Recombinant Mouse IL-5 R alpha/CD125 His-tag Protein, CF
Recombinant Mouse IL-5 R alpha/CD125 His-tag Protein, CF Summary
Product Specifications
Asp18-His339, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
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.
11367-5R
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 100 μg/mL in PBS. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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Measured by its binding ability in a functional ELISA. When Recombinant Mouse IL-5 (405-ML) is immobilized at 4.0 μg/mL (100 μL/well), Recombinant Mouse IL‑5R alpha /CD125 His-tag Protein (Catalog # 11367-5R) binds with an ED50 of 0.250-2.50 µg/mL
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2 μg/lane of Recombinant Mouse IL‑5 R alpha /CD125 His-tag Protein (Catalog # 11367-5R) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 48-54 kDa.
Reconstitution Calculator
Background: IL-5 R alpha/CD125
Interleukin‑5 Receptor alpha (IL‑5 R alpha ), also known as CD125, is a 60 kDa hematopoietin receptor that plays a dominant role in eosinophil biology (1‑3). Mature human IL‑5 R alpha consists of a 322 amino acid (aa) extracellular domain (ECD) with a WSxWS motif and a four cysteine motif, a 20 aa transmembrane segment, and a 58 aa cytoplasmic domain (4, 5). Within the ECD, mouse IL-5 R alpha shares 71% and 86% aa sequence identity with human and rat IL‑5 R alpha, respectively. Alternate splicing of human IL‑5 R alpha generates soluble secreted forms which function as IL‑5 antagonists (5‑7). The high affinity receptor for IL‑5 is a complex that consists of the ligand binding IL‑5 R alpha and the transmembrane common beta chain ( beta c/CD131) which is shared with the receptor complexes for IL‑3 and GM‑CSF (4). IL‑5 R alpha binds IL‑5 at low affinity and then associates with preformed beta c oligomers to form the signaling‑competent receptor complex (8). IL‑5 stimulation of CD34+ hematopoietic progenitor cells induces the up‑regulation of transmembrane IL‑5 R alpha followed by eosinophilic differentiation and activation (9 ‑ 11). IL‑5 R alpha also promotes the differentiation of basophils and B cells (12, 13). Exposure of mature eosinophils to IL‑5 attenuates their IL‑5 responsiveness by inducing the down‑regulation of surface IL‑5 R alpha and increased production of soluble IL‑5 R alpha (14, 15). Elevated production of IL‑5 at sites of allergic inflammation induces eosinophilia and exacerbation of immune cell infiltration, tissue damage, and remodeling (2, 3).
- Martinez-Moczygemba, M. and D.P. Huston (2003) J. Allergy Clin. Immunol. 112:653.
- Rothenberg, M.E. and S.P. Hogan (2005) Annu. Rev. Immunol. 24:147.
- Elsas, X.P. and M.I.G. Elsas (2007) Curr. Med. Chem. 14:1925.
- Tavernier, J. et al. (1991) Cell 66:1175.
- Murata, Y. et al. (1992) J. Exp. Med. 175:341.
- Tavernier, J. et al. (1992) Proc. Natl. Acad. Sci. 89:7041.
- Cameron, L. et al. (2000) J. Immunol. 164:1538.
- Zaks-Zilberman, M. et al. (2008) J. Biol. Chem. 283:13398.
- Tavernier, J. et al. (2000) Blood 95:1600.
- Clutterbuck, E.J. et al. (1989) Blood 73:1504.
- Lopez, A.F. et al. (1988) J. Exp. Med. 167:219.
- Denburg, J.A. et al. (1991) Blood 77:1462.
- Hasbold, J. et al. (2004) Nat. Immunol. 5:55.
- Gregory, B. et al. (2003) J. Immunol. 170:5359.
- Liu, L.Y. et al. (2002) J. Immunol. 169:6459.
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