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)

CD38 is a single chain type II integral transmembrane protein. It is highly expressed on thymocytes. It is also present on activated T cells and terminally differentiated B cells (plasma cells). Other reactive cells include NK cells, monocytes, macrophages, and dendritic cells. CD38 may be detected on cells from multiple myeloma, ALL (B and T) and some AML. It is not found on most mature resting peripheral lymphocytes. CD38 functions as a multicatalytic ectoenzyme serving as ADP-ribosyl cyclase, cyclic ADP-ribose hydrolase and possibly NAD+ glycohydrolase or as a cell surface receptor. Antibodies to CD38 are useful in subtyping of lymphomas and leukemias, detection of plasma cells (i.e. identification of myelomas), and as a marker for activated B and T cells.\n\nApplications:\nSuitable for use in Immunohistochemistry. Not suitable for use in Western Blot. Other applications not tested. \n\nRecommended Dilutions:\nImmunohistochemistry (Formalin/paraffin): 1:50-1:100 for 60 minutes at RT. Staining of formalin-fixed tissues requires boiling tissue sections in 10mM citrate buffer, pH 6.0 for 10-20 minutes, followed by cooling at RT for 20 minutes. Requires use of a high-sensitivity detection system.\nOptimal dilutions to be determined by the researcher.\n\nPositive Control: Tonsil\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

C2390-05

Size

500ul

Applications

IHC

Hosts

Mouse

Reactivities

Hum

Form

Supplied as a liquid, 0.09% sodium azide.

P Type

Mab

Purity

Tissue culture supernatant

Isotype

IgG1

References

1. Barclay, A.N., et al.: The Leucoctye Antigen Facts Book. Academic Press. London (1997). 2. Berthelier, V., et al., Research in Immunology147(6): 407-11 (1996). 3. Chen, Z., Shen, D.C., Yu, A.X., et al.: A group of monoclone antibodies reacted with human thymocyte differentiation antigens II. Biological properties. Shanghai J. of Immunol. 7(1): 1 (1987). 4. Ellis, J.H., et al.: Engineered anti-CD38 monoclonal antibodies for immunotherapy of multiple myeloma. J. Immunol. 155: 925-937 (1995). 5. Harada, N.L., et al.: Expression cloning of a cDNA encoding a novel murine B cell activation marker. Homology to human CD38. J. Immunol. 151: 3111-3118 (1993). 6. Howard, M., et al.: Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38. Science 262: 1056-1059 (1993). 7. Kirkham, P.A., et al.: Murine B-cell activation via CD38 and protein tyrosine phosphorylation. Immunology 83: 513-516 (1994). 8. Kishimoto, T., et al., eds.: Leucocyte Typing Workshop VI. Garland Publishing, Inc. (1998). 9. Knapp, W., et al., eds.: Leucocyte Typing Workshop IV. Oxford University Press (1989). 10. Ling, N.R., et al.: B-cell and plasma cell antigens: new and previously defined clusters. Leucocyte Typing III White cell differentiation antigens. McMichael, A.J., et al., Eds.: Oxford Univ. Press 302-335 (1987). 11. Lund, F., et al.: Murine CD38: an immunoregulatory ectoenzyme. Immunol. Today 16: 469-473 (1995). 12. Malavasi, F., et al.: Human CD38: a glycoprotein in search of a function. Immunol. Today 15: 95-97 (1994). 13. McMichael, A.J., Beverly, P.C.L., Gilks, W., et al., eds.: Leukocyte Typing III: White Cell Differentiation Antigens. pp41, 57, 66. Oxford University Press, New York (1987). 14. Mehta, K., et al.: Human CD38, a cell-surface protein with multiple functions. FASEB J. 18: 1408-1417 (1996). 15. Mikaelian, I., et al.: Antibodies That Label Paraffin-Embedded Mouse Tissues: A Collaborative Endeavor. Toxicology Pathology 32: 181-191 (2004). 16. Oliver, A.M., et al.: Mouse CD38 is down-regulated on germinal center B cells and mature plasma cells. J. Immunol. 158: 1108-1115 (1997). 17. Ramaschi, G.: Expression of cyclic ADP-Ribose-synthetizing CD38 molecule on human platelet membrane. Blood 6(87): 2308-2313 (1996). 18. Santos-Argumedo, L., et al.: A B lymphocyte surface molecule mediating activation and protection from apoptosis via calcium channels. J. Immunol. 151: 3119-3130 (1993). 19. Schlossman, S., Bloumsell, L., Gilks, W., et al., eds.: Leukocyte Typing V: White Cell Differentiation Antigens. pp249, 269. Oxford University Press, New York (1995). 20. Shen, D.C., Chen, Z., Yu, A.X., et al.: A group of monoclone antibodies reacted with human thymocyte differentiation antigens: production and specificity analysis. Chinese J. of Immunology 2(6): 331 (1986). 21. Yamada, M., et al., Brain Research 756(1-2): 52-60 (1997). 22. Yang, C.Y., Shen, D.C., She, M., et al.: The study of a CD38 monoclonal antibody. J. Monoclonal Antibody 9(4): 56 (1993). 23. Zocchi, E., et al.: A single protein immunologically identified as CD38 displays NAD+ Glycohydrolase, ADP-Ribosyl Cyclase and cyclic ADP-Ribose Hydrolase activities at the outer surface erythrocytes. Biochem. Biophys. Res. Com. 3(196): 1459-1465 (1993). 24. http://au.expasy.org/uniprot/P28907

Additional Info

Recognizes human CD38.