Desthiobiotinylation and Pull-Down Kit (Magnetic Beads)

Desthiiobiotin is a monocyclic sulfur-free biotin analogue with nearly the same specificity as biotin when bound to streptavidin, but with relatively low affinity, with dissociation constants (Kd) of 10^-11 M and 10^-15, respectively M. Due to this property, the use of biotin eluents enables the competitive displacement of thiobiotylin-bound desulfurin-bound biotin markers under mild conditions. This release characteristic of dethiobiotin has many advantages, on the one hand, it helps to reduce the co-purification of endogenous biotin molecules, and on the other hand, it does not require harsh separation conditions to dissociate the complex, thus effectively avoiding the destruction of intermolecular binding such as target proteins. Therefore, when native or recombinant proteins are not suitable for expression of fusion tags, or when the target protein needs to be isolated in a condition as close to its native state as possible, desthiobiotin labeling and pull-down technology are undoubtedly the ideal choice.

The Desthiobiotinylation and Pull-Down Kit (Magnetic Beads) is a kit for studying protein-protein interactions and related biomolecule-to-molecule interactions. The principle is to dethiobiotin label the protein, antibody, or other active biomolecules of interest, and then bind to streptavidin magnetic beads to capture the target protein or other binding molecules that interact with it, and to efficiently elute the bound target protein or other binding molecule under mild conditions.

This kit provides desthiobiotin labeling reagents as well as purification of desthiobiotin labeled protein components. Purification components include desalting columns, streptavidin magnetic beads, and reagents such as biotin eluent. Kits can be used to study the interaction of a known protein with a protein of interest to be discovered, or between a known protein and DNA, RNA, or other molecules, as well as to confirm known protein-to-protein interactions with biomolecules such as proteins. This is especially true when native or recombinant proteins are not suitable for expression of fusion tags or where the protein of interest needs to be isolated under native conditions.