Minigeles de proteínas NuPAGE™, Bis-Tris del 4 al 12 %, 1,0–1,5 mm
Minigeles de proteínas NuPAGE™, Bis-Tris del 4 al 12 %, 1,0–1,5 mm
Citas y referencias (4)
Invitrogen™

Minigeles de proteínas NuPAGE™, Bis-Tris del 4 al 12 %, 1,0–1,5 mm

Los geles de proteína Invitrogen NuPAGE Bis-Tris son geles de poliacrilamida prefundidos y diseñados para una separación óptima de unaMás información
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Número de catálogoPocillosGel ThicknessCantidad
NP0330BOXPocillo IPG1,0 mm10 geles/caja
NP0321BOX10 pocillo1,0 mm10 geles/caja
NP0321PK210 pocillo1,0 mm2 geles/caja
NP0322BOX12 pocillo1,0 mm10 geles/caja
NP0322PK212 pocillo1,0 mm2 geles/caja
NP0323BOX15 pocillo1,0 mm10 geles/caja
NP0323PK215 pocillo1,0 mm2 geles/caja
NP0324BOX1 pocillo1,0 mm10 geles/caja
NP0326BOXPocillo 2D1,0 mm10 geles/caja
NP0327BOX9 pocillo1,0 mm10 geles/caja
NP0329BOX17 pocillo1,0 mm10 geles/caja
NP0329PK217 pocillo1,0 mm2 geles/caja
NP0335BOX10 pocillo1,5 mm10 geles/caja
NP0335PK210 pocillo1,5 mm2 geles/caja
NP0336BOX15 pocillo1,5 mm10 geles/caja
NP0336PK215 pocillo1,5 mm2 geles/caja
Número de catálogo NP0330BOX
Precio (MXN)
-
Pocillos:
Pocillo IPG
Gel Thickness:
1,0 mm
Cantidad:
10 geles/caja
Los geles de proteína Invitrogen NuPAGE Bis-Tris son geles de poliacrilamida prefundidos y diseñados para una separación óptima de una amplia gama de proteínas en condiciones desnaturalizantes. A diferencia de los geles tradicionales de Tris-glicina, los geles NuPAGE Bis-Tris tienen un ambiente de pH neutro que minimiza las modificaciones de proteínas. Utilice los geles NuPAGE Bis-Tris para preparar las proteínas para la secuenciación, la espectrometría de masas y cualquier otra técnica donde la integridad de las proteínas resulte crucial. Además, utilice los geles NuPAGE para obtener resultados óptimos durante el día a día.

Características de los geles de Bis-Tris NuPAGE:
• Mejor integridad de las proteínas: proceso de preparación de muestras optimizado que conserva sus proteínas.
• Amplios intervalos de separación de peso molecular: seleccione el gel y el tampón de desplazamiento adecuados para obtener la separación óptima de sus proteínas.
•Tiempos de ejecución más rápidos: obtenga la separación de sus proteínas en tan solo 35 minutos.
• Vida útil más larga: los geles NuPAGE Bis-Tris se pueden almacenar durante al menos 12 meses a temperatura ambiente

Obtenga más información sobre todos nuestros geles NuPAGE Bis-Tris >
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Elija el gel NuPAGE Bis-Tris adecuado para su separación de proteínas
Obtenga una separación óptima de sus proteínas eligiendo la combinación correcta de gel y tampón de desplazamiento. Los geles NuPAGE Bis-Tris se suministran en cuatro concentraciones de poliacrilamida: 8 %, 10 %, 12 % y 4-12 % de gradiente. Los geles se suministran en dos tamaños: mini (8 cm x 8 cm) o medio (8,7 cm x 13,3 cm), y 1,0 mm (geles mini y medio) o 1,5 mm (solo formato minigel) de grosor. Los geles NuPAGE Bis-Tris también vienen en múltiples formatos de pocillo.

Los geles NuPAGE Bis-Tris están formulados para desnaturalización de aplicaciones de electroforesis en gel. Para una preparación de muestras óptima, utilice el tampón de muestras NuPAGE LDS y el agente de reducción de muestras NuPAGE. Utilice el antioxidante NuPAGE en el tampón de desplazamiento para mantener el estado reducido de las proteínas durante la ejecución y permitir la máxima nitidez de la banda. Los geles se pueden procesar utilizando el tampón de desplazamiento NuPAGE MES SDS para resolver mejor las proteínas pequeñas o el tampón de desplazamiento NuPAGE MOPS SDS para resolver las proteínas de tamaño medio a grande.

