>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
94 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
99 kDa and 103 kDa, migrates as a doublet under reducing conditions
ectonucleotide pyrophosphatase/phosphodiesterase family member 2
Extracellular lysophospholipase D
phosphodiesterase I/nucleotide pyrophosphatase 2
plasma lysophospholipase D
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 ENPP1 & 3, all of which contain a 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). The hydrolysis of nucleotides and lysophospholipids by ENPP-2 is mediated by a single catalytic site (2). Evidence shows LPA and sphingosine 1-phosphate to be specific 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).
Cimpean, A. et al. (2004) Biochem. J. 381:71.
Gijsbers, R. et al. (2003) FEBS Letters. 538:60.
Van Meeteren, L.A. et al. (2005) J. Biol. Chem. 280:21155.
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