Recombinant Equine IL-5 Protein

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).