IL-3 is produced mainly by T cells following cell activation by antigens and mitogens, but also by keratinocytes, natural killer cells, mast cells, endothelial cells, and monocytes. The analysis of bacterial-derived recombinant IL-3 shows that glycosylation is not required for the activity of IL-3. IL-3 sequences are evolutionarily less well conserved. Human and murine IL-3 show approximately 29% homology at the protein level while murine and rat IL-3 show approximately 54% homology. IL-3-alpha and IL-3-beta are two isoforms of rat IL-3. IL-3 receptors are expressed on macrophages, mast cells, eosinophils, megakaryocytes, basophils, bone marrow progenitor cells, and various myeloid leukemia cells. IL-3/receptor complexes have a Kdis of 10-9 - 10-10 M. Binding of IL-3 to its receptor causes specific phosphorylation of a 150 kDa membrane glycoprotein.
Aliases- IL-3, Mast cell growth factor, MCGF, Multipotential colony-stimulating factor, Multi-CSF, HCGF, P-cell stimulation factor, Hematopoietic growth factor
- Recombinant Mouse Interleukin-3 (IL3)
Formulation- Recombinant mouse Interleukin-3 was lyophilized from a 0.2 µm filtered PBS solution.
Endotoxin Level- <1.0 EU/µg of recombinant protein as determined by the LAL method.
Storage Condition- The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at +2° to +8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.