ArticleMolecular biology reports2022
Bacterial over-expression of functionally active human CT2 (SLC22A16) carnitine transporter.
Article in Molecular biology reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Causal association analysis between blood metabolomes and osteopenia and therapeutic target prediction for mechanomedicine.Mechanobiology in medicine · 2025Article
- Cloning, Expression and Functional Characterization ofInternational journal of molecular sciences · 2025Article
- The Human OCTN Sub-Family: Gene and Protein Structure, Expression, and Regulation.International journal of molecular sciences · 2024Review
- Involvement of mammalian SoLute Carriers (SLC) in the traffic of polyamines.Frontiers in molecular biosciences · 2024Review
- Over-Production of the Human SLC7A10 inInternational journal of molecular sciences · 2023Article
- Heterologous (Over) Expression of Human SoLute Carrier (SLC) in Yeast: A Well-Recognized Tool for Human Transporter Function/Structure Studies.Life (Basel, Switzerland) · 2022Review
- Production of recombinant human xCT (SLC7A11) and reconstitution in proteoliposomes for functional studies.Frontiers in physiology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundEscherichia coli is a widely used tool for the over-expression of human proteins for studying structure and function. The toxicity of human proteins for E. coli often hampers the expression. This study aims to find conditions for the expression of a membrane transporter known as the carnitine transporter CT2. The knowledge on this transporter is scarce, thus obtaining the recombinant protein is very important for further studies. METHODS AND
resultsThe cDNAs coding for human CT2 (hCT2) was cloned in the pH6EX3 vector and different transformed E. coli strains were cultured in absence or in presence of glucose. hCT2 expression was obtained. The protein was purified and reconstituted into proteoliposomes in a functionally active state.
conclusionsUsing the appropriate IPTG concentration, together with the addition of glucose, hCT2 has been expressed in E. coli. The protein is active and shows capacity to transport carnitine in proteoliposomes. The results have a great interest in basic biochemistry of membrane transporters and applications to human health since hCT2 is involved in human pathology.
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