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What else can I help you with?
Is all bacteria killed by hand gels?
No, not all bacteria is killed by hand gels. Most hand gel products do say that they are 99.99% effective, but the .01% is the bacteria that the hand gel cannot kill. Since bacteria have the ability to mutate to form resistance against hand gels, not all bacteria can be killed by hand gels.
Why dont you use ethidium bromide staining for non denaturing PAGE gels?
Ethidium bromide is commonly used for staining native PAGE gels where proteins are kept in their native state. However, ethidium bromide is typically used for staining DNA in denaturing PAGE gels as it binds to DNA molecules specifically, providing better visualization compared to proteins in native gels. This is why alternative stains such as Coomassie blue or silver staining are typically used for proteins in non-denaturing PAGE gels.
Do Gels conduct electricity?
Yes, some gels can conduct electricity if they contain ions that can move in response to an electric field. These gels are known as ion-conductive gels and are often used in applications like batteries, sensors, and actuators.
Is gel flammable?
Yes, some gels are flammable. How flammable would depend on it's alcohol, or flammable substance content. Some gels are not flammable at all, and others a very flammable.
What are water jelly crystals?
They are cross-linked polyacrylamide copolymeric gels.
Who discovered SDS PAGE electrophoresis?
SDS-PAGE electrophoresis was developed by biochemist Ulrich K. Laemmli in 1970. It is a widely used technique for separating proteins based on their molecular weight.
Why using DTT in laemmli?
Dithiothreitol (DTT) is commonly used in Laemmli buffer to reduce disulfide bonds in proteins, preventing their reformation during electrophoresis. This helps maintain proteins in their denatured state, allowing for more accurate separation based on size during SDS-PAGE. DTT also helps to ensure that proteins remain in a linear conformation for consistent migration through the gel.
What is the classification of gels?
By mass, they are classified as liquids. However, if one examines the intermolecular attractions in between the molecules, gels will appear solid. Therefore, gels are classified somewhere in between.
Why should people use bath gels?
People often use bath gels because they keep their skin soft, and moisturized. Gels without dyes are particularly good for the skin.
What are the differences between tris-glycine and bis-tris gels in terms of their composition and performance in protein electrophoresis?
Tris-glycine gels contain both tris and glycine buffers, while bis-tris gels use bis-tris buffer. Bis-tris gels offer better resolution and sharper bands in protein electrophoresis compared to tris-glycine gels.
Do you have to use a redken color gel developer with redken color gels or can you use any developer?
Redken Color Gels developer is formulated specifically for Gels, but using any developer will still work.
Do all shower gels have water?
yes, all shower gels will contain water unless they specifically state otherwise.
Can sds gels be reused?
SDS gels cannot typically be reused because the separating gel portion degrades during the electrophoresis process. However, stacking gels may be reusable if they remain intact and free from contamination. It is recommended to prepare fresh gels for subsequent experiments to ensure accurate and reliable results.
What are the dangers of sport gels?
They are unhealthy.
What is a compound that can hold water?
gels
Are gels used to read DNA sequences?
They do not sequence DNA by themselves but gels can separate DNA pieces to then be used for sequencing. Basically no
What are the differences between bis-tris and tris-glycine gels in terms of their composition and performance in protein electrophoresis?
Bis-Tris gels and Tris-Glycine gels differ in their composition and performance in protein electrophoresis. Bis-Tris gels use bis-Tris buffer and have a more stable pH range, resulting in sharper protein bands. Tris-Glycine gels use Tris-Glycine buffer and are more commonly used for separating smaller proteins. Overall, the choice between the two gels depends on the specific needs of the experiment and the proteins being analyzed.
