The combination of organic thin film transistors and biological molecules could open new approaches for the detection and measurement of properties of biological entities. To generate specific addressable binding sites on such substrates, it is necessary to determine how single biological molecules, capable of serving as such binding sites behave upon attachment to semiconductor surfaces. Here, we use a combination of high-resolution atomic force microscopy topographical imaging and single molecule force spectroscopy (TREC), to study the functionality of antibiotin antibodies upon adsorption on pentacene islands, using biotin-functionalized, magnetically coated AFM tips. The antibodies could be stably adsorbed on the pentacene, preserving their functionality of recognizing biotin over the whole observation time of more than one hour. We have resolved individual antigen binding sites on single antibodies for the first time. This highlights the resolution capacity of the technique.