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Zitierungen und Referenzen (6)
Invitrogen™
RediPlate™ 96 EnzChek™ Tyrosine Phosphatase Assay Kit
Das RediPlate 96 EnzChek Tyrosin-Phosphatase-Assay-Kit ist ein gebrauchsfertiger, fluoreszenzbasierter Mikrotiterplatten-Assay zum Nachweis von Tyrosin-Phosphatasen (PTPase) und ihren entsprechenden Modulatoren undWeitere Informationen
| Katalognummer | Menge |
|---|---|
| R22067 | 1 x 96-Well-Platte |
Katalognummer R22067
Preis (EUR)
728,00
Each
Menge:
1 x 96-Well-Platte
Preis (EUR)
728,00
Each
Das RediPlate 96 EnzChek Tyrosin-Phosphatase-Assay-Kit ist ein gebrauchsfertiger, fluoreszenzbasierter Mikrotiterplatten-Assay zum Nachweis von Tyrosin-Phosphatasen (PTPase) und ihren entsprechenden Modulatoren und Inhibitoren. Jede RediPlate 96-Well Mikrotiterplatte verfügt über herausnehmbare Spuren, sodass Forscher nur so viele Assays, wie für jedes Experiment erforderlich sind, oder eine Hochdurchsatzanalyse durchführen können.
Nur für Forschungszwecke. Nicht zur Verwendung bei diagnostischen Verfahren.
Specifications
NachweisverfahrenFluoreszenzintensitätsmessung
FarbstofftypDiFMU
Menge1 x 96-Well-Platte
VersandbedingungRaumtemperatur
SubstratDiFMUP
SubstrateigenschaftenChemisches Substrat
SubstrattypPhosphatasesubstrat
ZielenzymTyrosinphosphatasen
Emission358⁄452
Zur Verwendung mit (Anwendung)Tyrosinphosphatase-Assay
Zur Verwendung mit (Geräte)Mikrotiterplatten-Lesegerät
ProduktlinieEnzChek, RediPlate
ProdukttypPhosphatase-Assay
Unit SizeEach
Inhalt und Lagerung
In einem Tiefkühlgerät (-5 bis -30 °C) lagern und vor Licht schützen.
Zitierungen und Referenzen (6)
Zitierungen und Referenzen
Abstract
Negative regulation of EGFR signalling through integrin-alpha1beta1-mediated activation of protein tyrosine phosphatase TCPTP.
Journal:Nat Cell Biol
PubMed ID:15592458
'Integrin-mediated cell adhesion regulates a multitude of cellular responses, including proliferation, survival and cross-talk between different cellular signalling pathways. So far, integrins have been mainly shown to convey permissive signals enabling anchorage-dependent receptor tyrosine kinase signalling. Here we show that a collagen-binding integrin alpha(1)beta(1) functions as a negative regulator of
Differential coupling of M1 muscarinic and alpha7 nicotinic receptors to inhibition of pemphigus acantholysis.
Journal:J Biol Chem
PubMed ID:18073210
'The mechanisms mediating and regulating assembly and disassembly of intercellular junctions is a subject of intensive research. The IgG autoantibodies produced in patients with the immunoblistering skin disease pemphigus vulgaris (PV) can induce keratinocyte (KC) dyshesion (acantholysis) via mechanisms that involve signaling kinases targeting intercellular adhesion molecules, thus providing a
Protein tyrosine phosphatase: enzymatic assays.
Journal:Methods
PubMed ID:15588980
Activity assays for tyrosine phosphatases are based on the hydrolysis of a arylphosphate moiety from a synthetic substrate yielding a spectroscopically active product. Many different substrates can be used for these assays with p-nitrophenyl phosphate (pNPP), fluorescein diphosphate (FDP), and 6,8-difluoro-4-methylumbellyferyl phosphate (DiFMUP) being the most efficient and versatile. Equally,
Chaperone release and unfolding of substrates in type III secretion.
Journal:Nature
PubMed ID:16208377
Type III protein secretion systems are essential virulence factors of many bacteria pathogenic to humans, animals and plants. These systems mediate the transfer of bacterial virulence proteins directly into the host cell cytoplasm. Proteins are thought to travel this pathway in a largely unfolded manner, and a family of customized
Development of fluorescence-based selective assays for serine/threonine and tyrosine phosphatases.
Journal:Comb Chem High Throughput Screen
PubMed ID:12769677
A number of aromatic substrates were evaluated for their ability to detect tyrosine phosphatase and serine/threonine phosphatase activity. Results demonstrated that the fluorinated coumarin DiFMUP is the most sensitive substrate for detecting LAR and PP-2A activity. Using this substrate, selective high-throughput screening assays for serine/threonine and tyrosine phosphatases were developed.