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Citas y referencias (7)
Invitrogen™
Click-IT™ O-GlcNAc Enzymatic Labeling System
El sistema de etiquetado enzimático de O-GlcNAc Click-iT™ proporciona un método altamente sensible y eficaz para la modificación in vitroMás información
| Número de catálogo | Cantidad |
|---|---|
| C33368 | 1 Kit |
Número de catálogo C33368
Precio (MXN)
-
Cantidad:
1 Kit
El sistema de etiquetado enzimático de O-GlcNAc Click-iT™ proporciona un método altamente sensible y eficaz para la modificación in vitro de proteínas modificadas de O-GlcNAc. Las proteínas se etiquetan enzimáticamente mediante el mutante permisivo β-1,4-galactosiltransferasa (Gal-T1 (Y289L)), que transfiere galactosa modificada con azido (GalNAz) de UDP-GalNAz a residuos de O-GlcNAc. Después, a través de la ligadura quimioselectiva o la reacción de clic entre una azida y un alquino, las glicoproteínas etiquetadas con azido se pueden detectar con un kit de detección de glicoproteínas Click-iT™ para geles (alquino TAMRA o Dapoxyl™) o Western blots (alquino biotina). El etiquetado y la detección se pueden completar en menos de 24 horas, y los productos de glicoproteína Click-iT™ son compatibles con LC-MS/MS y tecnologías Multiplexed Proteomics™ para realizar análisis exhaustivos de esta importante modificación postranslacional.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Método de detecciónCon base de biotina, fluorescente
Línea de productosClick-iT
Tipo de productoSistema de etiquetado enzimático O-GlcNAc
Cantidad1 Kit
Condiciones de envíoHielo húmedo
Labeling TargetProteínas
Etiqueta o tinteAlexa Fluor 488, Alexa Fluor 555, Alexa Fluor 594, Alexa Fluor 647, biotina, Oregon Green 488, TMR (tetrametilrodamina)
Unit SizeEach
Contenido y almacenamiento
Almacenar en refrigerador a entre 2 °C y 8 °C
Citations & References (7)
Citations & References
Abstract
Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation.
Journal:Mol Cell Proteomics
PubMed ID:17507370
'O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli. O-GlcNAcylation is remarkably similar to O-phosphorylation and appears to have a dynamic interplay with O-phosphate in cellular regulation. A systematic glycoproteomics analysis of the affects of inhibiting
Novel in vivo-degradable cellulose-chitin copolymer from metabolically engineered Gluconacetobacter xylinus.
Journal:Appl Environ Microbiol
PubMed ID:20656868
'Despite excellent biocompatibility and mechanical properties, the poor in vitro and in vivo degradability of cellulose has limited its biomedical and biomass conversion applications. To address this issue, we report a metabolic engineering-based approach to the rational redesign of cellular metabolites to introduce N-acetylglucosamine (GlcNAc) residues into cellulosic biopolymers during
Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins.
Journal:J Am Chem Soc
PubMed ID:18683930
'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.
The chemical neurobiology of carbohydrates.
Journal:Chem Rev
PubMed ID:18452339
The problems associated with oligosaccharide analysis have hindered efforts to understand the biology of oligosaccharides yet have given chemists a unique opportunity to develop new methods to overcome these challenges. The development of chemical tools for the analysis of glycan structure and function is essential to advance our understanding of
O-linked N-acetylglucosamine modification on CCAAT enhancer-binding protein beta: role during adipocyte differentiation.
Journal:J Biol Chem
PubMed ID:19478079
CCAAT enhancer-binding protein (C/EBP)beta is a basic leucine zipper transcription factor family member, and can be phosphorylated, acetylated, and sumoylated. C/EBPbeta undergoes sequential phosphorylation during 3T3-L1 adipocyte differentiation. Phosphorylation on Thr(188) by MAPK or cyclin A/cdk2 primes the phosphorylations on Ser(184)/Thr(179) by GSK3beta, and these phosphorylations are required for the