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Citas y referencias (19)
Invitrogen™
Multiplexed Proteomics™ Phosphoprotein Gel Stain Kits (with Pro-Q™ Diamond and SYPRO™ Ruby Gel Stains)
Nuestra nueva tinción de gel de fosfoproteína Pro-Q Diamond proporciona un método práctico para la tinción selectiva de fosfoproteínas en geles de acrilamida, sin necesidad de transferencia o anticuerpos específicos de fosfoproteína y análisis western blot.
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| Número de catálogo | Cantidad |
|---|---|
| M33305 | 1 l por colorante |
| M33306 | 200 ml por colorante |
Número de catálogo M33305
Precio (MXN)
-
Cantidad:
1 l por colorante
Nuestra nueva tinción de gel de fosfoproteína Pro-Q Diamond proporciona un método práctico para la tinción selectiva de fosfoproteínas en geles de acrilamida, sin necesidad de transferencia o anticuerpos específicos de fosfoproteína y análisis western blot. Este reactivo, cuando se combina con nuestra tinción de proteína total, la tinción de gel de proteínas SYPRO Ruby, se convierte en una potente combinación para el análisis cuantitativo de proteoma.
Our new Pro-Q Diamond Phosphoprotein Gel Stain provides a convenient method for selectively staining phosphoproteins in acrylamide gels, without the need for blotting or phosphoprotein-specific antibodies and western blot analysis. This reagent, when combined with our total protein stain, SYPRO Ruby Protein Gel Stain, becomes a powerful combination for quantitative proteome analysis. This convenient Pro-Q Diamond Phosphoprotein Gel Stain and SYPRO Ruby Protein Gel Stain Pack provides each stain in 1-liter amounts (Cat. No. M-33305) or in 200-mL amounts (Cat. No. M-33306).
Features include:
• Sensitive—Pro-Q Diamond Phosphoprotein Gel Stain offers detection level down to 1–16 ng of phosphoprotein per band
• Convenient—selectively stain phosphoproteins in acrylamide gels, without the need for blotting or phosphoprotein-specific antibodies and western blot analysis. SYPRO Ruby Gel Stain is subsequently used for total protein staining and simplifies the determination of phosphorylation level
• Linear signal—quantify with ease as Pro-Q Diamond Phosphoprotein Gel Stain and SYPRO Ruby Gel Stain exhibit excellent linearity over three orders of magnitude, ideal for quantitation
Features include:
• Sensitive—Pro-Q Diamond Phosphoprotein Gel Stain offers detection level down to 1–16 ng of phosphoprotein per band
• Convenient—selectively stain phosphoproteins in acrylamide gels, without the need for blotting or phosphoprotein-specific antibodies and western blot analysis. SYPRO Ruby Gel Stain is subsequently used for total protein staining and simplifies the determination of phosphorylation level
• Linear signal—quantify with ease as Pro-Q Diamond Phosphoprotein Gel Stain and SYPRO Ruby Gel Stain exhibit excellent linearity over three orders of magnitude, ideal for quantitation
For Research Use Only. Not for use in diagnostic procedures.
Especificaciones
DescripciónKit de tinción de gel de fosfoproteína n.º 1 Multiplexed Proteomics™
Ubicación de detecciónDetección en gel
Método de detecciónFluorescencia
Línea de productosPRO-Q, SYPRO
Tipo de productoKit de tinción para geles de fosfoproteínas
Cantidad1 l por colorante
Condiciones de envíoTemperatura ambiente
Molécula dianaProteínas (fosfoproteínas)
Etiqueta o tinteSYPRO Ruby, Pro-Q Diamond
Unit SizeEach
Contenido y almacenamiento
• Tinción de gel de fosfoproteína Pro-Q Diamond, 1 l
• Tinción de gel de proteína SYPRO Ruby, 1 l
Almacenar a temperatura ambiente y protegido de la luz.
• Tinción de gel de proteína SYPRO Ruby, 1 l
Almacenar a temperatura ambiente y protegido de la luz.
Citations & References (19)
Citations & References
Abstract
Initial analysis of the phosphoproteome of Chinese hamster ovary cells using electrophoresis.
Journal:J Biomol Tech
PubMed ID:15585821
'Protein phosphorylation is a common post-translational modification of enormous biological importance. Analysis of phosphorylation at the global level should shed light on the use of this modification to regulate metabolism, signal transduction, and other processes. We have begun a proteomic analysis of phosphorylation using two-dimensional gel electrophoresis. Chinese hamster ovary
Comparative proteomes of the proliferating C(2)C(12) myoblasts and fully differentiated myotubes reveal the complexity of the skeletal muscle differentiation program.
Journal:Mol Cell Proteomics
PubMed ID:15286212
'When cultured in low serum-containing growth medium, the mouse C(2)C(12) cells exit cell cycle and undergo a well-defined program of differentiation that culminates in the formation of myosin heavy chain-positive bona fide multinucleated muscle cells. To gain an understanding into this process, we compared total, membrane- and nuclear-enriched proteins, and
Characterization of dynamic and steady-state protein phosphorylation using a fluorescent phosphoprotein gel stain and mass spectrometry.
Journal:Electrophoresis
PubMed ID:15300772
'Protein phosphorylation plays a vital role in the regulation of most aspects of cellular activity, being key to propagating messages within signal transduction pathways and to modulating protein function. Pro-Q Diamond phosphoprotein gel stain is suitable for the fluorescence detection of phosphoserine-, phosphothreonine-, and phosphotyrosine-containing proteins directly in sodium dodecyl
Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics.
Journal:Nat Cell Biol
PubMed ID:15580268
Cofilin is a key regulator of actin cytoskeletal dynamics whose activity is controlled by phosphorylation of a single serine residue. We report the biochemical isolation of chronophin (CIN), a unique cofilin-activating phosphatase of the haloacid dehalogenase (HAD) superfamily. CIN directly dephosphorylates cofilin with high specificity and colocalizes with cofilin in
Determination of in vivo protein phosphorylation in photosynthetic membranes.
Journal:Methods Mol Biol
PubMed ID:19083170
Light- and redox-controlled reversible phosphorylation of thylakoid proteins regulates short- and long-term acclimation of plants to environmental cues. The major phosphoproteins in thylakoids belong to photosystem II and its light-harvesting antenna but phosphorylation of subunits of other thylakoid protein complexes has been detected as well. The detection methods include electrophoretic