Both industrial and research scale protein purification require the development of superior procedures for increasing recovery yields. This places an emphasis on maintaining proteins in fully reduced states to solubilize inclusion bodies, while increasing the recovery of active proteins through improved protein-folding technologies. These concerns have a common theme: the ability to maintain the disulfide bonds in the protein in a sufficiently reduced state so as to facilitate correct folding while simultaneously avoiding protein aggregate formation. Dithiothreitol (DTT) is still…