Biotinylation of proteins and peptides has been used for many years and has become a common way to biochemically tag targets of interest (1). One advantage is the very strong binding interaction with avidin that can be used to purify biotin-tagged proteins (2,3). It can also be used as a method for conjugation of a variety of tags such as dyes, beads and other solid substrates for a variety of assays and tools (4,5).
New assays have been developed that improve elucidation of protein subcellular context, localization, and protein-protein interactions. These new cellular assays utilize biotin ligase or engineered ascorbate peroxidase (APEX) fusion proteins that are able to biotinylate nearby protein targets within specific cellular compartments. This type of biotin proximity assay can provide improved information about subcellular localization, multi-subunit components, and recruitment of unknown targets. Using CST's in house developed anti-biotin rabbit monoclonal antibody; we have developed a robust procedure for immunoaffinity enrichment followed by mass spectrometry analysis using CST’s proprietary PTMScan(R) protocols. This allows for identification of biotinylated targets and investigation of new protein interactions. This assay provides rich data for these types of biotin proximity assays such as the APEX (6,7) engineered cell system and other related methods.
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