Recombinant Escherichia coli Iron-sulfur cluster repair protein ytfE (ytfE) (Active)

YtfE plays a critical role in iron-sulfur cluster repair under nitrosative stress in *E. coli*, making it a valuable tool for studying bacterial NO signaling and stress response pathways. This full-length recombinant protein (aa 1–220) carries an N-terminal GST tag and is expressed in *E. coli*, preserving native folding context relevant to downstream functional studies. Binding activity has been validated by functional ELISA, where immobilized AqpZ at 5 μg/ml demonstrated interaction with ytfE at an EC50 of 197.90–259.70 μg/ml, supporting use in protein–protein interaction assays, binding kinetics studies, and ELISA-based screening of interaction partners. Purity exceeding 85% by SDS-PAGE provides a suitable basis for biochemical binding assays and as a positive control in functional ELISAs, though endotoxin levels have not been tested, which researchers should consider if planning cell-based experiments.