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Updated: Aug 7, 2026
Recombinant Protein Expression for Structural Biology in HEK 293F Suspension Cells: A Novel and Accessible Approach
Published on: October 16, 2014
Expression, renaturation and simultaneous purification of recombinant human stem cell factor in Escherichia coli
Wang Lili1, Wang Chaozhan, Geng Xindu
1Institute of Modern Separation Science, Key Lab of Modern Separation Science in Shaanxi Province, Northwest University, Xi'an 710069, China.
Abstract:
Recombinant human stem cell factor (rhSCF) was produced as an inclusion body by Escherichia coli DH5alpha 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.
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