Production of recombinant serpins in Escherichia coli.
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.
Bird
Phillip I
PI
Department of Biochemistry and Molecular Biology, Monash University 3800, Australia. phil.bird@med.monash.edu.au
Pak
Stephen C
SC
Worrall
D Margaret
DM
Bottomley
Stephen P
SP
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
D011994:Recombinant Proteins; D015843:Serpins; D010450:Endopeptidases