[Expression in E. coli and chemotactic activity analyzing of recombinant CC-chemokine RANTES].
OBJECTIVE
To further understand the structure and function of RANTES and provide basis for research for application.


METHODS
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.


RESULTS
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.


CONCLUSIONS
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.
Sun
R H
RH
Laboratory of Molecular Immunology, Health Science Center, Peking University, Beijing 100083, China.
Wang
Y
Y
Zhong
Y C
YC
Ma
D L
DL
D000818:Animals; D002478:Cells, Cultured; D018946:Chemokine CCL5 / Q000096:biosynthesis* / Q000235:genetics / Q000494:pharmacology*; D002633:Chemotaxis / Q000187:drug effects*; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000494:pharmacology
D018946:Chemokine CCL5; D011994:Recombinant Proteins