Recombinant Mouse ENPP-2/Autotaxin Protein, CF

ENPP-2, also known as Autotaxin, belongs to the ectonucleotide pyrophosphatase/phosphodiesterase (NPP) family. Some NPPs hydrolyze phosphates from nucleotides and their derivatives. ENPP-2 shares 40‑50% identity to ENPP-1 & -3, all of which contain an N‑terminal intracellular domain, a single transmembrane domain and a large extracellular domain that includes a catalytic domain, two somatomedin B-like domains, and a C-terminal nuclease like domain (1). Unlike ENPP‑1 and ENPP‑3, ENPP‑2 has weak activity against nucleotides, but exhibits a lysophospholipase D activity which allows the formation of lysophosphatidic acid (LPA) and choline from lysophosphatidylcholine (2). ENPP-2 can also hydrolyze sphingosylphosphorylcholine to produce sphingosine-1-phosphate, a lipid messenger molecule. The hydrolysis of nucleotides and lysophospholipids by ENPP2 is mediated by a single catalytic site (2). LPA and sphingosine-1-phosphate are inhibitors of ENPP-2 (3). ENPP-2 was originally found to stimulate tumor cell motility and has since been found to enhance tumor invasion and metastasis (4) and to be up‑regulated in several types of carcinomas including breast and lung (5). ENPP-2 is most highly expressed in brain and adipose tissue (6). Recombinant mouse ENPP-2 was expressed without its transmembrane and intracellular domains, resulting in the secretion of the recombinant enzyme.