Description
Interleukin-5 (IL-5) is a secreted glycoprotein that belongs to the alpha -helical group of cytokines. Unlike other family members, it is present as a covalently linked antiparallel dimer. The cDNA for rat IL-5 encodes a signal peptide and a 113 amino acid (aa) secreted mature protein. Mature rat IL-5 shares 70%, 94%, 56%, 63%, 59% and 59%, aa sequence identity with human, mouse, canine, equine, feline and porcine IL-5, respectively. 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). 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. 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. IL-5 R alpha first binds IL-5 at low affinity, then associates with preformed beta c dimers, forming a high-affinity receptor. IL-5 also binds proteoglycans, potentially enhancing its activity. Soluble forms of IL-5 R alpha antagonize IL-5 and can be found in vivo. 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. IL-5 also promotes differentiation of basophils and primes them for histamine and leukotriene release.
Product Properties
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Synonyms |
B-cell Differentiation Factor I, Eosinophil Differentiation Factor, TRF |
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Accession |
Q08125 |
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GeneID |
Rn.44227. |
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Source |
E.coli-derived Rat IL-5, Met20-Val132, with an N-terminal Met. |
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Molecular Weight |
Approximately 26.2 kDa. |
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AA Sequence |
MEIPMSTVVK ETLIQLSTHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEILFQNL SLIKKYIDGQ KEKCGEERRK TRHFLDYLQE FLGVMSTEWA MEV |
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Tag |
None |
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Physical Appearance |
Sterile Filtered White lyophilized (freeze-dried) powder. |
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Purity |
> 98% by SDS-PAGE and HPLC analyses. |
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Biological Activity |
The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.5 ng/mL, corresponding to a specific activity of > 2.0 × 106 IU/mg. Fully biologically active when compared to standard. |
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Endotoxin |
< 1.0 EU per 1μg of the protein by the LAL method. |
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Formulation |
Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4. |
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Reconstitution |
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions. |
Shipping and Storage
The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year.
Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.
Cautions
1. Avoid repeated freeze-thaw cycles.
2. For your safety and health, please wear lab coats and disposable gloves for operation.
3. For research use only!