ArticleBiotechnology letters2023
Enhanced soluble expression of active recombinant human interleukin-29 using champion pET SUMO system.
Article in Biotechnology letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Digital Microfluidics-Driven Cell-Free Protein Synthesis Platform Reveals Expression and Stability Determinants for Phytoglobins and Cysteine-to-Alanine Substituted Variants.Antioxidants (Basel, Switzerland) · 2025Article
- Development of chimeric multivalent proteins for serological diagnosis of African animal trypanosomosis.Parasitology · 2025Article
- Application of SUMO fusion technology for the enhancement of stability and activity of lysophospholipase from Pyrococcus abyssi.World journal of microbiology & biotechnology · 2024Article
- Small ubiquitin-like modifier-tag and modified protein purification significantly increase the quality and quantity of recombinant African swine fever virus p30 protein.Veterinary world · 2024Article
- Essential factors, advanced strategies, challenges, and approaches involved for efficient expression of recombinant proteins in Escherichia coli.Archives of microbiology · 2024Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
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Abstract
Current research focuses on the soluble and high-level expression of biologically active recombinant human IL-29 protein in Escherichia coli. The codon-optimized IL-29 gene was cloned into the Champion™ pET SUMO expression system downstream of the SUMO tag under the influence of the T7 lac promoter. The expression of SUMO-fused IL-29 protein was compared in E. coli Rosetta 2(DE3), Rosetta 2(DE3) pLysS, and Rosetta-gami 2(DE3). The release of the SUMO fusion partner resulted in approximately 98 mg of native rhIL-29 protein with a purity of 99% from 1 l of fermentation culture. Purified rhIL-29 was found to be biologically active, as evaluated by its anti-proliferation assay. It was found that Champion™ pET SUMO expression system can be used to obtained high yield of biologically active soluble recombinant human protein compared to other expression vector.
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