The two-dimensional gel electrophoresis-based technique is commonly used in protein analysis and identification. Though this technique is powerful, mature and sensitive there still remain some questions regarding its ability to characterize different types of proteomes. Different calmodulin isoforms play different roles in response to varying external stimulant signals during plant development, but their advanced structures are too small to be distinguished and purified at protein level. In this paper, a two-dimensional gel electrophoresis-based technology was investigated to identify different calmodulin isoforms, which will lay a foundation for subsequent researches.
