NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0 mm, WedgeWell™ format
NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0 mm, WedgeWell™ format
Invitrogen™

NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0 mm, WedgeWell™ format

Invitrogen NuPAGE Tris-Acetate protein gels, WedgeWell format provide excellent separation of large molecular weight proteins. They are high performance polyacrylamide gels that simulate the denaturing or native conditions of the traditional Laemmli system.
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Catalog NumberWells
TA03815BOX15-well
TA03810BOX10-well
TA03812BOX12-well
Catalog number TA03815BOX
Price (CNY)
1,121.00
飞享价
Ends: 31-Dec-2025
1,495.00
Save 374.00 (25%)
10 gels (1 box)
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Wells:
15-well
Price (CNY)
1,121.00
飞享价
Ends: 31-Dec-2025
1,495.00
Save 374.00 (25%)
10 gels (1 box)
Add to cart
Invitrogen NuPAGE Tris-Acetate protein gels, WedgeWell format provide excellent separation of large molecular weight proteins. They are high performance polyacrylamide gels that simulate the denaturing or native conditions of the traditional Laemmli system. The unique buffer formulation maintains a low operating pH during electrophoresis, resulting in superior resolution of high molecular weight proteins compared to traditional Tris-glycine SDS-PAGE gels.

Invitrogen NuPAGE Tris-Acetate WedgeWell format protein gels provide excellent separation of large molecular weight proteins. They are high performance polyacrylamide gels that simulate the denaturing or native conditions of the traditional Laemmli system. The unique buffer formulation maintains a low operating pH during electrophoresis, resulting in superior resolution of high molecular weight proteins compared to traditional Tris-glycine SDS-PAGE gels.

Product features

  • High resolution—gels offer optimal separation of high molecular weight proteins
  • Better protein integrity—sample preparation process has been optimized to help preserve proteins
  • Longer shelf life—gels can be stored for at least 12 months
  • Wedge-shaped wells—for easier sample loading and up to two times higher sample volume

Run your proteins in native or denatured form

NuPAGE Tris-Acetate protein gels do not contain SDS and can be used to separate proteins in native or denatured form. For denatured proteins, we recommend using NuPAGE LDS Sample Buffer (NP0007) and NuPAGE Tris-Acetate SDS Running Buffer (LA0041). For native proteins, we recommend using Novex Tris-Glycine Native Sample Buffer (LC2673) and Novex Tris-Glycine Native Running Buffer (LC2672).

For transfer of proteins to a membrane, we recommend using NuPAGE Transfer Buffer (NP00061) for traditional wet transfer using the XCell II Blot Module (EI9051) or the Mini Blot Module (B1000). Alternatively, rapid semi-dry transfer can be done using the Invitrogen Power Blotter or rapid dry transfer using the iBlot 3 Gel Transfer Device (IB31001).

Convenient to use

NuPAGE Tris-Acetate WedgeWell format gels have innovative wedge-shaped wells that allow up to two times more sample load volume than other 1.0 mm-thick gels. The wedge-shaped wells also have larger openings, making sample loading easier. The mini gels can be run using our XCell SureLock Mini-Cell (EI0001) or Mini Gel Tank (A25977).

For Research Use Only. Not for use in diagnostic procedures.
Specifications
Gel Thickness1.0 mm
Length (Metric)13 cm
Mode of SeparationMolecular Weight
Product LineNuPAGE
Quantity10 Gels/Box
Sample Loading VolumeUp to 35 μL
Shelf Life12 Months
Shipping ConditionWet Ice
Width (Metric)8 cm
For Use With (Equipment)Mini Gel Tank, XCell SureLock Mini-Cell
Gel Percentage3 to 8%
Gel SizeMini
Gel TypeTris-Acetate
Separation Range36 to 500 kDa
Separation TypeDenaturing, Native
Wells15-well
Unit Size10 gels (1 box)
Contents & Storage
Store at 4°C to 25°C. Do not freeze.

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 does it mean when bands appear to be getting narrower (or "funneling") as they progress down a protein gel?

There may be too much beta-mercaptoethanol (BME), sample buffer salts, or dithiothreitol (DTT) in your samples. If the proteins are over-reduced, they can be negatively charged and actually repel each other across the lanes causing the bands to get narrower as they progress down the gel.

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

View all NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0 mm, WedgeWell™ format FAQs