Mouse CD39/ENTPD1 PE-conjugated Antibody

Ectonucleoside Triphosphate Diphosphohydrolase-1 (ENTPD1) is a 65-80 kDa, two-transmembrane glycoprotein that contains an N- and C-terminal cytoplasmic domain (1, 2). ENTPD1 was originally described as CD39, a B lymphocyte cell surface marker and is now known to also be present on the surface of endothelial cells, neutrophils, mast cells, macrophages, pancreatic acinar and duct cells, dendritic cells, sympathetic neuron axon terminals, CD4⁺ CD39⁺ CD161⁺ Th17 precursors, PD-1⁺ CD39⁺ "exhausted" CD8⁺ T cells and FoxP3⁺ CD25⁺ CD4⁺ CD127^- CD49d^- suppressor plus FoxP3^- CD25^- CD4⁺ CD127⁺ CD49d⁺ non-suppressor T cells (1-9). ENTPD1 hydrolyzes the beta- and gamma phosphate residues of nucleotides, preferring ATP as the substrate. Through its hydrolysis of extracellular nucleotides, ENTPD1 plays a role in the regulation of purinergic signaling. Extracellular ATP released from dead or stressed cell creates a proinflammatory environment. In concert with CD73, the conversion of ATP to adenosine reverses this and creates an antiinflammatory environment (1,2). Over amino acids (aa) 38-478, mouse ENTPD1 shares 90% and 76% aa sequence identity with rat and human ENTPD1, respectively