ArticleThe open biochemistry journal2015
The Optimization of Soluble PTEN Expression in Escherichia coli.
Article in The open biochemistry journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 5 citations in OpenAlex.
- The DNA polymerase of bacteriophage YerA41 replicates its T-modified DNA in a primer-independent manner.Nucleic acids research · 2022Article
- Anti-HER2 scFv Expression in Escherichia coli SHuffleMolecular biotechnology · 2020Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As a vital tumor suppressor, PTEN (Phosphatase and tension homolog deleted on chromosome 10) is involved in inherited syndromes, and is among the most frequently inactivated tumor suppressor gene in sporadic cancers. PTEN loss-of-function widely occurs in human cancers via a variety of mechanisms, including genetic alterations and posttranslational modification. These suggest PTEN has a role of functional importance in a variety of cancers. In the present study, we constructed a prokaryotic expression vector that efficiently expresses GST-PTEN (the target protein in which PTEN is fused with glutathione S-transferase tag) in E. coli. We found that the target protein was partially soluble although major portions of the protein remained in the inclusion bodies. Furthermore, we explored the optimal induction temperature, isopropyl β-D-1-thiogalactopyranoside (IPTG) concentration and induction time in a series of experiments. Expression level analysis indicated that PTEN reached its peak level at 36(○)C for 8 h with 1.5625mM IPTG, while solubility analysis revealed the optimal induction temperature was at 20(○)C, the optimal IPTG concentration was 0.1µM and the optimal induction time was up to 8 h. Taken together, we provide an optimal induction condition for expressing soluble fusion protein of PTEN in E. coli, facilitating further analysis of PTEN's biological function in vitro.
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