The HiMark™ Pre-Stained and Unstained High Molecular Weight Protein Standards are specifically designed for large protein analysis on NuPAGE™ Novex了解更多信息
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货号
数量
LP0002
20 份凝胶
货号 LP0002
价格(CNY)
8,672.00
Each
添加至购物车
数量:
20 份凝胶
请求批量或定制报价
价格(CNY)
8,672.00
Each
添加至购物车
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.
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.
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.
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.