Recombinant plasmid PBV-SCF was transformed into the DH5α and a high expressing germ that could produce about 20 percent SCF product of all the bacterial protein was selected. The SCF product is expressed in form of inclusion body. By liquid chromatography, recombinated human SCF(rhSCF) was obtained with the purity of 90 percent. The sequence of the N-terminal amino acid and the isoelectric point of the rhSCF were analyzed. They are same as the natural SCF. The specific activity of the rhSCF is 6.6×10⁵ U/mg.Morcover, it can coordinate with the granule-macrophage stimulating facet (GM-SCF) to stimulate proliferate of the CFU-GM from the human bone marrow. The acquiration of the rhSCF is important to both the labotory research and the clinical therapy.