Galectins have the particular capacity to interact with distinct proteins, in addition to the typical reactivity of lectins with glycans. Therefore, they can be functionally active when residing at places other than the membrane or extracellular matrix. In fact, nuclear presence of galectins-1 and -3 is solidly documented but it is an open question whether these two cases are exceptional within this lectin family. Thus, galectin-2, which shares 43% sequence identity on the protein level with galectin-1, warrants study in this respect. Based on initial immunohistochemical evidence we herein address the issue as to whether this galectin can join the category of nuclear lectins. To do so we studied different types of cell in vitro using an antibody preparation free of cross-reactivity against other tested galectins. The immunocytochemical experiments revealed that galectin-2 was present in nuclei of murine 3T3 fibroblasts and also genetically engineered human colon carcinoma cells with stable ectopic expression. Transport of galectin-2 to the nucleus could be enhanced by physical (UV light), chemical (mitomycin C, serum withdrawal) or cell biological (coculture with stromal cells) treatment modalities. As a means of further characterizing the staining profile cytochemically, a series of markers with well-defined site of residency within the nuclear compartment was tested in parallel. Importantly, no colocalization with galectins-1 and -3 and the splicing factor SC35 was detectable, the former cases also serving as inherent specificity control. In contrast, a similarity was uncovered in the case of the promyelocytic leukemia (PML) protein as marker of PML nuclear bodies. In aggregate, nuclear localization is documented for galectin-2. This attribute should thus not be considered as an exceptional finding confined to galectins-1 and -3. That even closely related family members, here galectins-1 and -2, exhibit distinct intranuclear localization patterns gives ensuing research a clear direction.