Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is 0.02-0.1 ng/mL. The specific activity of Recombinant Human IL-3 is approximately 1.8 x 103 IU/μg, which is calibrated against recombinant human IL-3 WHO International Standard (NIBSC code: 91/510). Specific activity is for reference purposes only and is not routinely tested.
E. coli-derived human IL-3 protein Ala20-Phe152, with and without an N-terminal Met
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
<0.10 EU per 1 μg of the protein by the LAL method.
15 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
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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