We found that the mean and the CV of this value were significantly lower in the Isoetharine Mesylate radial maps respect to the Cartesian ones. We can confirm this result by observing the maps, where an even distribution of the background in radial maps can be appreciated. We can ascribe this result to the identical conditions of staining/ destaining of radial maps. In fact, owing to the possibility to load up to six strips on the same radial gel, not only the migrations of proteins, but also the grayscales of the background are identical among the maps of the same gel. This is an important result, since in a proteomic study the accuracy in quantification for differentially expressed proteins will increase in absence of uneven backgrounds. Regarding the number of detected spots, results are much more complex to assess, since several variables come into play. The first variable regards the gel size. In this study, the Cartesian gels have an area that is approximately twice that of the radial gel. Radial and Cartesian maps were obtained using respectively 7 and 17 cm long strips. Despite the radial maps ����started���� with a disadvantage in terms of resolution in the first dimension, we observed that spots separation in the final map showed equivalent quality in the two sets, as can be appreciated in the example of Figure 2 showing the separation of different isoforms of triosephosphate isomerase. Furthermore, in some instances, the migration of spots in the divergent radial field, despite of the reduced resolution related to the use of a shorter strip, was able to increase the resolution obtained in the Cartesian set, as can be observed in Figure 3 for what concerning the myoglobin protein spots. These cases were observed in the lower, fanning-out area of the map, where the effect of radial migration should theoretically lead to an accentuated spot resolution, directly proportional to the migration distance. The second variable regards the protein loading. To make a fair comparison, we decided to load a higher amount of protein in the larger gel set, i.e. the Cartesian one. In fact, an advantage of using large gels, as well as the possibility to increase resolution, lies in the opportunity of increasing the loading of proteins thus bringing many more proteins above the detection limit and consequently increasing the number of detected spots. On the other hand, Hexamethonium Bromide overloading would result in the risk of obscuring some zones, leading poor resolution in these zones. In this study, the absence of an overloading can be visually appreciated by looking at the Figure 1. Thanks to the increased loading of total protein in the Cartesian set, we observed the appearance of some spots, that were completely absent in the radial set. The third variable concerns the presence of a gradient of porosity on the 2nd dimension gel, which, for technical reasons, can be done only in Cartesian gels. Porosity gradients are useful because they give the highest possible resolution along the y-axis of the 2-DE map. However, in the radial maps we didn��t observe any problem of resolution along the y-axis, such us vertical streaking made of stacked spots, despite the shorter run length and the lacking of the porosity gradient. We believe that this result could be due to an interesting side effect of the radial electric field geometry. In fact, in association with the distancing of spots during the electrophoretic migration, we observed also a flattening of the spots. Starting from these experimental observations, we made a theoretical model to further validate these findings. We are currently carrying out further investigations to develop a more detailed mathematical model capable for representing the theoretical behavior of spot during polar electrophoresis, to find the ideal lengths of the radial gel radii and consequently to optimize the entire process.