Recombinant Mouse IL-3R alpha/CD123 Fc Chimera Protein, CF

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse IL-3R alpha/CD123 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its ability to inhibit the IL-3-induced proliferation of NFS‑60 mouse myelogenous leukemia lymphoblast cells. The ED₅₀ for this effect is 0.03‑0.15 µg/mL in the presence of 2.5 µg/mL Recombinant Mouse IL‑3 R beta Fc Chimera (Catalog # 549‑R3) and 2 ng/mL of Recombinant Mouse IL‑3 (Catalog # 403‑ML).
• Source: Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse IL-3 R alpha/CD123 protein
  

  Mouse IL-3 R alpha (Ser17-Lys331) Accession # P26952	IEGRID	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: P26952
• N-terminal Sequence: Ser17
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: Il3ra
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 61.0 kDa (monomer).
  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.
• SDS-PAGE: 70-80 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse IL-3R alpha/CD123 Fc Chimera Protein, CF

• CD123 antigen
• CD123
• hIL3Ra
• hIL-3Ra
• IL-3 R alpha
• IL-3 receptor subunit alpha
• IL3R alpha
• IL-3R alpha
• IL-3R subunit alpha
• IL3R
• IL3RA
• IL-3Ra
• IL-3R-alpha
• IL3RAY
• IL3RX
• IL3RY
• interleukin 3 receptor, alpha (low affinity)
• interleukin-3 receptor subunit alpha
• MGC34174

Background

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).

1. Broughton, S.E. et al. (2012) Immunol. Rev. 250:277.
2. Langer, J.A. et al. (2004) Cytokine Growth Factor Rev. 15:33.
3. Miyajima, A. et al. (1993) Blood 82:1960.
4. Hara, T. & A. Miyajima (1992) EMBO J. 11:1875.
5. Korpelainen, E.I. et al. (1993) Proc. Natl. Acad. Sci. USA 90:11137.
6. Ebner, S. et al. (2002) J. Immunol. 168:6199.
7. Gregory, B. et al. (2003) J. Immunol. 170:5359.
8. Dahl, C. et al. (2004) Allergy 59:1087.
9. Grouard, G. et al. (1997) J. Exp. Med. 185:1101.
10. Clark-Lewis, I. et al. (1984) J. Biol. Chem. 259:7488.
11. Knepper, T.P. et al. (1992) Biochemistry 31:11651.
12. Ogorochi, T. et al. (1992) Blood 79:895.
13. Murphy, J.M. et al. (2004) J. Biol. Chem. 279:26500.
14. Ichihara, M. et al. (1995) EMBO J. 14:939.
15. Chen, J. et al. (2009) J. Biol. Chem. 284:5763.
16. Mirza, S. et al. (2010) J. Biol. Chem. 285:22370.
17. Dentelli, P. et al. (1999) J. Immunol. 163:2151.

Publications for IL-3R alpha/CD123 (983-MR)(1)

Publication using 983-MR

• Mille F, Llambi F, Guix C, Delloye-Bourgeois C, Guenebeaud C, Castro-Obregon S, Bredesen DE, Thibert C, Mehlen P Interfering with multimerization of netrin-1 receptors triggers tumor cell death. Cell Death Differ., 2009-06-19;16(10):1344-51. 2009-06-19 [PMID: 19543238] (Bioassay, Mouse)

Bioinformatics

• Gene Symbol: Il3ra
• Uniprot:
  • P26952()