ArticleProtein science : a publication of the Protein Society2010
Fusion partners can increase the expression of recombinant interleukins via transient transfection in 2936E cells.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- Novel Enhanced Mammalian Cell Transient Expression Vector via Promoter Combination.International journal of molecular sciences · 2024Article
- Clinical Relevance of Domain-Specific Phospholipase AJournal of the American Society of Nephrology : JASN · 2020Article
- Development of a novel prostate apoptosis response-4 (Par-4) protein entity with an extended duration of action for therapeutic treatment of cancer.Protein engineering, design & selection : PEDS · 2019Article
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- Anti-tat Hutat2:Fc mediated protection against tat-induced neurotoxicity and HIV-1 replication in human monocyte-derived macrophages.Journal of neuroinflammation · 2014Article
- Over-expression of secreted proteins from mammalian cell lines.Protein science : a publication of the Protein Society · 2014Article
- An albumin leader sequence coupled with a cleavage site modification enhances the yield of recombinant C-terminal Mullerian Inhibiting Substance.Technology (Elmsford, N.Y.) · 2013Article
- Plant-produced human recombinant erythropoietic growth factors support erythroid differentiation in vitro.Stem cells and development · 2013Article
- Extending the serum half-life of G-CSF via fusion with the domain III of human serum albumin.BioMed research international · 2013Article
- High level expression of bikunin in Pichia pastoris by fusion of human serum albumin.AMB Express · 2012Article
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14 authors at 1 institution in 1 country.
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Abstract
The expression levels of five secreted target interleukins (IL-11, 15, 17B, 32, and IL23 p19 subunit) were tested with three different fusion partners in 2936E cells. When fused to the N-terminus, human serum albumin (HSA) was found to enhance the expression of both IL-17B and IL-15, cytokines which did not express at measurable levels on their own. Although the crystallizable fragment of an antibody (Fc) was also an effective fusion partner for IL-17B, Fc did not increase expression of IL-15. Fc was superior to HSA for the expression of the p19 subunit of IL-23, but no partner led to measurable levels of IL-32gamma secretion. Glutathione S-transferase (GST) did not enhance the expression of any target and suppressed the production of IL-11, a cytokine which expressed robustly both on its own and when fused to HSA or Fc. Cleavage of the fusion partner was not always possible. The use of HSA or Fc as N-terminal fusions can be an effective technique to express difficult proteins, especially for applications in which the fusion partner need not be removed.
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