Affitin

They are structurally derived from the DNA binding protein Sac7d, found in Sulfolobus acidocaldarius, a microorganism belonging to the archaeal domain.

Scientists have been able to purify human immunoglobulin G (hIgG), bacterial PulD protein, and chicken egg lysozyme using Affitin columns with a high degree of purity.

[5] Due to their small size and high solubility, they can be easily produced in large amounts using bacterial expression systems.

[3] Due to their small size and high solubility, they can easily be produced in large amounts using bacterial expression systems.

This was done by grafting the binding surface of D1Sac7d onto Sso7d, which is more stable, and by introducing point mutations previously identified as stabilizing for WT Sso7d.