Recombinant Rat Alkaline phosphatase (Alpp), partial (Active)

Alkaline phosphatase plays a central role in phosphate metabolism and serves as a widely used reporter enzyme, yet obtaining catalytically competent recombinant material with defined kinetics remains challenging for quantitative enzymology. This rat Alpp variant, spanning residues 19–501 with a C-terminal 10×His tag positioned distal to the active site, demonstrates robust catalytic function with a specific activity exceeding 8000 pmol/min/μg against p-nitrophenylphosphate at pH 10.0 and 37°C, providing a quantitative benchmark for kinetic parameter analysis including Km, Vmax, and kcat/Km determinations. The greater than 95% purity meets the quality thresholds commonly required for accurate enzyme kinetics, inhibitor screening with IC50 determination, and substrate specificity profiling where trace contaminants would confound rate measurements. Endotoxin levels below 1.0 EU/μg support use in cell-based assays for drug candidate evaluation, while the validated activity and high purity align with standards expected in structural studies by crystallography or cryo-EM.