IL3 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 IL3 shows that glycosylation is not required for activity. IL3 sequences are evolutionarily less well conserved with human and murine IL3 sharing approximately 29% homology (at the protein level) and murine and rat IL3 sharing approximately 54% homology. IL3 receptors are expressed on macrophages, mast cells, eosinophils, megakaryocytes, basophils, bone marrow progenitor cells and various myeloid leukemia cells. Binding of IL3 to its receptor causes specific phosphorylation of a 150 kDa membrane glycoprotein. Recombinant human IL3 is a non-glycosylated globular protein.
Aliases- IL-3, Mast cell growth factor, MCGF, Multi-CSF, Hematopoietic growth factor, HCGF, P-cell stimulation factor
- Recombinant Human Interleukin-3 (IL3)
Formulation- Lyophilized from a 0.2 µm filtered solution in Phosphate Buffer and NaCl (pH 6.3)
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.