Clean and folded: Production of active, high quality recombinant human interferon-λ1

Shaldzhyan, Aram A.; Zabrodskaya, Yana A.; Yolshin, Nikita; Kudling, Tatiana V.; Lozhkov, Alexey A.; Plotnikova, Marina; Ramsay, Edward; Taraskin, Aleksandr S.; Nekrasov, Peter A.; Grudinin, Mikhail; Васин, А. В.

doi:10.1016/j.procbio.2021.08.029

Cited by 2 publications

(1 citation statement)

References 26 publications

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“…The cleaved IL-29 was further purified by IMAC chromatography with step yield of 62% and 99% purity. The yield in current study was higher (98 mg/l) in comparison to other studies who have reported as 60 mg/l (Li & He 2006 ), 65 mg/l (Xie et al 2007 ), and 70 mg/l (Shaldzhyan et al 2021 ). The antiproliferation activity of rhIL-29 in HepG2, HCT-116, and MCF-7 cell lines was consistent with previous reports (Fujie et al 2011 ; Balabanov et al 2019 ; Akram et al 2023 ; Rahman et al 2023 ), indicating that our research is successful in producing functional IL-29.…”

Section: Discussioncontrasting

confidence: 84%

Enhanced soluble expression of active recombinant human interleukin-29 using champion pET SUMO system

et al. 2023

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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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