revealed that the pathogenic variant c.198_200delinsCC (p.Phe67ProfsTer10) in CFAP300 led to the absence of the functional CFAP300 protein, the complete loss of outer and inner dynein arms and immotile cilia. Air–liquid interface (ALI)-cultured cells from patients exhibited no ciliary beating, contrasting with healthy controls. Immunostaining confirmed the absence of CFAP300 in patient-derived cilia, underscoring its critical role in dynein arm assembly. These findings highlight the diagnostic utility of ALI cultures combined with functional and protein analyses for PCD, offering a clinically actionable framework that can be readily incorporated into standard diagnostic workflows.
Direct and indirect regulation of ?-glucocerebrosidase by the transcription factors USF2 and ONECUT2
NPJ Parkinson's Disease 2024 Oct
Abstract
Mutations in GBA1 encoding the lysosomal enzyme ?-glucocerebrosidase (GCase) are among the most prevalent genetic susceptibility factors for Parkinson’s disease (PD), with 10–30% of carriers developing the disease. To identify genetic modifiers contributing to the incomplete penetrance, we examined the effect of 1634 human transcription factors (TFs) on GCase activity in lysates of an engineered human glioblastoma line homozygous for the pathogenic GBA1 L444P variant. Using an arrayed CRISPR activation library, we uncovered 11 TFs as regulators of GCase activity. Among these, activation of MITF and TFEC increased lysosomal GCase activity in live cells, while activation of ONECUT2 and USF2 decreased it. While MITF, TFEC, and USF2 affected GBA1 transcription, ONECUT2 might control GCase trafficking. The effects of MITF, TFEC, and USF2 on lysosomal GCase activity were reproducible in iPSC-derived neurons from PD patients. Our study provides a systematic approach to identifying modulators of GCase activity and deepens our understanding of the mechanisms regulating GCase.
PP2A and GSK3 act as modifiers of FUS-ALS by modulating mitochondrial transport
Acta Neuropathologica 2024 Feb
Abstract
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease which currently lacks effective treatments. Mutations in the RNA-binding protein FUS are a common cause of familial ALS, accounting for around 4% of the cases. Understanding the mechanisms by which mutant FUS becomes toxic to neurons can provide insight into the pathogenesis of both familial and sporadic ALS. We have previously observed that overexpression of wild-type or ALS-mutant FUS in Drosophila motor neurons is toxic, which allowed us to screen for novel genetic modifiers of the disease. Using a genome-wide screening approach, we identified Protein Phosphatase 2A (PP2A) and Glycogen Synthase Kinase 3 (GSK3) as novel modifiers of FUS-ALS. Loss of function or pharmacological inhibition of either protein rescued FUS-associated lethality in Drosophila . Consistent with a conserved role in disease pathogenesis, pharmacological inhibition of both proteins rescued disease-relevant phenotypes, including mitochondrial trafficking defects and neuromuscular junction failure, in patient iPSC-derived spinal motor neurons (iPSC-sMNs). In FUS-ALS flies, mice, and human iPSC-sMNs, we observed reduced GSK3 inhibitory phosphorylation, suggesting that FUS dysfunction results in GSK3 hyperactivity. Furthermore, we found that PP2A acts upstream of GSK3, affecting its inhibitory phosphorylation. GSK3 has previously been linked to kinesin-1 hyperphosphorylation. We observed this in both flies and iPSC-sMNs, and we rescued this hyperphosphorylation by inhibiting GSK3 or PP2A. Moreover, increasing the level of kinesin-1 expression in our Drosophila model strongly rescued toxicity, confirming the relevance of kinesin-1 hyperphosphorylation. Our data provide in vivo evidence that PP2A and GSK3 are disease modifiers, and reveal an unexplored mechanistic link between PP2A, GSK3, and kinesin-1, that may be central to the pathogenesis of FUS-ALS and sporadic forms of the disease. The online version contains supplementary material available at 10.1007/s00401-024-02689-y.
更多信息
| 物种 | 人类, 其它物种, 大鼠, 小鼠, 非人灵长类 |
|---|---|
| 配方 | 化学成分, 无血清 |
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