Refolding of TIMP-2 from Escherichia coli Inclusion Bodies

Williamson, Richard A. (2010) Refolding of TIMP-2 from Escherichia coli Inclusion Bodies. Methods in Molecular Biology, 622 . pp. 111-121. ISSN 1064-3745. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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The TIMP proteins contain six intramolecular disulfide bonds and form unfolded insoluble aggregates when expressed in E. coli. Eukaryotic expression systems provide the necessary post-translational modification apparatus to produce authentic TIMP but are comparatively slow and more expensive. This chapter describes the production of native TIMP-2 (both full-length and the N-terminal domain) from E. coli by in vitro refolding. The technique allows high-level intracellular expression and efficient isolation of the recombinant product without the use of fusion tags or partners. Protein purity after ion exchange and gel filtration chromatography was judged to be greater than 95% with yields of 15 mg/L from LB medium and 10 mg/L from minimal medium.

Item Type: Article
Additional information: Also published in Methods in Molecular Biology Vol. 151, 2001. See KAR ID 5317.
Uncontrolled keywords: Animals Escherichia coli/chemistry/genetics Gene Expression Humans Inclusion Bodies/chemistry/genetics Protein Folding Protein Structure, Tertiary Recombinant Proteins/chemistry/genetics/isolation & purification Tissue Inhibitor of Metalloproteinase-2/*chemistry/genetics/isolation & purification
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 09 Oct 2012 13:08
Last Modified: 21 Mar 2014 16:19
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