Recombinant Mouse IL-3R alpha/CD123 Fc Chimera Protein, CF Summary
|Mouse IL-3 R alpha
Accession # P26952
|IEGRID||Human IgG1 |
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in sterile PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: IL-3R alpha
The IL-3 receptor chain (IL‑3 R alpha ; also SUT-1 and CD123) is a 60‑70 kDa member of the class I cytokine receptor family of proteins (1, 2, 3). Members of this class are type I transmembrane proteins that contain two fibronectin type III (FNIII) modules and a distinctive Trp‑Ser‑x‑Trp‑Ser peptide motif in the extracellular domain. This is in contrast to class II receptors that share the same fibronectin domains but lack both the WSxWS motif and analogous cysteine spacings. Mouse IL‑3 R alpha is synthesized as a 396 amino acid (aa) precursor that contains a 16 aa signal sequence, a 315 aa extracellular region, a 24 aa transmembrane segment, and a 41 aa cytoplasmic tail (3, 4). The molecule is expressed on multiple cell types, including endothelial cells (5), monocytes (6), eosinophils (7), basophils plus mast cells (8), and plasmacytoid CD4+ T cells (9). IL‑3 R alpha serves as a low affinity binding protein for 24‑28 kDa monomeric IL‑3 (1, 3, 4, 10, 11). Following binding, the IL‑3:IL‑3 R alpha complex likely interacts with a preformed signaling homodimer comprised of either 120 kDa AIC2A (= beta IL-3) or 130 kDa AIC2B (= beta c) chains. This tetramer appears to recruit one more IL‑3:IL‑3 R alpha complex, generating a fully functional hexamer (1, 3, 4, 12, 13). Signaling is mediated by receptor‑associated cytoplasmic kinases, as class I cytokine receptors do not possess intrinsic kinase activity. Notably, the IL‑3 R complex may not exist as a singularity, but actually form higher‑order complexes with FcR gamma, beta 1 integrin, and VEGF R2 (1). There are at least two IL‑3 Ra isoform variants in mouse. One is found in the AKR and A/J strains, and shows a deletion of aa 274‑283. This is not present at the cell membrane (14). The second (called SP2) shows a deletion of aa 20‑112, generating a 50‑55 kDa membrane form that binds IL‑3, but will only signal through beta IL-3 (15, 16). IL‑3’s choice of full‑length IL‑3 R alpha (SP1) or SP2 leads to different signaling outcomes, presumably due to the engagement of different binding sites on beta IL-3. The extracellular domain of mouse IL‑3 R alpha /SP1 shares only 44% and 29% aa sequence identity with rat and human IL‑3 R alpha, respectively. Nevertheless, human IL‑3 is reported to be active on the mouse receptor complex that is expressed on select cell types (17).
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Citation for Recombinant Mouse IL-3R alpha/CD123 Fc Chimera Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Interfering with multimerization of netrin-1 receptors triggers tumor cell death.
Authors: Mille F, Llambi F, Guix C, Delloye-Bourgeois C, Guenebeaud C, Castro-Obregon S, Bredesen DE, Thibert C, Mehlen P
Cell Death Differ., 2009;16(10):1344-51.
Sample Types: Whole Cells
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