Ectonucleoside triphosphate diphosphohydrolase-1 (NTPDase-1) is an integral membrane protein with an extracellular active site. rhNTPDase-1 was expressed as a protein lacking its N- and C-terminal transmembrane domains, resulting in the secretion of the soluble rhNTPDase-1 ectodomain. NTPDase-1 was originally described as CD39, a B lymphocyte cell surface marker (2), but it is also present on the surface of natural killer cells, T cells, and some endothelial cells (3). NTPDase-1 hydrolyzes the beta - and gamma phosphate residues of nucleotides, preferring ATP as the substrate. Through its hydrolysis of extracellular nucleotides, NTPDase-1 plays a role in the regulation of purinergic signaling (4). NTPDase-1 is involved in the processes of thromboregulation and vascular inflammation (5). The administration of soluble NTPDase-1 may have therapeutic applications for the treatment of some vascular and transplantation-associated diseases (6).
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