Cell: a brighter protein labeling system
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Last Update: 2015-01-30
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Source: Internet
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Author: User
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A single DNA or RNA molecule in an imaging cell usually inserts multiple copies of a specific sequence into the target molecule to allow the fluorescent labeled protein to bind The more copies of this sequence, the more fluorescent protein the target molecule binds, and the brighter the signal "Why not treat the protein like this?" Marvin Tanenbaum, a postdoctoral fellow at the University of California's Ronald vale laboratory, began to tackle the problem Previously, the main way to image intracellular proteins was to fill in their sequences with a fluorescent domain (such as GFP) Under the general fluorescence microscope, the single protein with GFP domain is very dim, but adding too many GFP domains will make the protein too large Tanenbaum developed the suntag technology for this purpose He added multiple copies (up to 24) of peptide epitopes to the target protein, and then co expressed the protein with fluorescent antibodies that recognize the epitope The technology is published in a recent cell magazine "The beauty of this technology is that it's relatively simple," said Robert singer of Albert Einstein School of medicine Tanenbaum and his colleagues have done a lot of optimization work on this system, which is worth the effort Suntag can not only make proteins brighter, but also attract other types of proteins to peptide epitopes For example, Tanenbaum used this technique to recruit multiple transcription factors to enhance the expression of a gene.
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