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Citas y referencias (10)
Invitrogen™
Tinción para blot de proteínas SYPRO™ Ruby
La tinción de transferencia de proteínas SYPRO Ruby es una tinción fluorescente muy sensible y lista para su uso paraMás información
| Número de catálogo | Cantidad |
|---|---|
| S11791 | 200 mL |
Número de catálogo S11791
Precio (CLP)
324.163
Each
Cantidad:
200 mL
Precio (CLP)
324.163
Each
La tinción de transferencia de proteínas SYPRO Ruby es una tinción fluorescente muy sensible y lista para su uso para proteínas en membranas de nitrocelulosa o PVDF, lo que facilita la evaluación de la eficacia de la transferencia de proteínas a la blot y la determinación de si las vías se cargan por igual. Es compatible con inmunotinción (Western blotting), microsecuenciación y espectrometría de masas. Las proteínas teñidas se pueden visualizar con un transiluminador de azul LED o UV, o con un equipo de adquisición de imágenes que contenga los filtros o láseres adecuados.
Compare todas las tinciones fluorescentes ›
Compare todas las tinciones fluorescentes ›
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Ubicación de detecciónDetección en transferencia
Método de detecciónFluorescente
Línea de productosSYPRO
Tipo de productoTinción de transferencia de proteínas
Cantidad200 mL
Condiciones de envíoTemperatura ambiente
Molécula dianaproteína
Etiqueta o tinteSYPRO Ruby
Unit SizeEach
Contenido y almacenamiento
Almacenar a temperatura ambiente y proteger de la luz.
Preguntas frecuentes
I have stained my blot with Pro-Q Diamond Phosphoprotein Blot Stain. Can I also stain the blot with SYPRO Ruby Blot Stain for total protein detection?
Citations & References (10)
Citations & References
Abstract
Laser capture microdissection and protein microarray analysis of human non-small cell lung cancer: differential epidermal growth factor receptor (EGPR) phosphorylation events associated with mutated EGFR compared with wild type.
Journal:Mol Cell Proteomics
PubMed ID:18687633
'Little is known about lung carcinoma epidermal growth factor (EGF) kinase pathway signaling within the context of the tissue microenvironment. We quantitatively profiled the phosphorylation and abundance of signal pathway proteins relevant to the EGF receptor within laser capture microdissected untreated, human non-small cell lung cancer (NSCLC) (n = 25)
Novel observations of Thiobacterium, a sulfur-storing Gammaproteobacterium producing gelatinous mats.
Journal:ISME J
PubMed ID:20220790
The genus Thiobacterium includes uncultivated rod-shaped microbes containing several spherical grains of elemental sulfur and forming conspicuous gelatinous mats. Owing to the fragility of mats and cells, their 16S ribosomal RNA genes have not been phylogenetically classified. This study examined the occurrence of Thiobacterium mats in three different sulfidic marine
Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress.
Journal:J Biol Chem
PubMed ID:10922362
Hyperhomocysteinemia, a risk factor for vascular disease, injures endothelial cells through undefined mechanisms. We previously identified several homocysteine-responsive genes in cultured human vascular endothelial cells, including the endoplasmic reticulum (ER)-resident molecular chaperone GRP78/BiP. Here, we demonstrate that homocysteine induces the ER stress response and leads to the expression of a
TrkB has a cell-autonomous role in the establishment of hippocampal Schaffer collateral synapses.
Journal:J Neurosci
PubMed ID:15829629
Neurotrophin signaling has been implicated in the processes of synapse formation and plasticity. To gain additional insight into the mechanism of BDNF and TrkB influence on synapse formation and synaptic plasticity, we generated a conditional knock-out for TrkB using the cre/loxp system. Using three different cre-expressing transgenic mice, three unique
A thousand points of light: the application of fluorescence detection technologies to two-dimensional gel electrophoresis and proteomics.
Journal:Electrophoresis
PubMed ID:10786886
As proteomics evolves into a high-throughput technology for the study of global protein regulation, new demands are continually being placed upon protein visualization and quantitation methods. Chief among these are increased detection sensitivity, broad linear dynamic range and compatibility with modern methods of microchemical analyses. The limitations of conventional protein