Recombinant Cynomolgus/Rhesus Neprilysin/CD10 His Protein CF

Neprilysin/CD10, also known as NEP, neutral endopeptidase, enkephalinase, and common acute lymphocytic leukemia antigen (CALLA), is a zinc-dependent metallopeptidase type II integral membrane protein of the M13 subfamily of neutral endopeptidases. The enzyme functions both as an endopeptidase with a thermolysin-like specificity and as a dipeptidylcarboxypeptidase. It cleaves and degrades a variety of bioactive peptides including natriuretic peptides, enkephalins, and tachykinins at the amino side of hydrophobic residues. Neprilysin is widely distributed in tissues and highly conserved among mammals (1). Neprilysin is a noncovalently associated homodimer where the monomer is composed of a short intracellular domain, transmembrane helix, and large C-terminal extracellular domain including two domains that form a central cavity containing the active site (2). Although a membrane protein, an alternatively processed soluble form has been documented in circulation and retains similar enzymatic activity to the membrane bound Neprilysin (3). The soluble form is of interest as a prognostic biomarker for heart failure (4,5) and inhibition of Neprilysin is a therapeutic strategy for heart failure (6). Neprilysin was found to be a major degrading enzyme of amyloid beta peptide (A beta) in the brain, making it an important target in Alzheimer's disease studies (7). It metabolizes sensory and inflammatory neuropeptides making it a target for pain perception (8) and is an important marker for some types of lymphomas (9,10). There is also interest in Neprilysin as a biomarker (11) and as a therapeutic inhibition target for treatment of type 2 diabetes (12).