The antibody was purified by affinity chromatography, and conjugated with PE under optimal conditions. The solution is free of unconjugated PE and unconjugated antibody.
Storage & Handling:
The antibody solution should be stored undiluted at 4°C and protected from prolonged exposure to light. Do not freeze.
Each lot of this antibody is quality control tested by immunofluorescent staining with flow cytometric analysis. For immunofluorescent staining, the suggested use of this reagent is 20 µl per million cells or 20 µl per 100 µl of whole blood. It is recommended that the reagent be titrated for optimal performance for each application.
Application Notes:
Additional reported applications (for the relevant formats) include: immunofluorescence microscopy3, immunohistochemical staining of acetone-fixed frozen tissue sections.
Application References:
1. Schlossman, S., et al., Eds. 1995. Leukocyte Typing V: White Cell Differentiation Antigens. Oxford University Press. New York. 2. McMichael, A., et al., 1987. Leucocyte Typing III. Oxford University Press. New York. 3. Yang , G. P., et al., 1999. Nucleic Acids Research 27:1517. 4. Kristiansen, G., et al., 2003. Clin. Cancer Res. 9:4906.
Human peripheral blood lymphocytes stained ML5 PE
Description:
CD24 is a 35-45 kD glycosylphosphatidylinositol (GPI)-linked protein also known as heat stable antigen (HSA), BA-1, Ly-52, and nectadrin. It is expressed on the surface of B cells (but not plasma cells), granulocytes, follicular dendritic cells, and epithelial cells. CD24 may play a role in the regulation of B-cell proliferation and maturation. CD24 crosslinking induces a Ca2+ flux in mature B cells. CD24 has been shown to interact with CD62P (P-selectin).
Other Names:
Ly-52, Heat Stable Antigen (HSA), Nectadrin, BA-1
Structure:
GPI-linked glycoprotein, 35-45 kD
Distribution:
B cells, granulocytes, epithelial cells
Function:
B cell proliferation and differentiation
Ligand Receptor:
CD62P (P-Selectin)
Antigen References:
1. Schlossman, S., et al., Eds. 1995. Leukocyte Typing V. Oxford University Press. New York.
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