Expression and purification of recombinant human hemangiopoietin in Escherichia coli

Ren Qian; Ma Fengxia#; Chen Zhong; Lu Shihong; Han Zhibo; Liu Yongjun; Xu Bin; Zhang Xiangyu; Han Zhongchao State Key Laboratory of Experimental Hematology; National Research Center for Stem Cell Engineering and Technology; Institute of Hematology; Hospital of Blood Diseases; Chinese Academy of Medical Sciences; Peking Union of Medical College; Tianjin 300020; China

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Expression and purification of recombinant human hemangiopoietin in Escherichia coli

Updated：2026-03-12

- Expression and purification of recombinant human hemangiopoietin in Escherichia coli
- Expression and purification of recombinant human hemangiopoietin in Escherichia coli
- 解放军医学杂志（英文版） 2008年第3期页码：148-153
- Affiliations：
- Author bio：
- Funds：
  
  the Natural Science Foundation of China （30300186）;the Grant of 863 projects from the Ministry of Science & Technology of China （2002AA223354）
- DOI：
  中图分类号： R378
- 纸质出版：2008
- Accepted：
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Expression and purification of recombinant human hemangiopoietin in Escherichia coli[J]. 解放军医学杂志（英文版）, 2008,(3):148-153.

[1].Expression and purification of recombinant human hemangiopoietin in Escherichia coli[J].Journal of Medical Colleges of PLA,2008(03):148-153.
Expression and purification of recombinant human hemangiopoietin in Escherichia coli[J]. 解放军医学杂志（英文版）, 2008,(3):148-153. DOI：

[1].Expression and purification of recombinant human hemangiopoietin in Escherichia coli[J].Journal of Medical Colleges of PLA,2008(03):148-153. DOI：

摘要

Abstract

Objective:To express the soluble recombinant hemangiopoietin protein in E.coli BL21（DE3）.Methods:Using human fetal live cDNA as a template

a partial cDNA fragment of HAPO coding N-terminal region was subcloned into plasmids pTrc99

pQE60 and pET32c to construct different recombinant prokaryotic expression systems.After selecting

the soluble rhHAPO fusion protein was expressed stably in E.coli BL21（DE3） by vector pET32c-HAPO and further isolated by nickelnitrilotriacetic acid（NTA） affinity chromatography.After cleavage with enterokinase

the rhHAPO protein was applied to Fast Flow SP sepharose column.Results:The rhHAPO protein had a purity of more than 95% and a good bioactivity based on the cell adhesion assay in ECV304 cells.Conclusion:We have established a protein engineering system to produce rhHAPO which may provide the possibility for clinical application.

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