Click-IT™ Tetramethylrhodamine (TAMRA) Protein Analysis Detection Kit
Citas y referencias (5)
Invitrogen™
Click-IT™ Tetramethylrhodamine (TAMRA) Protein Analysis Detection Kit
El kit de detección de glicoproteínas de tetrametilrodamina (TAMRA) Click-iT™ proporciona la segunda parte de la técnica simple y sólidaMás información
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Número de catálogo
Cantidad
C33370
1 Kit
Número de catálogo C33370
Precio (MXN)
-
Cantidad:
1 Kit
El kit de detección de glicoproteínas de tetrametilrodamina (TAMRA) Click-iT™ proporciona la segunda parte de la técnica simple y sólida de dos pasos para identificar y caracterizar las glicoproteínas mediante electroforesis en gel unidimensional o bidimensional. En el paso dos, después de la incorporación del asa 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. Los geles con glicoproteínas etiquetadas con TAMRA se pueden teñir posteriormente con las tecnologías Multiplexed Proteomics™, con tinción de proteína total SYPRO™ Ruby y tinción de glicoproteínas PRO-Q™ Emerald para el análisis diferencial de subclases de glicoproteínas, proteínas totales y glicoproteínas totales en el mismo gel. Las glicoproteínas modificadas con Click-iT™ también son compatibles con el análisis posterior de LC-MS/MS y MALDI MS para su identificación.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Método de detecciónFluorescente
Características ecológicasMenos peligroso
Diana de etiquetadoProteínas (glicoproteínas)
Etiqueta o tinteIsómeros TAMRA™, TMR (tetrametilrodamina)
Tipo de productoKit de detección de análisis de proteínas TAMRA
Cantidad1 Kit
Condiciones de envíoTemperatura ambiente
Línea de productosClick-iT
Unit SizeEach
Contenido y almacenamiento
Almacenar en congelador entre -5 °C y -30 °C
Preguntas frecuentes
I am using Click-iT AHA (L-azidohomoalanine) kit to label nascent proteins in live cells, then detecting with TAMRA alkyne after fixation and permeabilization and a click reaction. But I'm seeing nucleolar labeling in the cells. It this expected?
Yes. All proteins synthesized during the time the AHA is present will be detected, and they may be all over the cell. Our imaging shows strong labeling in the nucleoli and cytoplasm, as well as nuclear labeling.
Protein synthesis in distal axons is not required for growth cone responses to guidance cues.
Authors:Roche FK, Marsick BM, Letourneau PC,
Journal:J Neurosci
PubMed ID:19158291
'Recent evidence suggests that growth cone responses to guidance cues require local protein synthesis. Using chick neurons, we investigated whether protein synthesis is required for growth cones of several types to respond to guidance cues. First, we found that global inhibition of protein synthesis stops axonal elongation after 2 h. ... More
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
The cytoplasmic tail dileucine motif LL572 determines the glycosylation pattern of membrane-type 1 matrix metalloproteinase.
'Membrane-type 1 matrix metalloproteinase (MT1-MMP; MMP-14) drives fundamental physiological and pathological processes, due to its ability to process a broad spectrum of substrates. Because subtle changes in its activity can produce profound physiological effects, MT1-MMP is tightly regulated. Currently, many aspects of this regulation remain to be elucidated. It has ... More
A novel approach to tag and identify geranylgeranylated proteins.
Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.
Authors:Dias WB, Cheung WD, Wang Z, Hart GW,
Journal:J Biol Chem
PubMed ID:19506079
Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification. GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription. Here we show that calcium/calmodulin-dependent kinase IV (CaMKIV) is highly GlcNAcylated in vivo. ... More