Key Product Details
Structure / Form
Leu20-Gly134, with a C-terminal 6-His tag
N-terminal Sequence Analysis
Predicted Molecular Mass
The ED50 for this effect is 4-16 ng/mL.
Formulation, Preparation and Storage
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in sterile 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.
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). Equine IL-5 is synthesized as a 134 amino acid (aa) precursor that contains a 19 aa signal sequence and a 115 aa mature segment. Mature equine IL-5 shares 71%, 66%, 63%, 83%, 88% and 85%, aa sequence identity with human, mouse, rat, canine, 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) (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, betac (3, 6, 11). IL-5 R alpha first binds IL-5 at low affinity, then associates with preformed betac 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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- Shakoory, B. et al. (2004) J. Interferon Cytokine Res. 24:271.
- Lalani, T. et al. (1999) Ann. Allergy Asthma Immunol. 82:317.
- Sakuishi, K. et al. (2007) J. Immunol. 179:3452.
- Clutterbuck, E. J. et al. (1989) Blood 73:1504.
- Cameron, L. et al. (2000) J. Immunol. 164:1538.
- Tavernier, J. et al. (1991) Cell 66:1175.
- Zaks-Zilberman, M. et al. (2008) J. Biol. Chem. 283:13398.
- Lipscombe, R. et al. (1998) J. Leukocyte Biol. 63:342.
- Tavernier, J. et al. (2000) Blood 95:1600.
- Kopf, M. et al. (1996) Immunity 4:15.
- Horikawa, K. and K. Takatsu (2006) Immunology 118:497.
- Denburg, J. A. et al. (1991) Blood 77:1462.
Entrez Gene IDs
Product Specific Notices for Recombinant Equine IL-5 Protein, CF
For research use only