El kit de detección de glicoproteínas de biotina Click-iT™ proporciona la segunda parte de una técnica simple y sólida paraMás información
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Número de catálogo
Cantidad
C33372
1 kit
Número de catálogo C33372
Precio (EUR)
371,00
Each
Añadir al carro de la compra
Cantidad:
1 kit
Precio (EUR)
371,00
Each
Añadir al carro de la compra
El kit de detección de glicoproteínas de biotina Click-iT™ proporciona la segunda parte de una técnica simple y sólida para identificar y caracterizar las glicoproteínas mediante Western blot. En el paso dos, después de la incorporación de una porción de azida en estructuras de glucano de proteína con un reactivo de etiquetado metabólico Click-iT™ o el sistema de etiquetado enzimático Click-iT™, las glicoproteínas modificadas con azida se detectan mediante la ligadura quimioselectiva o la reacción de clic entre una azida y un alquino. Con esta técnica, la sensibilidad de detección está en el intervalo bajo de femptomoles, y las muestras marcadas con biotina pueden detectarse antes o después de sondear el Western con un anticuerpo primario.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Método de detecciónCon base de biotina, fluorescente
Características ecológicasMenos peligroso
Línea de productosClick-iT
Tipo de productoKit de detección de análisis de proteínas con biotina
Cantidad1 kit
Condiciones de envíoTemperatura ambiente
Labeling TargetProteínas
Etiqueta o tinteBiotina
Unit SizeEach
Contenido y almacenamiento
Almacenar en congelador entre -5 °C y -30 °C
Citations & References (6)
Citations & References
Abstract
Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins.
'We report an advanced chemoenzymatic labeling strategy for direct fluorescence detection of O-GlcNAc proteins in gels that facilitates proteomic studies and greatly extend the reach of existing technologies. These new tools also enable the expression and dynamics of O-GlcNAc modifications to be monitored by imaging in cells and tissues. ... More
Comparative methods for analysis of protein covalent modification by electrophilic quinoids formed from xenobiotics.
'Conjugation of biotin and fluorophore tags is useful for assaying covalent protein modification. Oxidative bioactivation of selective estrogen receptor modulators (SERMs) yields reactive quinoid electrophiles that covalently modify proteins, and bioactivation is associated with carcinogenic and chemopreventive effects. Identification of the protein targets of electrophilic metabolites is of general importance ... More
Rapid temporal dynamics of transcription, protein synthesis, and secretion during macrophage activation.
Authors:Eichelbaum K, Krijgsveld J,
Journal:
PubMed ID:24396086
Macrophages provide the first line of host defense with their capacity to react to an array of cytokines and bacterial components requiring tight regulation of protein expression and secretion to invoke a properly tuned innate immune response. To capture the dynamics of this system, we introduce a novel method combining ... More
A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly.
Authors:Ohn T, Kedersha N, Hickman T, Tisdale S, Anderson P,
Journal:Nat Cell Biol
PubMed ID:18794846
Stress granules (SGs) and processing bodies (PBs) are microscopically visible ribonucleoprotein granules that cooperatively regulate the translation and decay of messenger RNA. Using an RNA-mediated interference-based screen, we identify 101 human genes required for SG assembly, 39 genes required for PB assembly, and 31 genes required for coordinate SG and ... More
Identification of structural and functional O-linked N-acetylglucosamine-bearing proteins in Xenopus laevis oocyte.
O-Linked N-acetylglucosaminylation (O-GlcNAcylation) (or O-linked N-acetylglucosamine (O-GlcNAc)) is an abundant and reversible glycosylation type found within the cytosolic and the nuclear compartments. We have described previously the sudden O-GlcNAcylation increase occurring during the Xenopus laevis oocyte G(2)/M transition, and we have demonstrated that the inhibition of O-GlcNAc-transferase (OGT) blocked this ... More