Expression in E. coli and chemotactic activity analyzing of recombinant CC-chemokine RANTES

To further understand the structure and function of RANTES and provide basis for research for application.PCR product corresponding to region encoding mature RANTES protein was cloned into E. coli expression vector; purified recombinant protein was obtained by heparin affinity chromatography and its chemotactic activity was determined by Boyden chamber.The recombinant RANTES was expressed in E. coli with high efficiency. Purified protein showed chemotactic activity to peripheral blood lymphocytes, U937 cells, and CCR4 stable-transfected HEK293 cells.The purified recombinant protein exerted chemotactic activity on PBL and cultured cell lines, and we have established a experimental system for further study of structure and function of RANTES.PubMed02123-62