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Citas y referencias (6)
Invitrogen™
RediPlate™ 96 EnzChek™ Tyrosine Phosphatase Assay Kit
El kit de ensayo de fosfatasa tirosina RediPlate 96 EnzChek es un ensayo de microplaca basado en fluorescencia listo paraMás información
| Número de catálogo | Cantidad |
|---|---|
| R22067 | 1 placa de 96 pocillos |
Número de catálogo R22067
Precio (MXN)
-
Cantidad:
1 placa de 96 pocillos
El kit de ensayo de fosfatasa tirosina RediPlate 96 EnzChek es un ensayo de microplaca basado en fluorescencia listo para usar para detectar tirosina fosfatasas (PTPase) y sus correspondientes moduladores e inhibidores. Cada microplaca de 96 pocillos RediPlate tiene carriles extraíbles, lo que permite a los investigadores realizar tantos ensayos como sea necesario para cada experimento o realizar análisis de alto rendimiento.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Método de detecciónIntensidad de la fluorescencia
Tipo de coloranteDiFMU
Cantidad1 placa de 96 pocillos
Condiciones de envíoTemperatura ambiente
SustratoDiFMUP
Propiedades de sustratoSustrato químico
Tipo de sustratoSustrato de fosfatasa
Enzima dianaTirosina fosfatasas
Emission358⁄452
Para utilizar con (aplicación)Ensayo de tirosina fosfatasa
Para utilizar con (equipo)Lector de microplacas
Línea de productosEnzChek, RediPlate
Tipo de productoEnsayo de fosfatasa
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador de -5 °C a -30 °C y proteger de la luz.
Citations & References (6)
Citations & References
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.