Recombinant Human Dipeptidase 3(DPEP3), partial (Active)

Dipeptidase 3 plays a critical role in cellular peptide metabolism and has emerged as a target of interest in cancer biology, yet functional recombinant material for mechanistic studies has been limited. This mammalian-expressed protein spanning residues 36–463 demonstrates robust binding activity in functional ELISA, with an EC50 of 6.841–7.498 ng/mL against anti-DPEP3 antibody, confirming proper folding and epitope accessibility that supports its use as a positive control in immunoassays and as a reagent for inhibitor screening campaigns. The C-terminal His tag placement preserves the N-terminal catalytic domain architecture, providing a suitable basis for enzymatic activity assays, kinetic parameter determination (Km, Vmax, kcat/Km), and substrate specificity profiling experiments. Purity exceeding 95% by SDS-PAGE and endotoxin levels below 1.0 EU/μg meet the quality thresholds commonly required for accurate kinetic measurements and structure–function studies where contaminants would confound interpretation of catalytic efficiency or inhibition mechanisms.