Human IL-10 Biotinylated Antibody

Interleukin 10, also known as cytokine synthesis inhibitory factor (CSIF), is the charter member of the IL-10 family of alpha-helical cytokines that also includes IL-19, IL‑20, IL-22, IL-24, and IL-26/AK155 (1, 2). IL-10 is secreted by many activated hematopoietic cell types as well as hepatic stellate cells, keratinocytes, and placental cytotrophoblasts (2‑5). Mature human IL-10 shares 72% - 86% amino acid sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat IL-10. Whereas human IL-10 is active on mouse cells, mouse IL-10 does not act on human cells (6, 7). IL-10 is a 178 amino acid molecule that contains two intrachain disulfide bridges and is expressed as a 36 kDa noncovalently associated homodimer (6, 8, 9). The IL-10 dimer binds to two IL-10 R alpha/IL-10 R1 chains, resulting in recruitment of two IL-10 R beta/IL-10 R2 chains and activation of a signaling cascade involving JAK1, TYK2, and STAT3 (10). IL-10 R beta does not bind IL-10 by itself but is required for signal transduction (1). IL-10 R beta also associates with IL‑20 R alpha, IL-22 R alpha, or IL-28 R alpha to form the receptor complexes for IL-22, IL-26, IL-28, and IL‑29 (11‑13). IL-10 is a critical molecule in the control of viral infections and allergic and autoimmune inflammation (14‑16). It promotes phagocytic uptake and Th2 responses but suppresses antigen presentation and Th1 proinflammatory responses (2).