NuPAGE™ Bis-Tris Midi Protein Gels, 4 to 12%, 1.0 mm
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NuPAGE™ Bis-Tris Midi Protein Gels, 4 to 12%, 1.0 mm
Invitrogen™

NuPAGE™ Bis-Tris Midi Protein Gels, 4 to 12%, 1.0 mm

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 NumberWells
WG1401BOX12 + 2-well
WG1401A12 + 2-well, w/adapters
WG1402BOX20-well
WG1402A20-well, w/adapters
WG1403BOX26-well
WG1403A26-well, w/adapters
Catalog number WG1401BOX
Price (EUR)
269,65
Online Exclusive
290,00
Save 20,35 (7%)
10 gels (1 box)
Add to cart
Wells:
12 + 2-well
Price (EUR)
269,65
Online Exclusive
290,00
Save 20,35 (7%)
10 gels (1 box)
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.

NuPAGE Bis-Tris Midi gels can be used with the XCell SureLock Midi Cell gel apparatuses (WR0100) or conveniently with the Bio-Rad Criterion Cell using our adapters (WA0999).

For transfer of proteins to a membrane, rapid semi-dry transfer can be done using the Invitrogen Power Blotter or rapid dry transfer using the iBlot 2 Gel Transfer Device (IB21001). Alternatively, traditional wet transfer can be performed using the Bio-Rad Criterion Cell using NuPAGE Transfer buffer (NP00061).

For Research Use Only. Not for use in diagnostic procedures.
Specifications
AdaptersNo Adapters
Gel Thickness1.0 mm
Length (Metric)8 cm
Mode of SeparationMolecular Weight
Product LineNuPAGE
Quantity10 gels (1 box)
Recommended ApplicationsDenaturing
Sample Loading VolumeUp to 45 μL + 15 μL
Shelf Life12 Months
Shipping ConditionRoom Temperature
Storage RequirementsStore at 4–25°C. Do not freeze.
Width (Metric)13 cm
For Use With (Equipment)XCell4 SureLock Midi-Cell, SureLock Tandem Midi Gel Tank
Gel Percentage4 to 12%
Gel SizeMidi
Gel TypeBis-Tris
Separation Range3.5 to 260 kDa
Separation TypeDenaturing
Wells12 + 2-well
Unit Size10 gels (1 box)

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.

Do I need to add water or buffer to the Displacement Dam when I run one or two gels in the XCell4 SureLock Midi-Cell?

The XCell4 Displacement Dam is used when fewer than 3 gels are run in the XCell4 SureLock Midi-Cell. The Displacement Dam is placed in the lower buffer chamber instead of a second buffer core. Do not add any buffer or water to the Displacement Dam. However, if water or buffer is accidentally added to the Displacement Dam, it does not affect the electrophoresis run.

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

What are the maximum load volumes for the NuPAGE Midi Gels?

Recommended maximum load volumes:
12 + 2-well gel: 45 µL in sample well, 15 µL in marker well
20-well gel: 25 µL
26-well gel: 15 µL

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

Citations & References (3)

Citations & References
Abstract
Rapid purification and mass spectrometric characterization of mitochondrial NADH dehydrogenase (Complex I) from rodent brain and a dopaminergic neuronal cell line.
Authors:Schilling B, Bharath M M S, Row RH, Murray J, Cusack MP, Capaldi RA, Freed CR, Prasad KN, Andersen JK, Gibson BW,
Journal:Mol Cell Proteomics
PubMed ID:15591592
'Oxidative stress and mitochondrial dysfunction signify important biochemical events associated with the loss of dopaminergic neurons in Parkinson''s disease (PD). Studies using in vitro and in vivo PD models or tissues from diseased patients have demonstrated a selective inhibition of mitochondrial NADH dehydrogenase (Complex I of the OXPHOS electron transport ... More
Intrinsic protein fluorescence interferes with detection of tear glycoproteins in SDS-polyacrylamide gels using extrinsic fluorescent dyes.
Authors:Zhao Z, Aliwarga Y, Willcox MD,
Journal:J Biomol Tech
PubMed ID:18166676
Intrinsic protein fluorescence may interfere with the visualization of proteins after SDS-polyacrylamide electrophoresis. In an attempt to analyze tear glycoproteins in gels, we ran tear samples and stained the proteins with a glycoprotein-specific fluorescent dye. The fluorescence detected was not limited to glycoproteins. There was strong intrinsic fluorescence of proteins ... More
Trypanosoma brucei glycoproteins contain novel giant poly-N-acetyllactosamine carbohydrate chains.
Authors:Atrih A, Richardson JM, Prescott AR, Ferguson MA,
Journal:J Biol Chem
PubMed ID:15509560
The flagellar pocket of the bloodstream form of the African sleeping sickness parasite Trypanosoma brucei contains material that binds the beta-d-galactose-specific lectin ricin (Brickman, M. J., and Balber, A. E. (1990) J. Protozool. 37, 219-224). Glycoproteins were solubilized from bloodstream form T. brucei cells in 8 M urea and 3% ... More