Human IL-10 R beta PE-conjugated Antibody

IL-10 R beta, 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) type I transmembrane precursor protein with a 20 aa signal sequence, a 200 aa extracellular region, a 29 aa transmembrane segment and a 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.