More and more researchers use prefabricated glue instead of manual glue

First of all, let's popularize what prefabricated rubber is.
Prefabricated rubber, as the name implies, is a manufacturer prepared in advance of the gel. The advantage of prefabricated rubber is that it can be used when you open the package and the sample can run away, which can greatly speed up the experiment process, and keep you away from cumbersome operation and toxic reagents, no longer worry about leakage of glue and other problems.

Prefabricated rubber gives many researchers a better experience, the reasons are: the composition of prefabricated rubber is more uniform, small differences between batches, the final data will reflect a higher consistency and repeatability; At the same time, compared with manual gumming, the protein bands separated by preform gum are sharper, higher resolution and better electrophoretic results. Prefabricated rubber also has an advantage in the long shelf life. Homemade gels can only be preserved for about a week, while prefabricated gels can be preserved for months, or even a year.

Now, more and more researchers are using non-denatured gels. Compared with denatured gels, non-denatured gel systems without SDS can isolate proteins while retaining their natural structure, so they can be used in the study of protein interaction and the separation and analysis of protein complexes.

The NativePAGE Bis-Tris immutable protein preform is based on the principle of Blue-Native PAGE. Coomassie brilliant blue G-250 is attached to the protein with a negative charge while keeping the protein in its natural state without denaturation. Before adding G-250 to the protein sample containing Nonionic surfactant, the protein can be negatively charged. At the same time, G-250 will be added to the cathodic buffer to provide continuous G-250 for the gel. The traditional non-denaturing electrophoresis mostly uses Tris- glycine system, its working pH Higher (9.3-9.5) had adverse effects on sensitive proteins under high pH conditions, whereas the working pH of NativePAGE Bis-Tris preforms was close to neutral (7.5-7.7). Helps maintain the natural structure of proteins and the activity of proteins that are sensitive to high pH values. At the same time, the traditional Tris- glycine non-denaturing electrophoretic system mainly uses the working pH higher than the protein isoelectric point and causes it to carry on the electrophoretic after the negative charge, therefore is not suitable for the isoelectric point higher than the electrophoretic working pH protein. And NativePAGE uses Comas Bright blue G-250 causes the protein to be negatively charged under non-denaturation conditions and electrophoretic under near-neutral working pH, so the restriction caused by the isoelectric point of the protein is no longer considered.

The material comes from the network