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Roughly half of a cells proteins are located at or near the plasma membrane.In this restricted space the cell senses its environment, signals to itsneighbors and ex-changes cargo through exo- and endocytotic mechanisms. Ligandsbind to receptors, ions flow across channel pores, and transmitters andmetabolites are transported against con-centration gradients. Receptors, ionchannels, pumps and transporters are the molecular substrates of thesebiological processes and they constitute important targets for drug discovery.Total internal reflection fluorescence microscopy suppresses background fromcell deeper layers and provides contrast for selectively imaging dynamicprocesses near the basal membrane of live-cells. The optical sectioning oftotal internal reflection fluorescence is based on the excitation confinementof the evanescent wave generated at the glass-cell interface. How deep theexcitation light actually penetrates the sample is difficult to know, makingthe quantitative interpretation of total internal reflection fluorescence dataproblematic. Nevertheless, many applications like super-resolution microscopy,colocalization, fluorescence recovery after photobleaching, near-membranefluorescence recovery after photobleaching, uncaging orphoto-activation-switching, as well as single-particle tracking require thequantitative interpretation of evanescent-wave excited images. Here, we reviewexisting techniques for characterizing evanescent fields and we provide aroadmap for comparing total internal reflection fluorescence data acrossimages, experiments, and laboratories.

Calibrating evanescent-wave penetration depths for biological TIRF microscopy