what are biotinylated protein ?
In biochemistry, biotinylation is the process of covalently attaching biotin to a protein. Biotinylation is rapid, specific and is unlikely to perturb the natural function of the molecule due to the small size of biotin (MW = 244.31 g/mol). Biotin binds to streptavidin and avidin with an extremely high affinity, fast on-rate, and high specificity, and these interactions are exploited in many areas of biotechnology to isolate biotinylated molecules of interest.
Applications
Purification:The biotin tag can be used in affinity chromatography together with a column that has avidin (or streptavidin or Neutravidin) bound to it, which is the natural ligand for biotin. Detection:This tag can also be used in detection of the protein via anti-biotin antibodies or avidin/streptavidin-tagged detection strategies such as enzyme reporters or fluorescent probes. This can be useful in localization by fluorescent or electron microscopy,ELISA assays, ELISPOT assays, western blots and other immunoanalytical methods. Detection with monovalent streptavidin can avoid clustering or aggregation of the biotinylated target.

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