title: Expression, renaturation and simultaneous purification of recombinant human stem cell factor in Escherichia coli.
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.
authors.affiliation: Institute of Modern Separation Science, Key Lab of Modern Separation Science in Shaanxi Province, Northwest University, Xi'an 710069, China.
authors.forename: Wang
authors.initials: W
authors.lastname: Lili
authors.forename: Wang
authors.initials: W
authors.lastname: Chaozhan
authors.forename: Geng
authors.initials: G
authors.lastname: Xindu
mesh_terms: D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology; D006801:Humans; D011489:Protein Denaturation; D015202:Protein Engineering / Q000379:methods*; D017510:Protein Folding; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D019089:Stem Cell Factor / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins; D019089:Stem Cell Factor