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Zitierungen und Referenzen (16)
Invitrogen™
PFB-FDGlu (5-(Pentafluorobenzoylamino)Fluorescein Di-β-D-Glucopyranoside)
Das ß-Glucosidase-Substrat, 5-(Pentafluorobenzoylamino)Fluorescein di-ß-D-Glucopyranosid (PFB-FDGlu) liefert den grün-fluoreszierenden PFB-F-Farbstoff (Anregung/Emissionsmaxima ∼492/516 nm), der bei der Belastung in Zellen durch PinocytoseWeitere Informationen
| Katalognummer | Menge |
|---|---|
| P11947 auch als P-11947 bezeichnet | 5 mg |
Katalognummer P11947
auch als P-11947 bezeichnet
Preis (EUR)
920,00
Each
Menge:
5 mg
Preis (EUR)
920,00
Each
Das ß-Glucosidase-Substrat,
5-(Pentafluorobenzoylamino)Fluorescein di-ß-D-Glucopyranosid (PFB-FDGlu)
liefert den grün-fluoreszierenden PFB-F-Farbstoff (Anregung/Emissionsmaxima ∼492/516 nm), der bei der Belastung in Zellen durch Pinocytose zu endosomalen und lysosomalen Kompartimenten zu lokalisieren scheint.
5-(Pentafluorobenzoylamino)Fluorescein di-ß-D-Glucopyranosid (PFB-FDGlu)
liefert den grün-fluoreszierenden PFB-F-Farbstoff (Anregung/Emissionsmaxima ∼492/516 nm), der bei der Belastung in Zellen durch Pinocytose zu endosomalen und lysosomalen Kompartimenten zu lokalisieren scheint.
Nur für Forschungszwecke. Nicht zur Verwendung bei diagnostischen Verfahren.
Specifications
ZellpermeabilitätMembrangängig
FarbeGreen
Anregung/Emission492⁄516
Zur Verwendung mit (Geräte)Durchflusszytometer
Marker oder FarbstoffFluorescein
ProdukttypSubstrate
Menge5 mg
VersandbedingungRaumtemperatur
LagerungsbedingungenFreezer (-5°C to -30°C)
SubstratBeta-Galactosidase-Substrat
NachweisverfahrenFluoreszent
FormPowder
Substrate PropertiesChemisches Substrat
SubstrattypBeta-Glucosidase Substrate
Target EnzymeBeta-Glucosidase
Unit SizeEach
Inhalt und Lagerung
Im Gefrierschrank lagern (-5 bis -30 °C).
Zitierungen und Referenzen (16)
Zitierungen und Referenzen
Abstract
Activation and Purification of ß-Glucocerebrosidase by Exploiting its Transporter LIMP-2 - Implications for Novel Treatment Strategies in Gaucher's and Parkinson's Disease.
Journal:Advanced science (Weinheim, Baden-Wurttemberg, Germany)
PubMed ID:38666485
Genetic variants of GBA1 can cause the lysosomal storage disorder Gaucher disease and are among the highest genetic risk factors for Parkinson's disease (PD). GBA1 encodes the lysosomal enzyme beta-glucocerebrosidase (GCase), which orchestrates the degradation of glucosylceramide (GluCer) in the lysosome. Recent studies have shown that GluCer accelerates α-synuclein aggregation,
Late-onset Krabbe disease presenting as spastic paraplegia - implications of GCase and CTSB/D.
Journal:Annals of clinical and translational neurology
PubMed ID:38837642
Krabbe disease (KD) is a multisystem neurodegenerative disorder with severe disability and premature death, mostly with an infancy/childhood onset. In rare cases of late-onset phenotypes, symptoms are often milder and difficult to diagnose. We here present a translational approach combining diagnostic and biochemical analyses of a male patient with a
Tau accumulation in degradative organelles is associated to lysosomal stress.
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
Dysregulation of mitochondria-lysosome contacts by GBA1 dysfunction in dopaminergic neuronal models of Parkinson's disease.
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
Development of screening strategies for the identification of paramylon-degrading enzymes.
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