Issue

Vol. 61 No. 2: Issue 2

The undersigned hereby assign all rights, included but not limited to copyright, for this manuscript to CMB Association upon its submission for consideration to publication on Cellular and Molecular Biology. The rights assigned include, but are not limited to, the sole and exclusive rights to license, sell, subsequently assign, derive, distribute, display and reproduce this manuscript, in whole or in part, in any format, electronic or otherwise, including those in existence at the time this agreement was signed. The authors hereby warrant that they have not granted or assigned, and shall not grant or assign, the aforementioned rights to any other person, firm, organization, or other entity. All rights are automatically restored to authors if this manuscript is not accepted for publication.

Arabidopsis thaliana SEPALLATA3 protein prokaryotic expression and purification

Q. He
Key University Laboratory of Biotechnology and Utilization of Bio-resource of Shandong, College of Life Science, Dezhou University, Dezhou 253023
A. Y. Fu
Key University Laboratory of Biotechnology and Utilization of Bio-resource of Shandong, College of Life Science, Dezhou University, Dezhou 253023
G. C. Zhang
Key University Laboratory of Biotechnology and Utilization of Bio-resource of Shandong, College of Life Science, Dezhou University, Dezhou 253023
T. J. Li
Key University Laboratory of Biotechnology and Utilization of Bio-resource of Shandong, College of Life Science, Dezhou University, Dezhou 253023
J. H. Zhang
Key University Laboratory of Biotechnology and Utilization of Bio-resource of Shandong, College of Life Science, Dezhou University, Dezhou 253023

Corresponding Author(s) : Q. He

manuscript_sub@126.com

Cellular and Molecular Biology, Vol. 61 No. 2: Issue 2

Abstract

SEPALLATA3 (SEP3) can be attributed to E class gene of the ABCE model of floral organ development. In order to reveal how SEP3 proteins form polymers, and the relationship between the polymers and their biological functions, the experiments of Arabidopsis thaliana AtSEP3 protein soluble expression in vitro were performed to construct a vector of prokaryotic expression, and investigate induced expression of recombinant proteins in Escherichia coli cells. The protein soluble expression was analyzed through the aspects of different protein domains, induction time, induction temperature, etc. Different structural domains and expression conditions were screened, and 0.1% IPTG inducing at 22 oC for 15 h was estimated as an optimal expression strategy. The nickel chelating resin was used to purify the protein in size exclusion chromatography (SEC) and the results indicated that AtSEP3 protein was present in the form of tetramer.

Keywords

Botany SEP3 protein prokaryotic system protein purification polymer.
He, Q., Fu, A. Y., Zhang, G. C., Li, T. J., & Zhang, J. H. (2015). Arabidopsis thaliana SEPALLATA3 protein prokaryotic expression and purification. Cellular and Molecular Biology, 61(2), 60–63. Retrieved from https://cellmolbiol.org/index.php/CMB/article/view/1135
Download Citation
Endnote/Zotero/Mendeley (RIS)
BibTeX
Author biographies is not available.
Download this PDF file
PDF
Statistic
Read Counter : 577 Download : 284