Antigenic assessment of a recombinant human CD90 protein expressed in prokaryotic expression system

被引：6
作者：
Yousefi-Rad, Narges [1 ]
Shokrgozar, Mohammad Ali [2 ]
Behdani, Mandi [3 ]
Moradi-Kalbolandi, Shima [2 ]
Motamedi-Rad, Mandieh [4 ]
Habibi-Anbouhi, Mandi [2 ]
机构：
[1] Islamic Azad Univ, Pharmaceut Sci Branch, Fac Adv Sci & Technol, Dept Microbiol, Tehran, Iran
[2] Pasteur Inst Iran, Natl Cell Bank Iran, Tehran, Iran
[3] Pasteur Inst Iran, Biotechnol Res Ctr, Tehran, Iran
[4] Pasteur Inst Iran, Dept Hepatitis & AIDs, Tehran, Iran
来源：
PROTEIN EXPRESSION AND PURIFICATION | 2015年 / 116卷
基金：
美国国家科学基金会;
关键词：
Human CD90 (Thy-1); Prokaryotic expression system; Escherichia coli (E. coli); Recombinant protein; PROGENITOR CELLS; THY-1; GENE; STEM; IDENTIFICATION; POPULATION; STRATEGIES; EXPANSION;
D O I：
10.1016/j.pep.2015.08.017
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Cluster of Differentiation 90 (CD90, Thy-1) has been proposed as one of the most important biomarkers in several cancer cells including cancer stem cells (CSCs). CD90 is considered as a potential normal stem cell and CSCs biomarker and also has been identified in lung cancer stem cells, hepatocellular carcinoma cells and high-grade gliomas. Using eukaryotic host systems involves complex procedures and frequently results in low protein yields. The expression of recombinant proteins in Escherichia coli is comparatively easier than eukaryotic host cells. The potential of large scale production of recombinant protein has made this system an economic production platform. In this study we expressed the extra-membrane domain of human CD90 (exCD90) antigen (Gln(15)-Cys(130)) in E. coli expression host cells. The epitope integrity of purified recombinant antigen was confirmed by antibody-antigen interaction using 5E10 anti-CD90 monoclonal antibody and binding study through ELISA and florescent staining of CD90(+) cells in a flow cytometry experiment. (C) 2015 Elsevier Inc. All rights reserved.
引用
收藏
页码：139 / 143
页数：5
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