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Expression and purification of bioactive high-purity recombinant mouse CXCL14 in Escherichia coli
Jingjing Li1, Jin Gao, Sunita Sah
1Shanghai Municipality Key Laboratory of Veterinary Medicine and Biotechnology, School of Agriculture and Biology, Shanghai, People's Republic of China.
Abstract:
Mouse CXCL14/BRAK is a monocyte-selective chemokine which is expressed in almost all normal tissues. A flood of reports on its new functions of tumor suppression and fat metabolism modulation has left CXCL14 a potential therapeutic candidate for these diseases. Therefore, a simple accessible method is on demand for large-scale production of recombinant mouse CXCL14 protein for in vivo animal studies. Here, we introduce an efficient method for large-scale production of recombinant mouse CXCL14, by which an 18-mg protein is produced from 2-L Escherichia coli culture with good bioactivity and low level of endotoxin.
Insights
Researchers developed an efficient method for producing large quantities of mouse CXCL14/BRAK protein. This advancement supports further in vivo studies for potential therapeutic applications in cancer and metabolic diseases.
Area of Science:
- Biochemistry
- Molecular Biology
- Immunology
Background:
- Mouse CXCL14/BRAK is a monocyte-specific chemokine found in most normal tissues.
- Emerging research highlights its roles in tumor suppression and modulating fat metabolism.
- There is a need for scalable production methods for recombinant mouse CXCL14 protein for research.
Purpose of the Study:
- To establish an efficient and accessible method for the large-scale production of recombinant mouse CXCL14 protein.
- To ensure the produced protein possesses good bioactivity and low endotoxin levels for in vivo studies.
Main Methods:
- Utilized Escherichia coli (E. coli) as a host for recombinant protein expression.
- Optimized culture conditions for large-scale production.
- Purified the recombinant mouse CXCL14 protein.
Main Results:
- Successfully produced 18 mg of recombinant mouse CXCL14 protein from a 2-L E. coli culture.
- The produced protein demonstrated good bioactivity.
- Achieved a low level of endotoxin in the purified protein.
Conclusions:
- The developed method provides an efficient means for large-scale recombinant mouse CXCL14 production.
- This scalable method facilitates further in vivo investigations into CXCL14's therapeutic potential.
- The high yield, bioactivity, and low endotoxin levels make this method suitable for preclinical studies.
