To obtain recombinant sonic hedgehog N-terminal protein (Shh-N)and study its biological activity，the cDNA encoding the functional rat Shh-N was isolated using PCR. The expression plasmid was constructed by inserting Shh-N cDNA into plasmid pET28a (+) and transformed into E.coli. Then an expression strain was selected. SDS-PAGE and Western blotting analysis revealed that the rat Shh-N protein was highly expressed in the form of a large quantity of soluble protein and a small amount of inclusion body being induced by the IPTG. After Ni-NTA resin affinity chromatography, the purity of the final Shh-N protein was more than 85%. Purified protein being added to neural progenitor cells during developmental stages could induce the phenotype of tyrosine hydroxylase-immunopositive neurons. Based on this study, sufficient donor cells would be available to treat Parkinson′s disease in clinical therapy via inducing different kinds of stem cells from human being into dopaminergic neurons.