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Background  With the rapid advancement of cell biology, the evaluation of a given protein’s synthesis and release in cells becomes critical. However, up to now there has been no technique available to morphologically visualize and measure a newly synthesized protein in cells, nor can we measure the protein’s release from the cells.    Results  In this study, we developed a set of assays combining pulse chase amino acid substitution, non-radioactive labeling, and immunofluorescence co-localization to visualize newly synthesized proteins in individual cells and then to detect their release using modified ELISA. We demonstrated the synthesis and release of Bcl-2, MMP-9, and immunoglobulin G (IgG) in a human trophoblast cell line, of which the last finding has not been reported previously.    Conclusions  This new technique offers a powerful tool to evaluate the dynamics of the synthesis and release of target proteins in individual cultured cells with wide applications in genetic and protein analysis.    Electronic supplementary material  The online version of this article (doi:10.1186/s12860-014-0045-1) contains supplementary material, which is available to authorized users.

A morphologic and semi-quantitative technique to analyze synthesis and release of specific proteins in cells