Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human IL‑5 R alpha /CD125 Avi-tag His-tag (Catalog # AVI11394) binds to Recombinant Human IL-5 Protein (Catalog #
205-IL) with a ED50 of 0.030-0.300 μg/mL. |
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Source | Chinese Hamster Ovary cell line, CHO-derived human IL-5 R alpha/CD125 protein
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Accession # | |||||||
N-terminal Sequence | Asp21 |
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Structure / Form | Biotinylated via Avi-tag |
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Protein/Peptide Type | Recombinant Proteins |
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Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 40 kDa. 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 | 52-63 kDa, under reducing conditions. |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 250 μg/mL in PBS. |
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.
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Uniprot |
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