June 15, 2023

Heating-mediated purification of active FGF21 and structure-based design of its variant with enhanced potency

NEW iLite® CELLS CITATION

This new study employed iLite® FGF21 assay-ready to evaluate the protein stability of FGF21 during heating-mediated purification. 


The findings suggest that heated FGF21 retains its biological activity, similar to that of non-heated and commercial FGF21s.

June 15, 2023

Heating-mediated purification of active FGF21 and structure-based design of its variant with enhanced potency

NEW iLite® CELLS CITATION

This new study employed iLite® FGF21 assay-ready to evaluate the protein stability of FGF21 during heating-mediated purification. 


The findings suggest that heated FGF21 retains its biological activity, similar to that of non-heated and commercial FGF21s.

BACKGROUND AND STUDY OBJECTIVES

FGF21 is a protein involved in metabolic processes, such as glucose and lipid metabolism. It has shown promising therapeutic potential for treating obesity-related metabolic complications, as studies on animal models have demonstrated a reduction in fat mass and body weight, as well as improved energy metabolism and insulin sensitivity when administered with FGF21.

This study aimed to investigate the effects of heat treatment on the biological activity of human FGF21 and various FGF21 mutants with different structure-based designs. The researchers measured the activation of the Receptor Signaling Complex FGFR1c/ β-Klotho to determine the protein stability and activity.

STUDY OUTCOMES

Utilizing the iLite FGF21 assay-ready cells, the FGFR1c/β-Klotho activation levels of FGF21 were compared with the ones that underwent heating treatment. The article also reported that heated and non-heated FGF21 present comparable activity since the level of FGFR1c/ β-Klotho activation levels did not present a difference and were similar to the commercial FGFR21. The FGF21 iLite assay-ready cells were also used to determine the activity of structure-based FGF21 mutants. 

This article highlights the potential use for protein stability characterization, an integral step in biopharmaceutical development.

CITATION

Jung YE, Lee KW, Cho JH, et al. Heating-mediated purification of active FGF21 and structure-based design of its variant with enhanced potency. Sci Rep. 2023;13(1):1005. doi:10.1038/s41598-023-27717-x

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iLite FGF21 cells

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