DTT is frequently used to reduce the disulfide bonds of proteins and, more generally, to prevent "intramolecular" and "intermolecular" disulfide bonds from forming between cysteine residues of proteins. However, even DTT cannot reduce buried (solvent-inaccessible) disulfide bonds, so reduction of disulfide bonds is sometimes carried out under denaturing conditions (e.g., at high temperatures, or in the presence of a strong denaturant such as 6 M guanidinium chloride, 8 M urea, or 1% sodium dodecylsulfate). DTT is oftentimes used along with sodium dodecylsulfate in SDS-PAGE to further denature proteins by reducing their disulfide bonds to allow for better separation of proteins during electrophoresis. Because of the ability to reduce disulfide bonds, DTT can be used to denature CD38 on red blood cells. DTT will also denature antigens in the Kell, Lutheran, Dombrock, Cromer, Cartwright, LW and Knops blood group systems. Conversely, the solvent exposure of different disulfide bonds can be assayed by their rate of reduction in the presence of DTT.