Expression, purification and bioactivity identification of recombinant SCR15-18 domain of human soluble complement receptor type 1

谭兵; 张德纯; 汪正清

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Expression, purification and bioactivity identification of recombinant SCR15-18 domain of human soluble complement receptor type 1

更新时间：2026-01-09

- Expression, purification and bioactivity identification of recombinant SCR15-18 domain of human soluble complement receptor type 1
- Journal of Army Medical University Vol. 29, Issue 10, Pages: 892-895(2007)
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  CLC： R392-33;R392.11;{R392.13}
- Published：2007
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谭兵,张德纯,汪正清.重组人可溶性补体受体1型SCR15-18片段表达纯化及生物活性鉴定[J].陆军军医大学学报(原第三军医大学学报),2007,29(10):892-895.

　TAN Bing,ZHANG De-chun,WANG Zheng-qing.Expression, purification and bioactivity identification of recombinant SCR15-18 domain of human soluble complement receptor type 1[J].J Amry Med Univ (J Third Mil Med Univ),2007,29(10):892-895.
谭兵,张德纯,汪正清.重组人可溶性补体受体1型SCR15-18片段表达纯化及生物活性鉴定[J].陆军军医大学学报(原第三军医大学学报),2007,29(10):892-895. DOI：

　TAN Bing,ZHANG De-chun,WANG Zheng-qing.Expression, purification and bioactivity identification of recombinant SCR15-18 domain of human soluble complement receptor type 1[J].J Amry Med Univ (J Third Mil Med Univ),2007,29(10):892-895. DOI：

摘要

目的获得高表达、高纯度和高活性的可溶性补体受体1型SCR15-18 (sCR1-SCR15-18）蛋白。方法重组原核表达载体pET32a-sCR1-SCR15-18 在大肠杆菌BL21中经不同IPTG浓度、诱导时间和温度诱导表达，超声破菌，提取包含体，经Ni

-NTA 亲和层析后，选择不同氧化还原条件进行复性，进而检测其生物学活性。结果得到了有较高表达量、较高纯度和较好生物学活性的sCR1-SCR-15-18蛋白。结论优化了sCR1-SCR15-18蛋白的表达、纯化和复性的参数，所获结果为进一步动物体内保护实验研究奠定了基础。

Abstract

Objective To prepare highly expressed

purified and refolded SCR15-18 of human soluble complement receptor type 1 (sCR1-SCR15-18) protein. Methods The expression of recombinant pET32-sCR1-SCR15-18 in E.coli.. BL21 was induced by IPTG of different concentrations for different time period under different temperatures and the bacteria were split by sonication. The sCR1-SCR15-18 protein was purified by Ni

-NTA resin affinity chromatography. The purified protein was refolded under different conditions. Then the bioactivity of the protein was analyzed. Results The sCR1-SCR15-18 protein of high expression

purity and bioactivity was attained. Conclusion The parameters of expression

purificati

on and refolding of sCR1-SCR15-18 protein were optimized

which may pave a way for further studies.

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