Expression, renaturation and simultaneous purification of recombinant human stem cell factor in Escherichia coli

摘要

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.