También proporcionamos geles de Tris-acetato NuPAGE para separar las proteínas más grandes. Para la electroforesis clásica de Tris-glicina basada en Laemmli, proporcionamos geles de Tris-glicina Novex.

Para la transferencia de proteínas a una membrana, le recomendamos utilizar el tampón de desplazamiento NuPAGE. La transferencia semiseca rápida se puede realizar con el Pierce Power Blotter o la transferencia en seco rápida con el dispositivo de transferencia de gel iBlot 2. Como alternativa, la transferencia húmeda tradicional se puede realizar utilizando el módulo blot XCell II o el módulo Mini Blot.

Enlaces relacionados
Descripción general de la electroforesis de proteínas 1D
Comparación de los geles de Tris-Bis NuPAGE frente a los geles de Tris-glicina tradicionales
For Research Use Only. Not for use in diagnostic procedures.
Especificaciones
Gel Thickness1,0 mm
Longitud (métrico)8 cm
Modo de separaciónPeso molecular
Línea de productosNuPAGE, ZOOM
Cantidad10 geles/caja
Volumen de carga de muestrasTiras de 7 cm
Duración de almacenamiento12 meses
Condiciones de envíoTemperatura ambiente
Requisitos de almacenamientoAlmacenar de 4–25 °C. No la congele.
Anchura (métrico)8 cm
Para utilizar con (equipo)Depósito de minigel, Minicelda XCell SureLock
Porcentaje del gelDel 4 al 12%
Tamaño de gelMini
Tipo de gelBis-Tris
Intervalo de separaciónDe 3,5 a 260 kDa
Tipo de separaciónDesnaturalización
PocillosPocillo IPG
Unit SizeEach
Contenido y almacenamiento
Una caja contiene 10 geles. Almacenar entre 4–25° C. No congelar. La vida útil es de 12 meses.

Preguntas frecuentes

Can I prepare my protein sample with the reducing agent and store it for future use?

DTT is not stable, so it must be added and the reduction performed just prior to loading your samples.

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

My LDS or SDS sample buffer precipitates when stored at 4 degrees C. Can I warm it up? Can I store it at room temperature?

Precipitation of the LDS or SDS at 4 degrees C is normal. Bring the buffer to room temperature and mix until the LDS/SDS goes into solution. If you do not want to wait for it to dissolve, you can store the sample buffer at room temperature.

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

How are Bolt gels different than NuPAGE gels?

While they are both Bis-Tris based gels, the chemistries are very different since Bolt gels are optimized for western blotting. Another key difference is the wedge well design of the Bolt gels, which allows larger sample volumes to be loaded.

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

What is the advantage of NuPAGE Gels over regular Tris-Glycine gels?

The neutral operating pH of the NuPAGE Gels and buffers provides following advantages over the Laemmli system:
-Longer shelf life of 8-12 months due to improved gel stability
-Improved protein stability during electrophoresis at neutral pH resulting in sharper band resolution and accurate results (Moos et al, 1998)
-Complete reduction of disulfides under mild heating conditions (70 degrees C for 10 min) and absence of cleavage of asp-pro bonds using the NuPAGE LDS Sample buffer (pH > 7.0 at 70 degrees C)
-Reduced state of the proteins maintained during electrophoresis and blotting of the proteins by the NuPAGE Antioxidant
Please refer to the following paper: Moos M Jr, Nguyen NY, Liu TY (1988) Reproducible High Yield Sequencing of Proteins Electrophoretically Separated and Transferred to an Inert Support. J Biol Chem 263:6005-6008.

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

What may cause streaking on the 2nd dimension gel after IEF?

There are several reasons why streaking may occur.

(1) Sample is not completely solubilized prior to application.

(2) Sample is poorly soluble in rehydration solution.

(3) Non-protein impurities in the sample can interfere with IEF, causing horizontal streaking in the final 2-D result, particularly toward the acidic side of the gel.

(4) Ionic impurities are present in sample.

(5) Ionic detergent is present in sample.

