Figure 3. Sample experimental result from Table 1.

Human serum samples isothermally vitrified and stored for two weeks at 4 °C vs. 22 °C in sealed (constant relative humidity) vs. unsealed (uncontrolled relative humidity) conditions are compared to samples stored at −80 °C, −20 °C, 4 °C, and 22 °C without any cryoprotectant. (A) SDS-PAGE and silver staining were used to determine degradation and aggregation behaviors of total serum proteins exposed to various storage conditions. The serum proteins were prone to aggregation when stored in frozen and liquid states (lanes 1–4) or when vitrified, sealed, and stored at 4 °C (lanes 5–6). Sealing of vitrified samples and storage at 22 °C promotes both aggregation and degradation (lanes 7 and 9). Isothermally vitrified samples did not exhibit aggregation nor degradation when stored un-sealed (lanes 8 and 10). (B) Western Blot analysis was used to monitor modifications to the HAPs, albumin and haptaglobulin following storage. Albumin and haptaglobulin were unaffected by liquid and frozen storage. Sealed storage in the vitrified state resulted to modification on both proteins only when Tween was included in the matrix (lane 7).