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Background It has been widely observed that infants and young children can reossify large calvarial defects when they are younger than 2 years of age; afterwards, they lose this regenerative potential. Previous studies have implicated that the dura mater serves as a key regulator of calvarial regeneration. However, the molecular mechanism of caivarial reossification remains elusive.Methods In order to identify the proteins that may participate in this process, we performed a proteome-wide comparison of the protein expression levels of immature and mature dura using 2D electrophoresis and MALDI-TOF mass spectrometry. The Westem blotting was used to verify the results of the 2D electrophoresis/MALDI-TOF mass spectrometry.Results Eleven proteins were found to express with significant differences in the immature and the mature dura. Among them, the emergence of vimentin, tropomyosin,β-actin and y-actin were further confirmed by the Western blotting analysis.Conclusion The proteins and proteomic profiles provide a better understanding of the molecular mechanism of calvarial regeneration.