IL3RA Research Reagents

Interleukin-3 receptor subunit alpha is a protein in humans that is encoded by IL3RA gene. This is a receptor for interleukin-3.

The following IL3RA reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

IL3RA Antibodies

IL3RA Antibodies for Homo sapiens (Human)

IL3RA Proteins

IL3RA Proteins for Homo sapiens (Human)

IL3RA Proteins for Mus musculus (Mouse)

IL3RA Background

Interleukin-3 receptor alpha chain (IL3RA), also known as CD123 (Cluster of Differentiation 123), is one of the two subunits of heterodimeric human IL-3R [1]. The IL-3 receptor was first described on murine bone marrow cells. IL3RA belongs to a member of the cytokine receptor superfamily [2] but is more closely related to the GM-CSF receptor alpha chain (GM-CSFRA) and IL-5RA chains [3]. The expression of both IL3RA and beta subunit IL3RB, the other IL-3R chain, is necessary for triggering signalling and cellular proliferation in response to IL-3 [4]. Human IL-3 induces heterodimerization of IL-3R alpha and beta subunit IL3RB and that disulfide linkage of these chains is involved in receptor activation but not high-affinity binding [5]. Interaction between the human IL-3R and IL-3 triggers a variety of cellular signals leading to the preservation of cell viability, proliferation, and differentiation of hemopoietic cells against apoptosis [6][7]. Yao Tong et al. revealed the IL3RA is targeted for ubiquitination and degradation by the E3 ligase RNFT2 (RING finger transmembrane-domain containing protein 2, also TMEM118) and identifyied IL3RA Lys357 as a critical residue regulating IL3RA stability [8]. In vitro, IL3 promotes RNFT2-dependent IL3RA proteasomal degradation, an effect mitigated by LPS-priming. No mutations of the IL3RA gene have been reported in hematological and non hematological human malignancies [9]. Increased IL3RA expression has been reported in about 45% of patients with acute myeloid leukemia [10] and in 40% of patients with acute B lymphoid leukemia.

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[2] Bazan, J. F. Structural design and molecular evolution of a cytokinereceptor superfamily [J]. Proc. Natl. Acad. Sci. USA 1990, 87:6934-6938.
[3] Goodall G. J., C. J. Bagley, et al. A model for the interaction of the GM-CSF, IL-3 and IL-5 receptors with their ligands [J]. Growth Factors 1993, 8:87-97.
[4] Kitamura T., and A. Miyajima. Functional reconstitution of the human interleukin-3 receptor [J]. Blood 1992, 80:84-90.
[5] F C Stomski, Q Sun, et al. Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity binding [J]. MOLECULAR AND CELLULAR BIOLOGY, June 1996, 3035-3046.
[6] Clark, S. C., et al. The human hematopoietic colony-stimulating factors [J]. Science 1987, 236:1229-1237.
[7] Metcalf D. The molecular control of cell division, differentiation commitment and maturation in haemopoietic cells [J]. Nature (London) 1989, 339:27-30.
[8] Yao Tong, Travis B. Lear, et al. The RNFT2/IL3Ra axis regulates IL3 signaling and innate immunity [J]. JCI Insight. 2020;5(3):e133652.
[9] Muñoz L, Nomdedéu JF, et al. Interleukin-3 receptor alpha chain (CD123) is widely expressed in hematologic malignancies. Haematologica. 2001 ; 86 (12) : 1261-1269.
[10] Riccioni R, Rossini A, et al. Immunophenotypic features of acute myeloid leukemias overexpressing the interleukin 3 receptor alpha chain [J]. Leukemia & lymphoma. 2004 ; 45 (8) : 1511-1517.

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