(6) Sample load is too high.

(7) Underfocusing. Focusing time was not long enough to achieve steady state focusing.

(8) Overfocusing. Extended focusing times (over 100,000 Vh) may result in electroendosmotic water and protein movement, which can produce horizontal smearing.

What should be done?

(1) Be sure that the sample is completely and stably solubilized. Note: Repeated precipitation-resolubilization cycles produce or increase horizontal streaking.

(2) Increase the concentration of the solubilizing components in the rehydration solution.

(3) Modify sample preparation to limit these contaminants or dialyze protein.

(4) Reduce salt concentration to below 10 mM by dilution or desalt the sample by dialysis. Precipitation with TCA and acetone and subsequent resuspension is another effective desalting technique that removes lipids, nucleotides and other small molecules.
Note: Specific and non-specific losses of proteins can occur with dialysis, gel chromatography, and precipitation/resuspension of samples. If the sample preparation cannot be modified, the effect of ionic impurities can be reduced by modifying the IEF protocol. Limit the voltage to 100-150 V for 2 hours, then resume a normal voltage step program. This pre-step allows the ions in the sample to move to the ends of the IPG strip.

(5) If the ionic detergent SDS is used in sample preparation, the final concentration must not exceed 0.25% after dilution into the rehydration solution. Additionally, the concentration of the non-ionic detergent present must be at least 8 times higher than the concentration of any ionic detergent to ensure complete removal of SDS from the proteins.

(6) Extend focusing time. Load less sample.

(7) Prolong focusing time.

(8) Reduce focusing time.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

View all Minigeles de proteínas NuPAGE™, Bis-Tris del 4 al 12 %, 1,0–1,5 mm FAQs

Citations & References (4)

Citations & References
Abstract
Sero-epidemiology as a tool to screen populations for exposure to Mycobacterium ulcerans.
Authors:Yeboah-Manu D, Röltgen K, Opare W, Asan-Ampah K, Quenin-Fosu K, Asante-Poku A, Ampadu E, Fyfe J, Koram K, Ahorlu C, Pluschke G,
Journal:PLoS Negl Trop Dis
PubMed ID:22253937
'Previous analyses of sera from a limited number of Ghanaian Buruli ulcer (BU) patients, their household contacts, individuals living in BU non-endemic regions as well as European controls have indicated that antibody responses to the M. ulcerans 18 kDa small heat shock protein (shsp) reflect exposure to this pathogen. Here, ... More
Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease.
Authors:Zheng L, Nukuna B, Brennan ML, Sun M, Goormastic M, Settle M, Schmitt D, Fu X, Thomson L, Fox PL, Ischiropoulos H, Smith JD, Kinter M, Hazen SL,
Journal:J Clin Invest
PubMed ID:15314690
In recent studies we demonstrated that systemic levels of protein-bound nitrotyrosine (NO(2)Tyr) and myeloperoxidase (MPO), a protein that catalyzes generation of nitrating oxidants, serve as independent predictors of atherosclerotic risk, burden, and incident cardiac events. We now show both that apolipoprotein A-I (apoA-I), the primary protein constituent of HDL, is ... More
Akt-mediated valosin-containing protein 97 phosphorylation regulates its association with ubiquitinated proteins.
Authors:Klein JB, Barati MT, Wu R, Gozal D, Sachleben LR, Kausar H, Trent JO, Gozal E, Rane MJ,
Journal:J Biol Chem
PubMed ID:16027165
Hypoxia is a common environmental stress that influences signaling pathways and cell function. Previous studies from our laboratory have identified significant differences in cellular responses to sustained or intermittent hypoxia with the latter proving more cytotoxic. We hypothesized that differences in susceptibility of neurons to intermittent (IH) and sustained hypoxia ... More
Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1.
Authors:Asai R, Kato A, Kato K, Kanamori-Koyama M, Sugimoto K, Sairenji T, Nishiyama Y, Kawaguchi Y,
Journal:J Virol
PubMed ID:16698993
Epstein-Barr virus (EBV) BGLF4 is a viral protein kinase that is expressed in the lytic phase of infection and is packaged in virions. We report here that BGLF4 is a tegument protein that dissociates from the virion in a phosphorylation-dependent process. We also present evidence that BGLF4 interacts with and ... More