|Cell Proliferation Induced by IL‑3 and Neutralization by Human IL‑3 Antibody. Recombinant Human IL‑3 (Catalog # 203-IL) stimulates proliferation in the TF‑1 human erythroleukemic cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Human IL‑3 (1.25 ng/mL) is neutralized (green line) by increasing concentrations of Mouse Anti-Human IL‑3 Monoclonal Antibody (Catalog # MAB203). The ND50 is typically 0.03-0.08 µg/mL.|
|IL‑3 in Human PBMCs. IL‑3 was detected in immersion fixed human peripheral blood mononuclear cells (PBMCs) using Mouse Anti-Human IL‑3 Monoclonal Antibody (Catalog # MAB203) at 25 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.|
Interleukin 3 is a pleiotropic factor produced primarily by activated T cells that can stimulate the proliferation and differentiation of pluripotent hematopoietic stem cells as well as various lineage committed progenitors. In addition, IL-3 also affects the functional activity of mature mast cells, basophils, eosinophils and macrophages. Because of its multiple functions and targets, it was originally studied under different names, including mast cell growth factor, P-cell stimulating factor, burst promoting activity, multi-colony stimulating factor, thy-1 inducing factor and WEHI-3 growth factor. In addition to activated T cells, other cell types such as human thymic epithelial cells, activated murine mast cells, murine keratinocytes and neurons/astrocytes can also produce IL-3. At the amino acid sequence level, mature human and murine IL-3 share only 29% sequence identity. Consistent with this lack of homology, IL-3 activity is highly species-specific and human IL-3 does not show activity on murine cells.
IL-3 exerts its biological activities through binding to specific cell surface receptors. The high affinity receptor responsible for IL-3 signaling is composed of at least two subunits, an IL-3 specific alpha chain which binds IL-3 with low affinity and a common beta chain that is shared by the IL-5 and GM-CSF high-affinity receptors. Although the beta chain itself does not bind IL-3, it confers high-affinity IL-3 binding in the presence of the alpha chain. Receptors for IL-3 are present on bone marrow progenitors, macrophages, mast cells, eosinophils, megakaryocytes, basophils and various myeloid leukemic cells.
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