Using Avi-tag Biotinylated Proteins to Determine Protein Interaction Kinetics and Affinity with Surface Plasmon Resonance

Biotinylated proteins can be powerful tools for assessing protein interactions and screening antibody or small molecule libraries for potential therapeutics. R&D Systems™ Avi-tag biotinylated proteins contain an extra 15 amino acid sequence, the Avi-tag, fused to the N- or the C-terminus of the protein, which is enzymatically biotinylated by the E. coli BirA biotin ligase on a single lysine residue. In contrast to amine biotinylation, Avi-tag biotinylation is highly specific, consistent, and generates a homogeneous product with uniform protein orientation when bound to a streptavidin-coated surface.

Read this application note to learn how R&D Systems Avi-tag biotinylated proteins can be used as an alternative to chemical or amine biotinylated proteins to determine protein interaction kinetics and affinity using the Biacore surface plasmon resonance system.