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• W2396522900 endingPage "184" @default.
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• W2396522900 abstract "The binding between biotin and streptavidin or avidin is one of the strongest known non-covalent biological interactions. The (strept)avidin-biotin interaction has been widely used for decades in biological research and biotechnology. Therefore labeling of purified proteins by biotin is a powerful way to achieve protein capture, immobilization, and functionalization, as well as multimerizing or bridging molecules. Chemical biotinylation often generates heterogeneous products, which may have impaired function. Enzymatic biotinylation with E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide, giving a homogeneous product with high yield. AviTag can conveniently be added genetically at the N-terminus, C-terminus, or in exposed loops of a target protein. We describe here procedures for AviTag insertion by inverse PCR, purification of BirA fused to glutathione-S-transferase (GST-BirA) from E. coli, BirA biotinylation of purified protein, and gel-shift analysis by SDS-PAGE to quantify the extent of biotinylation." @default.
• W2396522900 created "2016-06-24" @default.
• W2396522900 creator A5012100815 @default.
• W2396522900 creator A5024914822 @default.
• W2396522900 date "2014-12-08" @default.
• W2396522900 modified "2023-10-16" @default.
• W2396522900 title "Site-Specific Biotinylation of Purified Proteins Using BirA" @default.
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• W2396522900 doi "https://doi.org/10.1007/978-1-4939-2272-7_12" @default.
• W2396522900 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4304673" @default.
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• W2396522900 hasPublicationYear "2014" @default.
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