Curious about the firsthand experience with GenScript SurePAGE gels?
In a recent conversation with the esteemed Li Laboratory from Arc Institute and Stanford University, Rebecca Chan (Graduate Student) shared insights into how SurePAGE Gel's exceptional features have significantly boosted their efficiency in high throughput protein analysis.
Let's dive into the discussion with the Stanford/Arc Li Lab to uncover how SurePAGE Gel has become an indispensable tool in their research.
How did the Stanford team discover the GenScript SurePAGE gel?
Rebecca: As a lab of 10-12 people who use a lot of gels daily, we were looking for alternative precast gels that are easy to use, provide reliable results, and are cost-effective. Once we discovered SurePAGE Gel that delivered the needed features, we decided to switch to the SurePAGE Gels.
Can you share how the SurePAGE Gel helped your day-to-day workflow?
Rebecca: We were using another popular brand before switching to SurePAGE Gels. Since our throughput is large, SurePAGE Gel with its cost-efficiency and reliable results is more advantageous for us in the long term. SurePAGE gels also have larger well capacity providing excellent convenience for loading more samples. Furthermore, unlike the previous gel, SurePAGE Gel doesn’t require the additional step of cutting the gel after electrophoresis, which makes it highly convenient. It was quite smooth for our team to switch to SurePAGE gel after we gave it a try.
Large well volume up to 80 μl
Do you have any concluding remarks to share with other scientists?
Rebecca: SurePAGE Gel has been extremely helpful for our workflow, especially with our large throughput. We’ve been consistently ordering bulk quantities of gels every 6-8 months, and the logistics and storage are quite easy.
Interview conducted by Monica Sun, Product Manager at GenScript's Products Division.
The Li Lab stands as a cornerstone within the partnership program of Stanford University and Arc Institute, a nonprofit research organization dedicated to advancing biomedical sciences and technology. By integrating chemistry, biochemistry, immunology, and physiology, the lab delves into the fundamental mechanisms of a critical innate immune pathway, the cGAS-cGAMP-STING pathway. This signaling axis is an important primary defense system against foreign pathogens and can be harnessed for a more targeted anti-cancer response. Activation of cGAS-STING is a viable therapeutic strategy for pathogen infection or to promote tumor surveillance by the immune system, while inhibition has proven beneficial for treating autoimmune diseases and neurodegeneration. The Li Lab explores the novel biochemistry of this pathway to develop new therapeutic targets and design drugs that can more precisely manipulate this signaling cascade in a variety of disease contexts.
Rebecca Chan Rebecca is currently a graduate student at the Department of Chemical and System Biology. She completed her B.S. in Chemical Biology from UC Berkeley followed by two years of research in Judith Frydman’s lab studying chaperone-huntingtin interactions. At Arc Institute with the Li Lab, Rebecca is dedicated to understanding the cellular and biochemical factors that regulate STING activation.
Li Lab’s Publications 1. Chan, R. J., Cao, X., Ergun, S. L., Evert Njomen, Lynch, S. R., Cravatt, B. F., & Li, L. (2023). Blocking oligomerization is the most viable strategy to inhibit STING. BioRxiv (Cold Spring Harbor Laboratory). Read more >> 2. Ritchie, C., Li, L. (2023). STING activation of IRF3 is tuned by PELI2 to suppress basal activation and reinforce the anti-viral response. BioRxiv (Cold Spring Harbor Laboratory). Read more >> 3. Cordova, A. F., Ritchie, C., Böhnert, V., & Li, L. (2021). Human SLC46A2 Is the Dominant cGAMP Importer in Extracellular cGAMP-Sensing Macrophages and Monocytes. ACS Central Science, 7(6), 1073–1088. Read more >> 4. Carozza, J. A., Brown, J. A., Böhnert, V., Fernandez, D., AlSaif, Y., Mardjuki, R. E., Smith, M., & Li, L. (2020). Structure-Aided Development of Small-Molecule Inhibitors of ENPP1, the Extracellular Phosphodiesterase of the Immunotransmitter cGAMP. Cell Chemical Biology, 27(11), 1347-1358.e5. Read more >> 5. Ergun, S. L., Fernandez, D., Weiss, T. G., & Li, L. (2019). STING Polymer Structure Reveals Mechanisms for Activation, Hyperactivation, and Inhibition. Cell, 178(2), 290-301.e10. Read more >> View the full publication list. click here >>
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