TY - JOUR
T1 - Production of recombinant serpins in Escherichia coli
AU - Bird, Phillip I.
AU - Pak, Stephen C.
AU - Worrall, D. Margaret
AU - Bottomley, Stephen P.
N1 - Funding Information:
We apologize to colleagues whose work we have not cited due to space limitations. P.I.B. and S.P.B. are supported by the Australian Research Council, and the National Health and Medical Research Council (Australia).
PY - 2004/2
Y1 - 2004/2
N2 - 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.
AB - 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.
KW - Escherichia coli
KW - Expression systems
KW - Recombinant protein
KW - Serpin
UR - https://www.scopus.com/pages/publications/0347753711
U2 - 10.1016/S1046-2023(03)00208-1
DO - 10.1016/S1046-2023(03)00208-1
M3 - Article
C2 - 14698629
AN - SCOPUS:0347753711
SN - 1046-2023
VL - 32
SP - 169
EP - 176
JO - Methods
JF - Methods
IS - 2
ER -