Expression and Purification of Arabidopsis CASPL1D2 Protein
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
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
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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