Introduction: There is evidence suggesting that recombinant preparations of the capsid protein of Dengue 2 virus (C2) induce protective cellular immune responses in mice and can significantly reduce viral loads after challenge in monkeys. Materials and Methods: In the present work we expressed, purified and antigenically characterized preparations of recombinant capsid proteins from Dengue virus serotypes 1, 3 and 4, which will later be employed in preclinical studies. Results: We managed to implement fermentation processes for each protein with expression levels ≥15%, and a simple, common purification process based on a single cation exchange chromatographic step that yields purities higher than 90%. The purified proteins were recognized by the anti-capsid monoclonal antibody 8H8 and by homologous hyperimmune ascitic fluids. An in vitro aggregation assay were performed in the presence of the ODN 39M, which evidenced that under the studied conditions, protein C2 aggregates less efficiently than capsid proteins from the remaining serotypes. Conclusions: The study and characterization of these proteins will contribute to a deeper understanding of their contribution to the immunogenicity and protective effect of current vaccine candidates under development by our group, and may guide the design of future candidates.