A wide array of clinically relevant aspects are associated with the function or malfunction of T-cells: Autoimmune diseases, control of viral or bacterial pathogens, development of cancer or graft versus host responses.
The Strep-tag is a short peptide sequence that displays moderate binding affinity for the biotin-binding site of a mutated streptavidin molecule, called Strep-Tactin.
For the Streptamer technology, the Strep-Tactin molecules are multimerized and form the "backbone", thus creating a platform for binding to strep-tagged proteins.
Incubation of MHC-Strep-tag fusion proteins with the Strep-Tactin backbone results in the formation of a MHC-multimer, which is capable for antigen-specific staining of T cells.
[2][3] Therefore, a MHC multimer based on the interaction of Strep-tag with Strep-Tactin is easily disrupted in the presence of relatively low concentrations of d-biotin.