NuPAGE™ Large Protein Staining Kit
Product Image
Invitrogen™

NuPAGE™ Large Protein Staining Kit

The HiMark™ Pre-Stained and Unstained High Molecular Weight Protein Standards are specifically designed for large protein analysis on NuPAGE™ NovexRead more
Have Questions?
Catalog NumberQuantity
LP000220 gels kit
Catalog number LP0002
Price (HKD)
7,843.00
Each
Add to cart
Quantity:
20 gels kit
Request bulk or custom format
Price (HKD)
7,843.00
Each
Add to cart
The HiMark™ Pre-Stained and Unstained High Molecular Weight Protein Standards are specifically designed for large protein analysis on NuPAGE™ Novex Tris-Acetate Gels under denaturing conditions. Both standards offer a time-saving load-and-go format.

The HiMark™ Pre-stained Standard includes one pink colored orientation band and eight blue bands ranging in apparent molecular weight of 31 - 460 kDa* in NuPAGE™ Tris-Acetate Gel/SDS buffer system (Figure 1). It's suitable for monitoring electrophoresis, western transfer, and approximating molecular weight of unknown big proteins.

The HiMark Unstained Standard, along with the NuPAGE™ Tris-Acetate Gel/SDS buffer system, offers the highest accuracy for molecular weight estimation of large proteins. It consists of nine proteins, ranging in size from 40 to 500 kDa in NuPAGE™ Novex 3-8% and 7% Tris-Acetate Gel/SDS buffer systems (Figure 2). Visualize with Coomassie™ stain, silver, and fluorescent protein stains post-electrophoresis. A downloadable molecular weight calculator is designed for easy and accurate MW estimation of large proteins using the HiMark™ Unstained Standard on a NuPAGE™ Tris-Acetate Gel.**

Several NuPAGE™ Large Protein Starter Kits are available to provide you with all necessary reagents and optimized protocols for highresolution large protein separation and analysis (Table 1). Each kit includes two boxes of NuPAGE™ 3-8% Tris-Acetate Gels, Tris-Acetate SDS Buffer Kit, a staining reagent or blotting membranes, and a vial of the appropriate HiMark™ Standard.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
For Use With (Equipment)XCell SureLock Mini-Cell
Quantity20 gels kit
Sample Loading Volume25 μL
Thickness1.0 mm
Well Design1D Well
Product LineNuPAGE
Product TypeProtein Stain Kit
Separation Range40 to 500 kDa
Stain TypeUnstained
Unit SizeEach
Contents & Storage
See product manual for kit contents and component storage conditions. Components of each kit are also available individually.

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.

I ran my protein under native conditions on a Tris-Glycine gel. It has a pI that is higher than the pH of the Tris-Glycine transfer buffer. Can you offer some tips for transferring it?

- Increase the pH of Tris-Glycine transfer buffer to 9.2, allowing all the proteins below pI 9.2 to transfer towards the anode electrode.
- Use the Tris-Glycine transfer buffer and place a membrane on both sides of the gel. If there are any proteins that are more basic than the pH of the transfer buffer, they will be captured on the extra membrane placed on the cathode side of the gel. Both membranes can then be developed in the same manner.
- Prior to blotting, incubate the gel for 15 minutes in Tris-Glycine transfer buffer containing 0.1% SDS. The small amount of SDS will give the proteins enough charge to move unidirectionally towards the anode and in most cases, should not denature the protein. Proceed with the transfer using regular Tris-Glycine transfer buffer.

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