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

R&D Systems, part of Bio-Techne | Catalog # 983-MR

R&D Systems, part of Bio-Techne
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983-MR-100
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Key Product Details

Source

Sf 21 (baculovirus)

Accession #

P26952

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

View all IL-3R alpha Proteins and Enzymes »

Product Specifications

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

Purity

>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Ser17

Predicted Molecular Mass

61.0 kDa (monomer)

SDS-PAGE

70-80 kDa, reducing conditions

Activity

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).

Formulation, Preparation and Storage

983-MR
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 100 μg/mL in sterile PBS.

Reconstitution Buffer Available:
Size / Price
Qty
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.
  • 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.

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 (= betaIL-3) or 130 kDa AIC2B (= betac) 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, beta1 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 betaIL-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 betaIL-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).

References

  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.

Long Name

Interleukin 3 Receptor alpha

Alternate Names

CD123, IL-3 R alpha, IL-3Ra, IL3R alpha, IL3RA

Entrez Gene IDs

3563 (Human); 16188 (Mouse); 102138639 (Cynomolgus Monkey)

Gene Symbol

IL3RA

UniProt

P26952

Additional IL-3R alpha Products

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

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Product Specific Notices for Recombinant Mouse IL-3R alpha/CD123 Fc Chimera Protein, CF

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