What question did this study set out to answer?

To facilitate proper folding and increase soluble expression of scFv-BsAb in Escherichia coli.

Enhancing soluble expression and purification of a bispecific scFv antibody in Escherichia coli using chaperones

View Full Paper

Ask AI

Bookmark

Authors

Experimental approach improved soluble scFv antibody yield in Escherichia coli, suggesting co-expression with chaperones enhances protein function.

To facilitate proper folding and increase soluble expression of scFv-BsAb in Escherichia coli.
Used Escherichia coli BL21(DE3) cells for protein expression
Investigated temperature and IPTG concentrations effects via SDS-PAGE and densitometry analysis
Purified the expressed protein using Ni-NTA affinity column
Evaluated binding ability with flow cytometry
Co-expression with chaperones enhanced soluble scFv-BsAb expression
Optimal conditions: 30 °C and 1 mM IPTG
Yield of 2.9 mg protein per L of culture

Alidousti-Shahraki et al. (2026) studied this question.

View Full Paper

Ask AI

Bookmark

Experimental approach improved soluble scFv antibody yield in Escherichia coli, suggesting co-expression with chaperones enhances protein function.