We have recently created a fully synthetic human antibody library in the yeast Saccharomyces cerevisae.  This new antibody discovery tool yields high quality, fully human, aglycosylated monoclonal antibodies (IgG1s) in unprecedented time frames.  After isolating yeast clones from the antibody selection process, we developed a high throughout expression and purification system to produce purified antibodies, facilitating further in vitro and in vivo antibody characterization.  This method uses standard 24-square-well microtiter plates for expression and simple liquid handling robots for Protein A affinity purification.  With this system, we routinely produce 1,000 unique, fully human monoclonal antibodies per week.  To illustrate this capability, we describe the production of several hundred unique, fully human antibodies that bind to EGFR (a well studied oncology target).  We also show that these antibodies can be readily reformatted for production in mammalian cell culture (transient transfection into HEK293).  This new high throughput production process coupled to our antibody selection process, allows for unprecedented speed from target antigen to high affinity, full length, human antibodies thus greatly accelerating the early phase of the antibody drug discovery process.