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

被引：5
作者：
Munir, Ayesha [1 ]
Ahmed, Nadeem [1 ]
Akram, Muhammad [1 ]
Fujimura, Nao Akusa [1 ]
Tahir, Saad [1 ]
Malik, Kausar [1 ]
机构：
[1] Univ Punjab, Ctr Excellence Mol Biol, Lahore, Pakistan
来源：
BIOTECHNOLOGY LETTERS | 2023年 / 45卷 / 08期
关键词：
Interferon-lambda; 1; Interleukin-29; Recombinant protein; pET SUMO; Rosetta-gami 2(DE3); IMAC purification; INTERFERON-LAMBDA; ESCHERICHIA-COLI; IFN-LAMBDA; FUSION TECHNOLOGY; III INTERFERON; IN-VIVO; PURIFICATION; PROTEIN; IL-29; SOLUBILITY;
D O I：
10.1007/s10529-023-03402-x
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
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 (TM) 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 (TM) 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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页码：1001 / 1011
页数：11
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