Traditionally, affinity reagents such as antibodies are generated using animals. Unfortunately this process is time-consuming and costly, sometimes taking months to isolate binding reagents. In addition, the animals used are not a renewable source of material and are expensive to maintain. In fact, many antibodies generated via animal methods are promiscuous, binding to more than one target. A different strategy is to isolate binding reagents is to use phage-display. In this case, the process is performed entirely in vitro, and the reagents isolated are recombinant (thus renewable). Furthermore, the process itself is much faster than traditional methods, taking only a few weeks. Researchers at UIC have streamlined this process, using phage-display to isolate binding reagents and subsequently using affinity maturation to increase affinity of the reagent into the low nanomolar range. The reagent has been successfully used in ELISA and pulldown. Nelson Grihalde grihalde@otm.uic.edu 312-996-4129
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