Expression, Purification and Characterization of Recombinant Canine FGF21 in Escherichia coli

Title:Expression, Purification and Characterization of Recombinant Canine FGF21 in Escherichia coli

Volume: 23 Issue: 9

Author(s): Zhong Zhenga, Chengjun Yanga, Ruofeng Yinb, Jinxi Jiangc, Haiting Hea, Xinxin Wanga, Mujie Kan and Yechen Xiao

Affiliation:

Keywords: Recombinant canine FGF21, Escherichia coli, purification, plasma glucose.

Abstract: The canine metabolic diseases, such as obesity and diabetes, have become a worldwide problem. Fibroblast growth factor 21 (FGF21) is a potent regulator which has many biological functions relative to metabolism regulation. It suggests that FGF21 plays important roles in regulating canine metabolic diseases. To acquire the recombinant canine FGF21 (rcFGF21) in Escherichia coli, the recombinant bacteria were induced by 0.5 mM IPTG for 16 hours at 16 °C, and the rcFGF21 protein was purified by Ni-NTA. 8 mg rcFGF21 was acquired from one liter bacteria. The rcFGF21 protein has specific immunoblot reactivity against anti-FGF21 and anti-His antibody. The in vivo experimental result showed that rcFGF21 can significantly reduce plasma glucose of STZ-induced diabetic mice.

Cite this article as:

Zhenga Zhong, Yanga Chengjun, Yinb Ruofeng, Jiangc Jinxi, Hea Haiting, Wanga Xinxin, Kan Mujie and Xiao Yechen, Expression, Purification and Characterization of Recombinant Canine FGF21 in Escherichia coli, Protein & Peptide Letters 2016; 23 (9) . https://dx.doi.org/10.2174/0929866523666160628091657