Antibodies are large, Y-shaped proteins produced by the immune system to combat foreign invaders such as virus particles and bacteria. They accomplish this feat by binding to a specific epitope on a particular antigen, and do so with great affinity. The concept of using antibodies as a therapy to treat illness dates back to the late 19th century with the pioneering work of Emil von Behring and Erich Wernicke on the development of an antitoxin against diphtheria. As might be expected, great strides have been made in the field of medicine and antibody therapeutics since these early experiments. A major breakthrough in the field occurred relatively recently in 1975 with the advent of hybridoma technology. In particular, this marked the first time in which almost unlimited quantities of extremely pure affinity reagents could be generated in the form of monoclonal antibodies. Even so, the successful development of such monoclonal therapies has only truly blossomed in recent years. Today, twenty-four FDA-approved monoclonals are currently on the market and more than 150 new monoclonals are entering clinical trials - this represents close to 50% of all drugs entering clinical trials. Altogether, these novel therapies show great promise in providing a new means to treat a number of different human illnesses and comprise more than a $30 billion market in 2010 alone. Nevertheless, there still remains several major difficulties in their successful formulation; the top two challenges being antibody stability and the propensity for aggregation. Both of these pitfalls render the protein unusable as a therapy. As such, the focus of my East Asia and Pacific Summer Institutes (EAPSI) research has been to further develop the tools necessary to create and improve novel antibody therapies for the treatment of human disease. To this end, I have successfully cloned the appropriate antibody sequences into phage and confirmed this by DNA sequencing. These antibody molecules were then tested against their cognate antigens and binding specificity was also confirmed. Most importantly, a panel of 9 mutant variants was generated and preliminarily tested for antigen binding and stability. From these early experiments one variant in particular demonstrated a considerable improvement in stability as compared to the parental protein. This variant holds great promise as a potential therapeutic candidate and validates the scientific approach taken to obtain such a clone. While further testing is required to characterize its detailed properties, it certainly acts as a great starting template for further protein engineering studies.