Research Report

Expression and Purification of Arabidopsis CASPL1D2 Protein  

Yujie Qu1,2 , Shenkui Liu3 , Yuanyuan Bu1,2
1 Key Laboratory of Saline-Alkali Vegetation Ecology Restoration (Northeast Forestry University), Ministry of Education, Harbin, 150040, China
2 College of Life Science, Northeast Forestry University, Harbin 150040, China
3 The State Key Laboratory of Subtropical Silviculture, Zhejiang Agriculture and Forestry University, Lin’An, 311300, China
Author    Correspondence author
Molecular Soil Biology, 2023, Vol. 14, No. 2   doi: 10.5376/msb.2023.14.0002
Received: 18 Jan., 2023    Accepted: 08 Apr., 2023    Published: 16 May, 2023
© 2023 BioPublisher Publishing Platform
This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Preferred citation for this article:

Qu Y.J., Liu S.K., and Bu Y.Y., 2023, Expression and purification of Arabidopsis CASPL1D2 protein, Molecular Soil Biology, 14(2): 1-5 (doi: 10.5376/msb.2023.14.0002)


AtCASPL1D2 belongs to the non-featured protein family UPF0497. To investigate the optimal conditions for its protein expression and purification, the AtCASPL1D2 gene from wild-type Arabidopsis thaliana was cloned and constructed into the protein expression vector pET-32a. The AtCASPL1D2 gene was expressed in Escherichia coli BL21 as a His fusion protein. The His-AtCASPL1D2 fusion protein was induced and purified under the optimized culturing condition of 0.2 mM IPTG and 20 ℃ for 5 h. The study laid the foundation for subsequent experiments to analyze the activity of AtCASPL1D2 protein and to verify the interaction between the gene and the proteins.

AtCASPL1D2; Protein expression; Protein purification; Arabidopsis thaliana
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