Human IL‑22BP Antibody

Interleukin 22 Binding Protein (IL-22BP), also known as Cytokine Receptor Family (CRF) 2‑10, CRF2-X, and IL-22 RA2, is a secreted glycoprotein belonging to the type II cytokine receptor family. It encodes a precursor protein of 231 amino acid (aa) residues with a 21 aa putative signal peptide and five potential N-linked glycosylation sites. IL-22BP lacks a transmembrane and cytoplasmic domain and is most closely related to the extracellular domains of IL‑22 R (CRF2-9) and IL-20 R (CRF2-8), sharing 33% and 34% aa sequence identity, respectively. It also shares sequence homology with the extracellular domains of IL-10 R (29%), IL-10 R beta (30%), the IFN receptors (23‑25%) and tissue factor (26%). IL-22BP antagonizes IL-22 activity by specifically binding IL-22 with high affinity and blocking its interaction with the cell surface IL-22 receptor heteromeric complex composed IL-22 R and IL‑20 R. IL-22BP is expressed in multiple tissues. The highest levels of expression are found in breast, lungs and colon. The major cell types producing IL-22BP are monocytes, activated B cells and epithelial cells (1), and is constitutively expressed by a subset of conventional dendritic cells (2). IL-22BP is regulated by the inflammasome and it has been suggested to modulate tumorigenesis in the intestine (3).