Tampón de muestra de Tris-glicina SDS Novex™ (2X)
Tampón de muestra de Tris-glicina SDS Novex™ (2X)
Tampón de muestra de Tris-glicina SDS Novex™ (2X)
Tampón de muestra de Tris-glicina SDS Novex™ (2X)
Citas y referencias (1)
Invitrogen™

Tampón de muestra de Tris-glicina SDS Novex™ (2X)

El tampón de muestra de SDS de Tris-glicina Novex (2X) se utiliza para preparar muestras de proteínas para la desnaturalizaciónMás información
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Número de catálogoCantidad
LC267620 mL
Número de catálogo LC2676
Precio (MXN)
-
Cantidad:
20 mL
El tampón de muestra de SDS de Tris-glicina Novex (2X) se utiliza para preparar muestras de proteínas para la desnaturalización de la electroforesis en gel con geles de Tris-glicina. Tiene un pH de 6,8 y contiene azul de bromofenol como colorante de seguimiento.

Consulte todos los tampones y reactivos disponibles para SDS-PAGE

Para su uso: Caliente la muestra en una dilución 1X (reducida o no reducida) a 85 °C durante 2–5 minutos para obtener resultados óptimos. El calentamiento de las muestras a 100 °C en tampones que contienen SDS provoca la proteólisis.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Nombre del producto químico o materialTampón de carga de muestras
Almacenamiento recomendadoTampón de muestra de Tris-glicina (2X) que contiene dodecilsulfato sódico (SDS) a pH 6,8 con azul de bromofenol.

Almacenar entre 2 °C y 8 °C.

Concentración2 X
Forma físicaLíquido
Línea de productosNovex
Cantidad20 mL
Unit SizeEach

Preguntas frecuentes

Where do I find buffer recipes for your precast protein gels?

The formulations of buffers for our precast protein gels can be found at this link: https://www.thermofisher.com/us/en/home/life-science/protein-biology/protein-gel-electrophoresis/protein-electrophoresis-buffers-reagents.html

Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.

What is the recipe for traditional Laemmli Buffer?

The Laemmli buffer or 2X SDS Buffer is composed of the following: 100 mM Tris HCl , pH 6.8, 200 mM dithiothreitol, 4% SDS, 0.2% bromophenol blue, 20% glycerol. 2X SDS gel loading buffer lacking dithiothreitol can be stored at room temperature. Dithiothreitol should then be added, just before use.

Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.

If a Tricine gel is accidentally run with buffers used in the Tris-Glycine system, what will happen and why?

If the Tricine gel is run with Tris-Glycine sample buffer, the bands will behave abnormally and resolve poorly. If the Tricine gel is accidentally run with Tris-Glycine running buffer, the gel will take longer to run and the resolution, especially for smaller proteins, will be worse than when the proteins are run on a Tris-Glycine gel with Tris-Glycine buffers. This is due to a combination of increase in stack area size (glycine is a slower ion than Tricine) and the higher ionic strength of the Tricine gel.

Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.

Why is LDS (lithium dodecyl sulfate) used in the 4X NuPAGE sample buffer instead of SDS?

SDS in a 4X sample buffer concentrate tends to precipitate from solution and to make the solution viscous and difficult to pipette. The LDS is much more soluble.

Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.

Can I use CTAB rather than SDS in my sample buffer?

No, CTAB will not work with any of our gels except for the NuPAGE Tris-Acetate gels. To use CTAB, you would need to use a running buffer of 50 mM acetic acid and 50 mM beta-alanine in equal concentrations. You would also need to switch the electrodes. Since CTAB is a cationic detergent, this would establish conditions for running a basic protein towards the anode (into the gel).

Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.

Citations & References (1)

Citations & References
Abstract
Identification of components of protein complexes using a fluorescent photo-cross-linker and mass spectrometry.
Authors: Wine Robert N; Dial John M; Tomer Kenneth B; Borchers Christoph H;
Journal:Anal Chem
PubMed ID:12033289
'This study describes a novel method for improving the specific recognition, detection, and identification of proteins involved in multiprotein complexes. The method is based on a combination of coimmunoprecipitation, chemical cross-linking, and specific fluorescent tagging of protein components in close association with one another. Specific fluorescent tagging of the protein ... More