Technical Data
CD38 (Acute Lymphoblastic Leukemia Cells Antigen, ADP Ribosyl Cyclase, CADPr Hydrolase 1, Cyclic ADP Ribose Hydrolase, Ecto Nicotinamide Adenine Dinucleotide Glycohydrolase, I19 (Mouse), Lymphocyte Differentiation Antigen) (PE)
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). 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. 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-. 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. Monoclonal antibodies to CD38 have been shown to induce B- and T-cell proliferation, protect B cells from apoptosis, and inhibit B lymphopoiesis (1-7).

Suitable for use in Flow Cytometry, Immunoprecipitation, Immunohistochemistry and Induction of B lymphocyte proliferation. Other applications not tested.

Recommended Dilution:
Flow Cytometry: 0.2ug/10e6 cells
Immunohistochemistry: Frozen sections.
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C before opening. DO NOT FREEZE! Stable at 4C as an undiluted liquid. Dilute only prior to immediate use. Stable for at least 12 months at 4C. Freezing R-Phycoerythrin (PE) conjugates will result in a substantial loss of activity. PE conjugates are sensitive to light.
100ug4C Do not freezeBlue IceMouseRat
Mouse CD38
Supplied as a liquid in PBS, 0.1% sodium azide and a stabilizing agent. Labeled with PE.
Recognizes mouse CD38, Mr 42-46kD.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Harada, N., L. Santos-Argumedo, R. Chang, J. C. Grimaldi, F. E. Lund, C. I. Brannan, N. G. Copeland, N. A. Jenkins, A. W. Heath, and R. M. Parkhouse. 1993. J. Immunol. 151:3111. 2. Santos-Argumedo, L., C. Teixeira, G. Preece, P. A. Kirkham, and R. M. E. Parkhouse. 1993. J. Immunol. 151:3119. 3. Howard, M., J. C. Grimaldi, J. F. Bazan, F. E. Lund, L. Santos-Argumedo, R. M. E. Parkhouse, T. F. Walseth, and H. C. Lee. 1993. Science 262:1056. 4. Lund, F., N. Solvason, J. C. Grimaldi, R. M. Parkhouse, and M. Howard. 1995. Immunol. Today 16:469. 5. Kirkham, P. A., L. Santos-Argumedo, M. M. Harnett, and R. M. Parkhouse. 1994. Immunology 83:513. 6. Bean, A. G. D., D. I. Godfrey, W. G. Ferlin, L. Santos-Argumedo, R. M. E. Parkhouse, M. C. Howard, and A. Zlotnik. 1996. Int. Immunol. 7:213. 7. Kumagai, M., E. Coustan-Smith, D. J. Murray, O. Silvennoinen, K. G. Murti, W. E. Evans, F. Malavasi, and D. Campana. 1995. J. Exp. Med. 181:1101.