Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is 0.04-0.15 ng/mL. |
Source | Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse IL-5 protein Met21-Gly133 |
Accession # | |
N-terminal Sequence | Met21 |
Structure / Form | Disulfide-linked homodimer |
Protein/Peptide Type | Recombinant Proteins |
Gene | Il5 |
Purity | >97%, 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. |
Dilutions |
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Theoretical MW | 13.1 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. |
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SDS-PAGE | 12-20 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Supplied as a 0.2 μm filtered solution in PBS. |
Purity | >97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Interleukin-5 (IL-5) is a secreted glycoprotein that belongs to the alpha -helical group of cytokines (1 ‑ 3). Unlike other family members, it is present as a covalently linked antiparallel dimer (4, 5). The cDNA for mouse IL‑5 encodes a signal peptide and a 113 amino acid (aa) mature protein. Mature mouse IL‑5 shares 70%, 94%, 58%, 66%, 59% and 63%, aa sequence identity with human, rat, canine, equine, feline and porcine IL-5, respectively, and shows cross-reactivity with human IL-5 receptor. IL-5 is primarily produced by CD4+ Th2 cells, but also by activated eosinophils, mast cells, EBV-transformed B cells, Reed-Sternberg cells in Hodgkin’s disease, and IL-2-stimulated invariant natural killer T cells (iNKT) (1 ‑ 3, 6 ‑ 8). IL-5 increases production and mobilization of eosinophils and CD34+ progenitors from the bone marrow and causes maturation of eosinophil precursors outside the bone marrow (1, 6, 9, 10). The receptor for human IL-5, mainly expressed by eosinophils, but also found on basophils and mast cells, consists of a unique ligand-binding subunit (IL-5 R alpha ) and a shared signal‑transducing subunit, beta c (3, 6, 11). IL-5 R alpha first binds IL-5 at low affinity, then associates with preformed beta c dimers, forming a high-affinity receptor (12). IL-5 also binds proteoglycans, potentially enhancing its activity (13). Soluble forms of IL-5 R alpha antagonize IL-5 and can be found in vivo (10, 14). In humans, IL-5 primarily affects cells of the eosinophilic lineage, and promotes their differentiation, maturation, activation, migration and survival, while in mice IL-5 also enhances Ig class switching and release from B1 cells (1 ‑ 3, 9, 10, 15, 16). IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release (17).
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