It is similar, in principle, to the JP 1302 dihydrochloride differential extraction procedure first described by Gill et al. and modified by forensic laboratories for casework samples that contain sperm cells. The differential procedure uses repeated washes to remove epithelial and sperm cells from evidentiary swabs, and then additional washes to remove non-sperm DNA from the pelleted sperm cells. Those washes are often discarded, along with any DNA that may be in them. The swab re-suspension method presented in this work sequentially uses the extraction buffer as the wash to dislodge cells that are caught in, or adhered to, the cotton fibers of the swab. As no buffer is discarded, DNA is not lost. The swab re-suspension method also proved to be effective with samples that had been stored up to six months at 4��C. Under these conditions the DNA should not have been significantly degraded and testing supported that the swab re-suspension method did not cause additional DNA damage to aged samples while increasing yield. The proteasome, a multisubunit proteolytic complex involved in degradation of ubiquitinated proteins, plays a crucial role in assuring completion of meiosis and formation of a developmentally- competent embryo. Early in maturation, completion of meiosis I requires inactivation of maturation promoting factor through a process mediated by proteasomal cleavage of ubiquitinated cyclin B1. Other aspects of oocyte function during maturation are also under control of the proteasome. In mice, for example, the proteasome is required for the initiation and maintenance of translation of mRNA for the RNA IT 901 binding protein SLBP. Abundance of another protein involved in RNA processing, CPEB, is under negative regulation by proteasomes in Xenopus. In addition, cumulus cells encasing the oocyte require proteasomal activity for optimal function as indicated by negative effects of the proteasomal inhibitor MG132 on progesterone production and expression of genes involved in expansion of the extracellular matrix. This peptide aldehyde, N- leucinylleucinylleucinal, functions as a substrate analog and transition-state inhibitor of the chymotrypsin-like activity of the proteasome. Late in the process of oocyte maturation, the proteasome may contribute to a reduction in the functional properties of the oocyte. Treatment with MG132 reduced the effect of in vitro aging on oocyte competence in the mouse. Furthermore, treatment of oocytes with MG132 late in maturation increased abundance of specific transcripts and improved developmental competence of parthenogenetically-activated oocytes in the pig. If inhibition of the ubiquitin-proteasome pathway late in maturation improves oocyte competence, it may be possible to improve the success rate of assisted reproductive technologies that utilize in vitro matured oocytes.