Proteomic profiling attempts to elucidate not only protein repertoire, but the structure and function of proteins. Post genome sequencing, scientists are now focusing on studying what proteins are decoded from the genome. The first step in many proteomic studies is the extraction and isolation of proteins from the sample of interest. The success of a protein assay is often dependent on quality and method of this first step. A common method for extraction of proteins from animal tissues is mechanical homogenization. While many tissue types can be robust and require significant mechanical force to dissociate them and access their cellular components, tissues like brain and liver are quite soft and require a gentler homogenization approach in order to ensure adequate sample extraction without sacrificing the molecular integrity of the proteins of interest. This is especially important for proteomic studies aiming to analyze tertiary structure, enzyme activity or post-translational modifications.
The Omni Bead Ruptor Elite is a bead mill homogenizer capable of processing up to 24 tissue samples per cycle and has been used in a number of studies for the isolation of proteins from soft tissues. Bead mills function by the high speed shaking of a sample in a sealed tube in the presence of beads. The beads impact the sample with sufficient force to dissociate both the tissues and the cells.
In this study, we demonstrate protein extraction from soft tissues through bead milling using the Omni Bead Ruptor Elite bead mill homogenizer. Efficiency and analyte integrity were evaluated.
Table 2: Protein concentration of samples