Recombinant Macaca fascicularis ADAM metallopeptidase domain 9 (ADAM9), partial, Biotinylated (Active)

ADAM9 metallopeptidase plays critical roles in ectodomain shedding and cell-surface protein processing, making it a key target in neuroscience research focused on synaptic remodeling and neuroinflammation. This cynomolgus macaque ortholog, spanning residues 29–698 with C-terminal His-Avi tags, demonstrates specific binding activity with an EC50 of 114.4–171.1 ng/mL in functional ELISA, confirming proper folding and epitope accessibility that supports its use in antibody-based detection assays and as a positive control in enzyme-linked screening platforms. The >95% purity determined by SDS-PAGE, combined with endotoxin levels below 1.0 EU/μg, meets the quality thresholds commonly required for inhibitor screening, IC50 determination, and drug candidate evaluation where contaminants could confound dose-response measurements. Biotinylation enables straightforward immobilization in surface plasmon resonance and biolayer interferometry experiments, facilitating kinetic parameter analysis and substrate specificity profiling without compromising the catalytic domain.