论文
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| 第一作者所在部门: | |
| 中文论文题目: | Expression, purification, and functional characterization of recombinant human interleukin-7. |
| 英文论文题目: | Expression, purification, and functional characterization of recombinant human interleukin-7. |
| 作者: | Luo Y, Kong X, Xu A, Jin S, Wu D |
| 论文出处: | |
| 刊物名称: | Protein Expr Purif. |
| 年: | 2009-1-1 |
| 卷: | 63 |
| 期: | 1 |
| 页: | 1-4 |
| 联系作者: | Wu D. |
| 收录类别: | |
| 影响因子: | 1.94 |
| 摘要: | Human interleukin-7 (IL-7) is a member of the interleukin family. Numerous studies have demonstrated IL-7's effect on B- and T-cell development as well as its potential in various clinical applications. Previously, a study reported that IL-7 could be purified from inclusion bodies using a prokaryotic system, however, the required refolding step limits the recovery rate. This study was designed to produce a bioactive recombinant human IL-7 (rhIL-7) in a eukaryotic expression system in order to obtain higher yields of the protein with simpler purification steps. We cloned human IL-7 cDNA and successfully expressed active recombinant protein in yeast using the Pichia pastoris expression system. A simple purification strategy was established to purify the rhIL-7 from the fermentation supernatant, yielding 35 mg/L at 95% purity by the use of a common SP Sepharose FF cation-exchange chromatography. Functional analysis of the purified rhIL-7 by the pre-B cell MTT (3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazolium bromide) proliferation assay demonstrated a specific activity comparable to commercial sources. These results suggest that purification of rhIL-7 from yeast provides a sound strategy for large-scale production of the rhIL-7 for clinical applications as well as basic researches. |
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