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期刊论文
Expression, refolding, and characterization of a novel recombinant dual human stem cell factor
Protein Expression and PuriWcation 43(2005)126-132，-0001，（）：
A novel recombinant dual human stem cell factor (rdhSCF) gene which consisted of a full-length hSCF(1-165 aa) cDNA and atruncated hSCF (1-145 aa) cDNA, linked by a peptide (GGGGSGGGGSGG) coding region, was constructed and cloned into Escherichia coli expression vector pET-22b. The rdhSCF was expressed at high level in E. coli BL21(DE3) and existed mainly as inclusion bodies. The inclusion bodies were solubilized in urea and refolded by ion-exchange chromatography. After renaturation, the purity of the yielded rdhSCF was up to 90%. Cell proliferation assay showed that the speciWc activity of the rdhSCF was 2.86
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