Recombinant human stem cell factor (rhSCF) was produced as an inclusion body by Escherichia coli DH5 alpha grown in a 5 l fermentor. Inclusion bodies of rhSCF were purified and solubilized in urea solution, then renatured with simultaneous purification using a high performance hydrophobic interaction chromatographic (HPHIC) squat column. The refolded rhSCF had a purity of 94% and a bioactivity of 1.2 x 10(6) IU mg(-1)of rhSCF protein. The method described is fast and simple to implement.