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Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained SDS-PAGE gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).

Journal: The Journal of Biological Chemistry

Article Title: Structural basis for the mechanism and stability of the EEPD1 5′ endonuclease

doi: 10.1016/j.jbc.2026.111432

Figure Lengend Snippet: Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained SDS-PAGE gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).

Article Snippet: The isolated Flag-EEPD1 full length WT sample was loaded onto an SDS polyacrylamide gel (12% Mini-PROTEAN TGX, Bio-Rad Laboratories Inc) and electrophoreses to a distance of 1 cm and stained with Coomassie Brilliant Blue R-250.

Techniques: Purification, Staining, SDS Page, Size-exclusion Chromatography