在大肠杆菌中表达和纯化具有生物活性的高纯度重组小鼠 CXCL14。

Expression and purification of bioactive high-purity recombinant mouse CXCL14 in Escherichia coli.

机构信息

Shanghai Municipality Key Laboratory of Veterinary Medicine and Biotechnology, School of Agriculture and Biology, Shanghai, People's Republic of China.

出版信息

Appl Biochem Biotechnol. 2011 Aug;164(8):1366-75. doi: 10.1007/s12010-011-9218-y. Epub 2011 Mar 23.

DOI:10.1007/s12010-011-9218-y

PMID:21431320

Abstract

Mouse CXCL14/BRAK is a monocyte-selective chemokine which is expressed in almost all normal tissues. A flood of reports on its new functions of tumor suppression and fat metabolism modulation has left CXCL14 a potential therapeutic candidate for these diseases. Therefore, a simple accessible method is on demand for large-scale production of recombinant mouse CXCL14 protein for in vivo animal studies. Here, we introduce an efficient method for large-scale production of recombinant mouse CXCL14, by which an 18-mg protein is produced from 2-L Escherichia coli culture with good bioactivity and low level of endotoxin.

摘要

小鼠 CXCL14/BRAK 是一种单核细胞选择性趋化因子，几乎在所有正常组织中表达。大量关于其抑制肿瘤和调节脂肪代谢的新功能的报道，使 CXCL14 成为这些疾病的潜在治疗候选物。因此，对于大规模生产用于体内动物研究的重组小鼠 CXCL14 蛋白，需要一种简单、可及的方法。在此，我们介绍了一种高效生产重组小鼠 CXCL14 的方法，通过该方法，从 2-L 的大肠杆菌培养物中可获得 18mg 蛋白，具有良好的生物活性和低内毒素水平。