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首页> 外文期刊>The Kasetsart Journal >Cloning, Expression, Purification and Biological Activities of Recombinant Mouse Interleukin-2 in E. coli M15
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Cloning, Expression, Purification and Biological Activities of Recombinant Mouse Interleukin-2 in E. coli M15

机译：重组小鼠白细胞介素2在大肠杆菌M15中的克隆，表达，纯化及生物学活性

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摘要

Molecular cloning, sequencing and expression of recombinant mouse interleukin 2 (rmIL-2) were described. The interleukin-2 (IL-2) cDNA, 450 base pairs in length with repeating CAG, was amplified using specific primers. The IL-2 cDNA showed high homology at 100%, 100%, 91%, 96% and 94% with five strains of mice previously reported (GeneBank accession number AY147902.1, MMU41494, MMU41504, MMU41505 and MMU41506). The IL-2 gene was cloned into the pDrive cloning vector and consequently expressed using pQE30 expression vector which provided high expression level of the recombinant protein. The predicted rmIL-2 sequence is 161 amino acids with a molecular weight of 19 kDa. The expressed protein was then purified by Ni-NTA column under denaturing condition. Analysis of the rmIL-2 by SDS-PAGE demonstrated two bands of 19 and 38 kDa representing monomeric and dimeric forms of this protein. The biological activity in stimulating T-cell proliferation was also described and the binding signal to the receptor was easily observed by immunofluorescence.
机译：描述了重组小鼠白介素2（rmIL-2）的分子克隆，测序和表达。使用特异性引物扩增白介素2（IL-2）cDNA，其长度为450个碱基对，并带有重复的CAG。 IL-2 cDNA与先前报道的五种小鼠品系（GeneBank登录号AY147902.1，MMU41494，MMU41504，MMU41505和MMU41506）在100％，100％，91％，96％和94％处显示出高度同源性。将IL-2基因克隆到pDrive克隆载体中，并随后使用pQE30表达载体表达，该载体提供了高水平的重组蛋白表达。预测的rmIL-2序列是161个氨基酸，分子量为19 kDa。然后在变性条件下通过Ni-NTA柱纯化​​表达的蛋白。通过SDS-PAGE对rmIL-2的分析表明，有19 kDa和38 kDa的两条带代表该蛋白的单体和二聚体形式。还描述了刺激T细胞增殖的生物学活性，并且通过免疫荧光很容易观察到与受体的结合信号。

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