title: Production of recombinant serpins in Escherichia coli.
abstract: Expression systems based on Escherichia coli offer fast, cheap, and convenient means for the production of recombinant serpins. Over 30 active serpins from prokaryotic and eukaryotic organisms have been produced in this way, using a variety of vectors, promoters, fusion partners, and host strains. Serpins forming insoluble inclusion bodies in E. coli can generally be solubilized and refolded. Here, we outline the general approaches and procedures to be considered when contemplating the use of E. coli for recombinant serpin production.
authors.affiliation: Department of Biochemistry and Molecular Biology, Monash University 3800, Australia. phil.bird@med.monash.edu.au
authors.forename: Phillip I
authors.initials: PI
authors.lastname: Bird
authors.forename: Stephen C
authors.initials: SC
authors.lastname: Pak
authors.forename: D Margaret
authors.initials: DM
authors.lastname: Worrall
authors.forename: Stephen P
authors.initials: SP
authors.lastname: Bottomley
mesh_terms: D001433:Bacteriolysis; D010450:Endopeptidases / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D015870:Gene Expression; D005822:Genetic Vectors / Q000235:genetics; D011489:Protein Denaturation; D017510:Protein Folding; D020871:RNA Stability; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification; D015843:Serpins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D012995:Solubility
chemical_list: D011994:Recombinant Proteins; D015843:Serpins; D010450:Endopeptidases