How do I dissociate or break the streptavidin-biotin interaction?

Some information below is borrowed from some other vendors, as this is a commonly asked question. If you do need to remove the captured antigen from the SA beads, you might also consider using a cleavable biotinylation reagent. Without a cleavable reagent, below are some of the common strategies used, which are harsh, yet necessary, to break the very strong bond.

The streptavidin-biotin interaction is the strongest known non-covalent, biological interaction between a protein and molecule. The bond formation between biotin and avidin is very rapid and, once formed, is unaffected by wide extremes of pH, temperature, organic solvents and other denaturing agents. Unless derivative forms of biotin or modified streptavidin have been adopted for your experiment, requiring a specific form and normally gentle way to dissociate biotin from streptavidin, often very harsh methods are required to dissociate the biotin from streptavidin which will denature the streptavidin. A couple of these methods are discussed below. For biotinylated proteins, boil the beads in 0.1% SDS or SDS-PHAGE buffer for 3 min.