NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0–1.5 mm
NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0–1.5 mm
Invitrogen™

NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0–1.5 mm

Invitrogen NuPAGE Tris-Acetate 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.
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Catalog NumberWellsGel ThicknessQuantity
EA0375BOX10-well1.0 mm10 Gels/Box
EA0375PK210-well1.0 mm2 Gels/Box
EA03752BOX12-well1.0 mm10 Gels/Box
EA03752PK212-well1.0 mm2 Gels/Box
EA03755BOX15-well1.0 mm10 Gels/Box
EA0378BOX10-well1.5 mm10 Gels/Box
EA03785BOX15-well1.5 mm10 Gels/Box
Catalog number EA0375BOX
Price (USD)
164.00
Each
Add to cart
Wells:
10-well
Gel Thickness:
1.0 mm
Quantity:
10 Gels/Box
Price (USD)
164.00
Each
Add to cart
Invitrogen NuPAGE Tris-Acetate 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.

Features of NuPAGE Tris-Acetate gels:
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 self life—gels can be stored for at least eight months

Choose the right NuPAGE Tris-Acetate gel for your protein separation
Obtain optimal separation of your high molecular weight proteins by choosing the right combination of gel and running buffer. NuPAGE Tris-Acetate protein gels come in a polyacrylamide concentration of 7% and a 3–8% 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 Tris-Acetate gels also come in multiple well formats. Mini gels can be run using our XCell SureLock Mini-Cell (EI0001) or Mini Gel Tank (A25977). Midi gels can be run using our XCell4 SureLock Midi-Cell (WR01000) or conveniently with the Bio-Rad Criterion™ Cell using our adapters (WA0999).

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 2 Gel Transfer Device (IB21001).

For Research Use Only. Not for use in diagnostic procedures.
Specifications
For Use With (Equipment)Mini Gel Tank, XCell SureLock Mini-Cell
Gel Percentage3 to 8%
Gel SizeMini
Gel Thickness1.0 mm
Gel TypeTris-Acetate
Recommended ApplicationsDenaturing, Native
Sample Loading VolumeUp to 25 μL
Separation Range36 to 500 kDa
Separation TypeDenaturing, Native
Shelf Life8 Months
Wells10-well
Mode of SeparationMolecular Weight
Product LineNuPAGE™
Quantity10 Gels/Box
Shipping ConditionWet Ice
Storage RequirementsStore at 2°C to 8°C. Do not freeze.
Length (Metric)13 cm
Width (Metric)8 cm
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 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.