NuPAGE™ Bis-Tris Mini Protein Gels, 4–12%, 1.0–1.5 mm

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NuPAGE™ Bis-Tris Mini Protein Gels, 4–12%, 1.0–1.5 mm

Name: NuPAGE™ Bis-Tris Mini Protein Gels, 4–12%, 1.0–1.5 mm
SKU: NP0330BOX
Price: 992.00 CNY

Invitrogen NuPAGE Bis-Tris protein gels are precast polyacrylamide gels that provide broad molecular weight protein separation with high resolution and sample integrity.

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Catalog Number	Wells	Gel Thickness	Quantity
NP0330BOX	IPG-well	1.0 mm	10 gels (1 box)
NP0321BOX	10-well	1.0 mm	10 gels (1 box)
NP0321PK2	10-well	1.0 mm	2 gels (1 box)
NP0322BOX	12-well	1.0 mm	10 gels (1 box)
NP0322PK2	12-well	1.0 mm	2 gels (1 box)
NP0323BOX	15-well	1.0 mm	10 gels (1 box)
NP0323PK2	15-well	1.0 mm	2 gels (1 box)
NP0324BOX	1-well	1.0 mm	10 gels (1 box)
NP0326BOX	2D-well	1.0 mm	10 gels (1 box)
NP0327BOX	9-well	1.0 mm	10 gels (1 box)
NP0329BOX	17-well	1.0 mm	10 gels (1 box)
NP0329PK2	17-well	1.0 mm	2 gels (1 box)
NP0335BOX	10-well	1.5 mm	10 gels (1 box)
NP0335PK2	10-well	1.5 mm	2 gels (1 box)
NP0336BOX	15-well	1.5 mm	10 gels (1 box)
NP0336PK2	15-well	1.5 mm	2 gels (1 box)

16 Options

Catalog number NP0330BOX

Price (CNY)

992.00

Each

Add to cart

Wells:

IPG-well

Gel Thickness:

1.0 mm

Quantity:

10 gels (1 box)

Price (CNY)

992.00

Each

Add to cart

Invitrogen NuPAGE Bis-Tris protein gels are precast polyacrylamide gels that provide broad molecular weight protein separation with high resolution and sample integrity. These precast gels are ideal for applications where protein integrity is crucial. Unlike traditional Tris-glycine gels, NuPAGE Bis-Tris gels have a neutral pH environment that minimizes protein modifications. Use NuPAGE Bis-Tris gels for preparing proteins for sequencing, mass spectrometry, and any other techniques where protein integrity is important.

Features of NuPAGE Bis-Tris gels:
• Better protein integrity—optimized sample preparation process preserves your proteins
• Wide ranges of molecular weight separation—select the right gel and running buffer to get the optimal separation of your proteins
• Faster run times—get separation of your proteins in as little as 35 minutes
• Longer shelf life—NuPAGE Bis-Tris gels can be stored for at least 12 months at room temperature

Choose the right NuPAGE Bis-Tris gel for your protein separation
Obtain optimal separation of your proteins by choosing the right combination of gel and running buffer. NuPAGE Bis-Tris protein gels come in four polyacrylamide concentrations: 8%, 10%, 12%, and a 4–12% gradient. Gels come in two sizes: mini (8 cm x 8 cm) or midi (8.7 cm x 13.3 cm) and either 1.0 mm (mini and midi gels) or 1.5 mm (mini gel format only) in thickness. NuPAGE Bis-Tris gels also come in multiple well formats.

NuPAGE Bis-Tris gels are formulated for denaturing gel electrophoresis applications. For optimal sample preparation, use the NuPAGE LDS Sample Buffer (NP0007) and NuPAGE Sample Reducing Agent (NP0004). Use NuPAGE Antioxidant (NP0005) in the running buffer to maintain the reduced state of the proteins during the run and to allow maximum band sharpness. The gels can be run using NuPAGE MES SDS Running Buffer (NP0002) to better resolve small proteins or NuPAGE MOPS SDS Running Buffer (NP000102) to resolve medium- to large-size proteins.

For transfer of proteins to a membrane, we recommend using NuPAGE Transfer Buffer (NP00061) for traditional wet transfer using the Mini Blot Module (B1000) or XCell II Blot Module (EI9051). Alternatively, rapid semi-dry transfer can be done using the Invitrogen Power Blotter or rapid dry transfer using the iBlot 2 Gel Transfer Device (IB21001).

For Research Use Only. Not for use in diagnostic procedures.

Specifications

Gel Thickness1.0 mm

Length (Metric)8 cm

Mode of SeparationMolecular Weight

Product LineNuPAGE™, ZOOM™

Quantity10 gels (1 box)

Sample Loading Volume7 cm strips

Shelf Life12 Months

Shipping ConditionRoom Temperature

Storage RequirementsStore at 4–25°C. Do not freeze.

Width (Metric)8 cm

For Use With (Equipment)Mini Gel Tank, XCell SureLock Mini-Cell

Gel Percentage4 to 12%

Gel SizeMini

Gel TypeBis-Tris

Separation Range3.5 to 260 kDa

Separation TypeDenaturing

WellsIPG-well

Unit SizeEach

Frequently asked questions (FAQs)

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™ Bis-Tris Mini Protein Gels, 4–12%, 1.0–1.5 mm FAQs