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Why two stains required in SDS PAGE- bromophenol blue and coomassie blue?
Wiki User
∙ 13y ago
bromophenol blue is used as the tracking dye while coomassie brilliant blue is the staining dye.
Wiki User
∙ 13y ago
Bromophenol blue is a tracking dye used to monitor the progress of electrophoresis, helping visualize the migration of proteins in the gel. Coomassie blue is a protein dye used for staining proteins after electrophoresis, allowing for their visualization and quantification. Both stains serve distinct purposes in the SDS-PAGE process to ensure accurate results and analysis.
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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.
What is difference between sds page and western blotting?
SDS-PAGE is a technique used to separate proteins based on their size, while western blotting is a technique used to detect specific proteins in a sample using antibodies. In SDS-PAGE, proteins are separated by gel electrophoresis, while in western blotting, proteins are transferred from a gel to a membrane for detection using antibodies.
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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.
Why you put bromophenol blue in lysis buffer?
Bromophenol blue is added to lysis buffer as a tracking dye to monitor the progress of protein electrophoresis. It helps visualize the sample migration through the gel during SDS-PAGE by imparting a blue color to the proteins.
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