Murine CD38, a type II transmembrane glycoprotein, is a bifunctional ectoenzyme capable of catabolizing nicotinamide adenine dinucleotide (NAD+) to cyclic ADP-ribose (cADPR), and then hydrolyzing cADPR to adenosine diphosphoribose (ADPR).1-3 It is expressed at high levels on the surface of peripheral B-lineage cells, and at low density on germinal center B cells from unimmunized mice.4 It has also been reported to be expressed at moderate levels on NK cells, a proportion of peripheral T cells, and a subpopulation of thymocytes which are mostly TCRalpha beta+, CD4-, CD8-.5, 6 Murine CD38 is also expressed by all Mac-1+ macrophages in the peritoneal cavities of unimmunized mice, but not by unstimulated bone-marrow-derived macrophages.4, 7 Monoclonal antibodies to CD38 have been shown to induce B- and T-cell proliferation, protect B cells from apoptosis, and inhibit B lymphopoiesis.2 ,5, 8