Human IL-10 R beta Biotinylated Antibody

IL-10, also known as IL-10 R2, mediates its biological activities via binding to a heteromeric receptor complex consisting of two distinct type II cytokine receptor subunits, the ligand binding IL-10 R alpha and the IL-10 R beta which does not bind IL-10 by itself but is required for signal transduction. The cDNA for human IL-10 R beta encodes a 325 amino acid (aa) residue type I transmembrane precursor protein with a 20 aa signal sequence, a 200 aa extracellular region, a 29 aa transmembrane segment, and a short 76 aa cytoplasmic domain. Within the extracellular region, there are two 100 aa subdomains that resemble the constant region of immunoglobulins. This structural motif is responsible for the alternative designation of IL-10 R beta as CRF2-4 (the 4^th member of the cytokine receptor family class II/2). Human and mouse IL-10 R beta share approximately 69% aa sequence identity. Binding of the non-covalent IL-10 dimer to two IL-10 R alpha chains recruits two IL‑10 R beta chains resulting in the activation and phosphorylation of the signaling cascade involving JAK1, TYK2, and STAT3. IL-10 R beta is expressed ubiquitously. IL‑10 R beta is also a component of the IL-22 receptor complex consisting of the IL-10 R beta chain and IL-22 R, another type II cytokine receptor family member.