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一种在大肠杆菌中高效表达和纯化 S100 蛋白的策略。

An efficient expression and purification strategy for the production of S100 proteins in Escherichia coli.

机构信息

Shanghai Municipality Key Laboratory of Veterinary Biotechnology, School of Agriculture and Biology; Shanghai Jiao Tong University, Shanghai, P.R. China.

出版信息

Bioengineered. 2013 Jan-Feb;4(1):55-8. doi: 10.4161/bioe.22172. Epub 2012 Sep 18.

Abstract

S100 proteins belong to a family of small, acidic, EF-hand Ca ( 2+) -binding proteins and have been found to exert both intracellular and extracellular functions in regulation of Ca ( 2+) homeostasis, cytoskeletal dynamics, cell cycle, motility and differentiation. As a result, they have been widely investigated for their association with diseases, such as, neurological diseases, cardiomyopathy, neoplasias and inflammatory diseases. To facilitate further studies of S100 proteins, we reported a simple and efficient method for the expression and purification of human S100A4 and S100A11 proteins in Escherichia coli. Since S100 proteins share many common physical and chemical characteristics, we expect that this approach can be extended to the production of most S100 proteins.

摘要

S100 蛋白属于一族小的、酸性的 EF 手型 Ca(2+)结合蛋白,已发现其在调节 Ca(2+)稳态、细胞骨架动力学、细胞周期、运动和分化方面具有细胞内和细胞外功能。因此,它们已被广泛研究与疾病的关联,如神经疾病、心肌病、肿瘤和炎症性疾病。为了促进对 S100 蛋白的进一步研究,我们报道了一种在大肠杆菌中表达和纯化人 S100A4 和 S100A11 蛋白的简单有效的方法。由于 S100 蛋白具有许多共同的物理和化学特性,我们预计这种方法可以扩展到大多数 S100 蛋白的生产。

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本文引用的文献

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Expression and purification of bioactive high-purity human S100A6 in Escherichia coli.
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