Recombinant Human IL-5 R alpha/CD125 Avi-tag His Protein, CF
Recombinant Human IL-5 R alpha/CD125 Avi-tag His Protein, CF Summary
Product Specifications
| Human IL-5 R alpha (Asp21-Glu335) Accession # Q01344.2 | Avi-tag | 6-His tag |
| N-terminus | C-terminus | |
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.
AVI11394
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 250 μg/mL in 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.
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Scientific Data
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Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human IL-5 R alpha /CD125 Avi-tag His-tag Protein (Catalog # AVI11394) binds to Recombinant Human IL-5 Protein (205-IL) with a ED50 of 0.030 -0.300 μg/mL.
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2 μg/lane of Biotinylated Recombinant Human IL‑5 R alpha /CD125 Avi-tag His-tag Protein (Catalog # AVI11394) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 52-63 kDa, under reducing conditions.
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, human IL-5 R alpha shares 71% aa sequence identity with mouse and rat IL‑5 R alpha. 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). Our Avi-tag Biotinylated human IL-5 R alpha Fc chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- 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.
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- 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.
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- 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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