Abstract: his work aimed to construct a prokaryotic expression for mouse gene CCL2, express and purify recombinant CCL2 protein, and detect the adhesion of leukemia cells. The mouse gene CCL2 was amplified by PCR and cloned into the prokaryotic expression vector pGEX-4T-1 by ligation-independent cloning. The recombinant plasmid pGEX-4T-CCL2 was transformed into Escherichia coli BL21（DE3）and the recombinant protein was purified by affinity chromatography. The purified protein was identified by SDS-PAGE and Western Blot. Finally, the effect of CCL2 on C1498 cell adhesion and migration was detected. Results showed that the recombinant vector pGEX-4T-CCL2 was successfully constructed, and GST-CCL2 was successfully induced by 0.1 mmol/L IPTG at 20 ℃ for 6 h; recombinant protein with biological function was prepared, and CCl2 could promote leukemia cell adhesion and migration. This work would provide a foundation for further study of CCL2 in leukemia.

Key words: CC chemokine ligand 2(CCL2), protein purification, leukemia, cell adhesion, cell migration