Porcine IL‑5 Antibody

Interleukin-5 (IL-5) is a secreted disulfide-linked homodimeric glycoprotein that belongs to the alpha -helical group of cytokines that includes IL-3, IL-5 and GM-CSF (1‑3). IL-5 is primarily produced by CD4⁺ Th2 cells, but eosinophils and mast cells also produce IL-5. Porcine IL-5 is synthesized as a 134 amino acid (aa) precursor that contains a 19 aa signal sequence and a 115 aa mature segment (5). Four alpha -helices and two cysteines that form interchain disulfide bonds with a second, antiparallel IL-5 molecule are conserved among species (3-5). Monomeric IL-5 is a predicted 14 kDa protein but usage of N-linked glycosylation sites may increase its molecular weight (5). Mature porcine IL-5 shares 90%, 88%, 86%, 85%, 84%, 66%, 68%, 63%, 63% and 59% aa sequence identity with mature bovine, sheep, cat, equine, canine, human, guinea pig, cotton rat, murine and rat IL-5, respectively. Recombinant porcine IL-5 induced proliferation in the human TF-1 cell line (5). The receptor for human IL-5 consists of a 60 kDa ligand-binding subunit (IL-5 R alpha ) and a 120 kDa signal-transducing subunit ( beta _c). It is suggested that dimeric IL-5 binding to IL-5 R alpha recruits beta _c, which subsequently covalently links with IL-5 R alpha. Two receptor complexes then associate to form the physiologic IL-5 receptor (6, 7). IL-5 binds proteoglycans, potentially enhancing its activity (8). Following receptor binding, IL-5 promotes the maturation, activation and migration of eosinophils, as demonstrated during asthmatic eosinophilic lung inflammation (1‑3). It also mobilizes eosinophils and CD34⁺ progenitors from marrow. It also enhances Ig release from B cells and contributes to IL-4 production. Finally, it primes basophils for histamine and leukotriene release (1, 2, 9).