NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0–1.5 mm
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NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0–1.5 mm
Citations & References (4)
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
EA03755BOX15-well1.0 mm10 Gels/Box
EA0375BOX10-well1.0 mm10 Gels/Box
EA0375PK210-well1.0 mm2 Gels/Box
EA03752BOX12-well1.0 mm10 Gels/Box
EA03752PK212-well1.0 mm2 Gels/Box
EA0378BOX10-well1.5 mm10 Gels/Box
EA03785BOX15-well1.5 mm10 Gels/Box
Catalog number EA03755BOX
Price (CNY)
696.00
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Ends: 31-Dec-2025
992.00
Save 296.00 (30%)
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Wells:
15-well
Gel Thickness:
1.0 mm
Quantity:
10 Gels/Box
Price (CNY)
696.00
Online Exclusive
Ends: 31-Dec-2025
992.00
Save 296.00 (30%)
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
Gel Thickness1.0 mm
Length (Metric)8 cm
Mode of SeparationMolecular Weight
Product LineNuPAGE
Quantity10 Gels/Box
Recommended ApplicationsDenaturing, Native
Sample Loading VolumeUp to 15 μL
Shelf Life8 Months
Shipping ConditionWet Ice
Storage RequirementsStore at 2°C to 8°C. Do not freeze.
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 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.

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

Citations & References (4)

Citations & References
Abstract
The cytoplasmic tail of L-selectin interacts with members of the Ezrin-Radixin-Moesin (ERM) family of proteins: cell activation-dependent binding of Moesin but not Ezrin.
Authors:Ivetic A, Deka J, Ridley A, Ager A,
Journal:J Biol Chem
PubMed ID:11706008
L-selectin regulates the recruitment of naive lymphocytes from the bloodstream to secondary lymphoid organs, mediating their initial capture and subsequent rolling along high endothelial cell surface-expressed ligands in peripheral lymph nodes. In vivo, distribution of L-selectin and cell surface levels determine the tethering efficiency and rolling velocity of leukocytes, respectively. ... More
The 'involution' of mannose-binding lectin.
Authors:Seyfarth J, Garred P, Madsen HO,
Journal:Hum Mol Genet
PubMed ID:16115813
Mannose-binding lectin (MBL) acts as a serum opsonin in innate immune defense and induces complement activation by the lectin pathway. In humans, low levels of functional serum MBL are caused by the dominant action of three single nucleotide substitutions in exon 1 that disrupt the glycine-rich backbone structure of the ... More
Tethering sigma70 to RNA polymerase reveals high in vivo activity of sigma factors and sigma70-dependent pausing at promoter-distal locations.
Authors:Mooney RA, Landick R,
Journal:Genes Dev
PubMed ID:14630944
Bacterial sigma factors compete for binding to RNA polymerase (RNAP) to control promoter selection, and in some cases interact with RNAP to regulate at least the early stages of transcript elongation. However, the effective concentration of sigmas in vivo, and the extent to which sigma can regulate transcript elongation generally, ... More
Complement factor H is a serum-binding protein for adrenomedullin, and the resulting complex modulates the bioactivities of both partners.
Authors:Pio R, Martinez A, Unsworth EJ, Kowalak JA, Bengoechea JA, Zipfel PF, Elsasser TH, Cuttitta F,
Journal:J Biol Chem
PubMed ID:11116141
Adrenomedullin (AM) is an important regulatory peptide involved in both physiological and pathological states. We have previously demonstrated the existence of a specific AM-binding protein (AMBP-1) in human plasma. In the present study, we developed a nonradioactive ligand blotting assay, which, together with high pressure liquid chromatography/SDS-polyacrylamide gel electrophoresis purification ... More