PFB-FDGlu (5-(Pentafluorobenzoylamino)Fluorescein Di-β-D-Glucopyranoside)
PFB-FDGlu (5-(Pentafluorobenzoylamino)Fluorescein Di-β-D-Glucopyranoside)
Invitrogen™

PFB-FDGlu (5-(Pentafluorobenzoylamino)Fluorescein Di-β-D-Glucopyranoside)

ß-グルコシダーゼ基質 5-(ペンタフルオロベンゾイルアミノ)フルオレセイン、di-ß-D-グルコピラノシド(PFB-FDGlu)は、ピノサイトーシスにより細胞にロードする際に、エンドソーム細胞やリソソーム細胞に局在するように見える緑色蛍光PFB-F色素(励起/最大発光約492/516詳細を見る
製品番号(カタログ番号)数量
P11947
または、製品番号P-11947
5 mg
製品番号(カタログ番号) P11947
または、製品番号P-11947
価格(JPY)
131,900
Each
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数量:
5 mg
ß-グルコシダーゼ基質

5-(ペンタフルオロベンゾイルアミノ)フルオレセイン、di-ß-D-グルコピラノシド(PFB-FDGlu

)は、ピノサイトーシスにより細胞にロードする際に、エンドソーム細胞やリソソーム細胞に局在するように見える緑色蛍光PFB-F色素(励起/最大発光約492/516 nm)を生成します。
研究用にのみ使用できます。診断用には使用いただけません。
仕様
細胞透過性細胞透過性
Green
励起/発光492⁄516
使用対象 (装置)フローサイトメーター
標識または色素Fluorescein
製品タイプSubstrate
数量5 mg
出荷条件室温
保存要件Freezer (-5°C to -30°C)
基質β‐グルコシダーゼ基質
検出法蛍光
形状Powder
Substrate Properties化学基質
基質タイプBeta-Glucosidase Substrate
Target EnzymeBeta-Glucosidase
Unit SizeEach
組成および保存条件
冷凍庫(-5~-30℃)に保存。

引用および参考文献 (16)

引用および参考文献
Abstract
Flow Cytometry Measurement of Glucocerebrosidase Activity in Human Monocytes.
Authors:Hughes LP,Halliday GM,Dzamko N
Journal:Bio-protocol
PubMed ID:33659542
Glucocerebrosidase (GCase) is an important enzyme for the metabolism of glycolipids. GCase enzyme deficiency is implicated in human disease and the efficient measurement of GCase activity is important for evaluating the efficacy of therapeutics targeting this enzyme. Existing approaches to measure GCase activity include whole blood mass spectrometry-based assays, where ... More
Tau accumulation in degradative organelles is associated to lysosomal stress.
Authors:Piovesana E,Magrin C,Ciccaldo M,Sola M,Bellotto M,Molinari M,Papin S,Paganetti P
Journal:Scientific reports
PubMed ID:37865674
Neurodegenerative disorders are characterized by the brain deposition of insoluble amyloidogenic proteins, such as α-synuclein or Tau, and the concomitant deterioration of cell functions such as the autophagy-lysosomal pathway (ALP). The ALP is involved in the degradation of intracellular macromolecules including protein aggregates. ALP dysfunction due to inherited defects in ... More
Development of screening strategies for the identification of paramylon-degrading enzymes.
Authors:Gissibl A,Care A,Sun A,Hobba G,Nevalainen H,Sunna A
Journal:Journal of industrial microbiology & biotechnology
PubMed ID:30806871
Enzymatic degradation of the β-1,3-glucan paramylon could enable the production of bioactive compounds for healthcare and renewable substrates for biofuels. However, few enzymes have been found to degrade paramylon efficiently and their enzymatic mechanisms remain poorly understood. Thus, the aim of this work was to find paramylon-degrading enzymes and ways ... More
Dysregulation of mitochondria-lysosome contacts by GBA1 dysfunction in dopaminergic neuronal models of Parkinson's disease.
Authors:Kim S,Wong YC,Gao F,Krainc D
Journal:Nature communications
PubMed ID:33753743
Mitochondria-lysosome contacts are recently identified sites for mediating crosstalk between both organelles, but their role in normal and diseased human neurons remains unknown. In this study, we demonstrate that mitochondria-lysosome contacts can dynamically form in the soma, axons, and dendrites of human neurons, allowing for their bidirectional crosstalk. Parkinson's disease ... More
The Parkinson's disease risk gene cathepsin B promotes fibrillar alpha-synuclein clearance, lysosomal function and glucocerebrosidase activity in dopaminergic neurons.
Authors:Jones-Tabah J,He K,Karpilovsky N,Senkevich K,Deyab G,Pietrantonio I,Goiran T,Cousineau Y,Nikanorova D,Goldsmith T,Del Cid Pellitero E,Chen CX,Luo W,You Z,Abdian N,Ahmad J,Ruskey JA,Asayesh F,Spiegelman D,Fahn S,Waters C,Monchi O,Dauvilliers Y,Dupré N,Miliukhina I,Timofeeva A,Emelyanov A,Pchelina S,Greenbaum L,Hassin-Baer S,Alcalay RN,Milnerwood A,Durcan TM,Gan-Or Z,Fon EA
Journal:Molecular neurodegeneration
PubMed ID:39587654
Variants in the CTSB gene encoding the lysosomal hydrolase cathepsin B (catB) are associated with increased risk of Parkinson's disease (PD). However, neither the specific CTSB variants driving these associations nor the functional pathways that link catB to PD pathogenesis have been characterized. CatB activity contributes to lysosomal protein degradation ... More