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NuPAGE™ 4 bis 12 %, Bis-Tris, 1,0–1,5 mm, Mini-Protein-Gele
Run Invitrogen Mini Protein Gels in Bio-Rad's Mini-PROTEAN® Tetra Cell. Click here for more information.
NuPAGE™ 4 bis 12 %, Bis-Tris, 1,0–1,5 mm, Mini-Protein-Gele
Zitierungen und Referenzen (4)
Invitrogen™

NuPAGE™ 4 bis 12 %, Bis-Tris, 1,0–1,5 mm, Mini-Protein-Gele

Invitrogen NuPAGE Bis-Tris Proteingele sind vorgegossene Polyacrylamid-Gele, die zur optimalen Trennung eines großen Bereichs von Proteinen unter denaturierenden Bedingungen entwickeltWeitere Informationen
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KatalognummerWellsGel ThicknessMenge
NP0330BOXIPG-Well1,0 mm10 Gele/Karton
NP0321BOX10-Well1,0 mm10 Gele/Karton
NP0321PK210-Well1,0 mm2 Gele/Karton
NP0322BOX12-Well1,0 mm10 Gele/Karton
NP0322PK212-Well1,0 mm2 Gele/Karton
NP0323BOX15-Well1,0 mm10 Gele/Karton
NP0323PK215-Well1,0 mm2 Gele/Karton
NP0324BOX1-Well1,0 mm10 Gele/Karton
NP0326BOX2D-Well1,0 mm10 Gele/Karton
NP0327BOX9-Well1,0 mm10 Gele/Karton
NP0329BOX17-Well1,0 mm10 Gele/Karton
NP0329PK217-Well1,0 mm2 Gele/Karton
NP0335BOX10-Well1,5 mm10 Gele/Karton
NP0335PK210-Well1,5 mm2 Gele/Karton
NP0336BOX15-Well1,5 mm10 Gele/Karton
NP0336PK215-Well1,5 mm2 Gele/Karton
Katalognummer NP0330BOX
Preis (EUR)
183,65
Exklusiv online
227,00
Ersparnis 43,35 (19%)
Each
Zum Warenkorb hinzufügen
Wells:
IPG-Well
Gel Thickness:
1,0 mm
Menge:
10 Gele/Karton
Preis (EUR)
183,65
Exklusiv online
227,00
Ersparnis 43,35 (19%)
Each
Zum Warenkorb hinzufügen
Invitrogen NuPAGE Bis-Tris Proteingele sind vorgegossene Polyacrylamid-Gele, die zur optimalen Trennung eines großen Bereichs von Proteinen unter denaturierenden Bedingungen entwickelt wurden. Im Gegensatz zu herkömmlichen Tris-Glycin-Gelen bieten NuPAGE Bis-Tris-Gele eine Umgebung mit neutralem pH-Wert, was Proteinmodifikationen minimiert. Verwenden Sie NuPAGE Bis-Tris-Gele für Proteinvorbereitungen bei Sequenzierungen, für die Massenspektrometrie und alle anderen Methoden, bei denen es auf Proteinintegrität ankommt. NuPAGE Gele eignen sich zur Erzielung optimaler Ergebnisse bei routinemäßiger Anwendung.

Merkmale der NuPAGE Bis-Tris-Gele:
• Bessere Protein-Integrität: optimierter Probenvorbereitungsprozess bewahrt Ihre Proteine
• Trennung breiter Bereiche von Molekülmassen: Wählen Sie das richtige Gel und den richtigen Laufpuffer für eine optimale Trennung der Proteine
• Kürzere Laufzeiten: Erhalten Sie Trennungen Ihrer Proteine in nur 35 Minuten
• Längere Haltbarkeit: NuPAGE Bis-Tris-Gele können bei Raumtemperatur mindestens 12 Monate lang gelagert werden

Erfahren Sie mehr über unsere NuPAGE Bis-Tris-Gele >
Migrationsdiagramme ansehen ›

Wählen Sie das richtige NuPAGE Bis-Tris-Gel für Ihre Proteintrennung
Erzielen Sie die optimale Trennung Ihrer Proteine durch Auswahl der richtigen Kombination aus Gel und Laufpuffer. NuPAGE Bis-Tris Proteingele sind in vier Polyacrylamid-Konzentrationen erhältlich: 8 %, 10 %, 12 % und 4 bis 12 %-Gradient. Gele sind in zwei Größen erhältlich: Mini (8 cm x 8 cm) oder Midi (8,7 cm x 13,3 cm) und entweder 1,0 mm (Mini- und Midi-Gele) oder 1,5 mm (nur Mini-Gel-Format) in Dicke. NuPAGE Bis-Tris-Gele sind auch in verschiedenen Well-Formaten erhältlich.

NuPAGE Bis-Tris-Gele sind für denaturierende Gelelektrophoreseanwendungen formuliert. Für eine optimale Probenvorbereitung verwenden Sie NuPAGE LDS-Probenpuffer und NuPAGE-Probenreduktionsmittel. Verwenden Sie NuPAGE Antioxidans im Laufpuffer, um den reduzierten Proteinzustand während des Laufs aufrechtzuerhalten und eine maximale Bandenschärfe zu ermöglichen. Die Gele können mit NuPAGE MES SDS-Laufpuffer zur besseren Auflösung kleiner Proteine oder mit dem NuPAGE MOPS SDS-Laufpuffer zur Auflösung mittlerer bis großer Proteine verwendet werden.

Darüber hinaus bieten wir NuPAGE Tris-Acetat-Gele für die Trennung größerer Proteine. Für die klassische Laemmli-basierte Tris-Glycin-Elektrophorese bieten wir Novex Tris-Glycin-Gele an.

Für die Übertragung von Proteinen auf eine Membran empfehlen wir die Verwendung des NuPAGE Transferpuffers. Ein schneller halbtrockener Transfer kann mit dem Invitrogen Power Blotter, ein schneller trockener Transfer mit dem iBlot 2 Gel Transfergerät durchgeführt werden. Alternativ kann der herkömmliche Nasstransfer mit dem XCell II Blot-Modul oder dem Mini-Blot-Moduldurchgeführt werden.

Verwandte Links
Überblick über die 1D-Proteinelektrophorese
Vergleich von NuPAGE Tris-Bis und herkömmlichen Tris-Glycin-Gelen
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Zur Verwendung mit (Geräte)XCell SureLock Mini-Zelle
Gel Thickness1,0 mm
Länge (metrisch)8 cm
TrennmodusMolekulargewicht
Menge10 Gele/Karton
Probenladevolumen7 cm-Streifen
Haltbarkeit12 Monate
VersandbedingungRaumtemperatur
LagerungsbedingungenBei 4–25 °C lagern. Nicht einfrieren.
Breite (metrisch)8 cm
Gelanteil (%)4 bis 12%
GelgrößeMini
GeltypBis-Tris
ProduktlinieNuPAGE, ZOOM
Trennbereich3,5 bis 260 kDa
TrennverfahrenDenaturierung
WellsIPG-Well
Unit SizeEach
Inhalt und Lagerung
Jede Packung enthält 10 Gele. Bei 4 – 25 °C lagern. Nicht einfrieren. Die Haltbarkeit beträgt 12 Monate.

Häufig gestellte Fragen (FAQ)

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 NuPAGE™ 4 bis 12 %, Bis-Tris, 1,0–1,5 mm, Mini-Protein-Gele FAQs

Zitierungen und Referenzen (4)

Zitierungen und Referenzen
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