Pichia pastoris is a popular yeast strain for heterologous protein expression. The yeast cells can be transformed with exogenous DNA and programmed to express proteins from different sources. For instance, Pichia pastoris has been used to express human proteins for medicinal purposes. One advantage of the P. pastoris system is that the proteins can be programmed to be secreted out of the cell and into the liquid medium where they grow. This should make purification of the engineered protein easier. Unfortunately, two problems often result. First, the protein often gets caught within the cell and never arrives in the liquid medium. A second problem is if the protein does get secreted outside the cell, it is hard to purify. We have constructed a new plasmid, which allows the heterologous protein to be expressed as a fusion with the maltose binding protein (MBP). We hypothesize that the MBP fusion partner will improve the ability of the cell to secrete a heterologous protein and make its purification much easier. We are currently assessing our data to see if MBP is an effective secretable fusion partner using SDS PAGE and western analysis. If the protein is successfully secreted and purified, it assures us that P. pastoris is more useful in laboratory work and the advancement of research