With the DUALmembrane Screening System, full-length membrane integrated bait proteins are screened against cDNA library expressed prey proteins to identify interactions between potentially unidentified integral membrane and soluble proteins. This technology takes advantage of the split-ubiquitin activation mechanism in which a first protein (the bait) is fused to the C-terminal half of ubiquitin, and a second protein (the prey) is fused to the mutated ubiquitin N-terminus. Interaction between bait and prey results in translocation of an artificial transcription factor to the nucleus to activate a reporter gene. This system allows screening integral membrane proteins without the traditional issues of protein solubility and nuclear localization. Full-length membrane proteins, including those with multiple transmembrane domains, can be screened without truncation or selection of specific subdomains. Complete vector sets allow cloning and expression of type I and II membrane proteins, and a highly sensitive yeast host strain ensures superior screening stringency.
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