Construction, Expression, and Purification of ZNF191 (243-368) Zinc Finger Deletion Mutants
Journal: Journal of Biotechnology Research (Vol.4, No. 11)Publication Date: 2018-11-15
Authors : Dongxin Zhao; Zhongxian Huang;
Page : 80-82
Keywords : Affinity purification; Deletion mutant; GST fusion protein; Zinc finger protein; Recombinant vector.;
Abstract
The C-terminal region of the zinc finger protein ZNF191(243-368) contains a putative DNA-binding domain containing four Cys2His2 zinc finger motifs. To understand the properties and functions of the zinc finger motifs, a deletion gene of ZNF191(243-368) was inserted into pGEX-4T-2. The recombinant vector was transformed into Escherichia coli BL21, and a glutathione S-transferase (GST) fusion protein was expressed and purified using glutathione agarose affinity resin. The results show that this expression system can be used to express and purify zinc finger deletion mutants of ZNF191(243-368), providing a basis for further investigation of this protein.
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