Human IL-4 PE-conjugated Antibody

Interleukin-4 (IL-4), also known as B cell-stimulatory factor-1, is a monomeric, approximately 13-18 kDa Th2 cytokine that shows pleiotropic effects during immune responses (1-3). It is a glycosylated polypeptide that contains three intrachain disulfide bridges and adopts a bundled four alpha-helix structure (4). Human IL-4 is synthesized with a 24 aa signal sequence. Alternate splicing generates an isoform with a 16 aa internal deletion. Mature human IL-4 shares 55%, 39%, and 43% aa sequence identity with bovine, mouse, and rat IL-4, respectively. Human, mouse, and rat IL-4 are species-specific in their activities (5-7). IL-4 exerts its effects through two receptor complexes (8, 9). The type I receptor, which is expressed on hematopoietic cells, is a heterodimer of the ligand binding IL-4 R alpha and the Common gamma Chain (a shared subunit of the receptors for IL-2, -7, -9, -15, and -21). The type II receptor on non-hematopoietic cells consists of IL-4 R alpha and IL-13 R alpha1. The type II receptor also transduces IL-13 mediated signals. IL-4 is primarily expressed by Th2-biased CD4⁺ T cells, mast cells, basophils, and eosinophils (1, 2). It promotes cell proliferation, survival, and immunoglobulin class switch to IgG4 and IgE in human B cells, acquisition of the Th2 phenotype by naïve CD4⁺ T cells, priming and chemotaxis of mast cells, eosinophils, and basophils, and the proliferation and activation of epithelial cells (10-13). IL-4 plays a dominant role in the development of allergic inflammation and asthma (12, 14).