Detection of IL‑3 R beta in DA3 Mouse Myeloma Cell Line by Flow Cytometry.
DA3 mouse myeloma cell line was stained with Rat Anti-Mouse IL‑3 R beta APC‑conjugated Monoclonal Antibody (Catalog # FAB5492A, filled histogram) or isotype control antibody (Catalog # IC006A, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
Background: IL-3 R beta
Interleukin 3 (IL-3) is a pleiotropic cytokine produced primarily by activated T cells or mast cells. IL-3 stimulates the proliferation and differentiation of hemopoietic cells including the pluripotent hematopoietic stem cells as well as various lineage-committed cells. The biological effects of IL-3 on the various cell types are mediated by the binding of IL-3 to specific cell surface receptor complexes. The functional high-affinity IL-3 receptor is a heterodimer consisting of a ligand binding alpha subunit and the beta subunit. The alpha subunit alone binds IL-3 with low affinity. The beta subunit is required for the high-affinity binding of IL-3 to the heterodimeric receptor complex. The beta subunit has also been found to be a component of the high-affinity receptor complex for IL-5 and GM-CSF and is also referred to as the beta common ( beta c) chain. In the mouse, there are two IL-3 R beta proteins. The first identified mouse IL-3 R beta was also called AIC2A and binds IL-3 with low affinity (1). The second mIL-3 R beta was referred to as AIC2B (2). AIC2B doesn’t bind IL-3 and is the homolog of the human IL-3 R beta. AIC2A was found to be the result of a gene duplication event. Both the alpha and the beta subunits are members of the cytokine receptor superfamily (3).
Itoh, N. et al. (1990) Science 247:324.
Gorman, D.M. et al. (1990) Proc. Natl. Acad. Sci. USA 87:5459.
Schrader, J.W. in Cytokine Reference, (2001) J.J. Oppenheim and M. Feldmann, eds. Academic Press, New York, p. 1899.
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