Mouse IL-20 Biotinylated Antibody

Mouse Interleukin 20 (IL-20) was identified by searching sequence databases for translated sequences with a signal sequence and amphipathic helices found in helical cytokines. Based on the human molecule, mouse IL-20 was discovered in a skin library. Mouse IL-20 is synthesized as a 176 amino acid (aa) precursor that contains a 24 aa signal sequence and a 152 aa mature segment. There are no N-linked glycosylation sites and it is doubtful that the native molecule is glycosylated. Although IL-20 is a distant member of the IL-10 family, it functions as a monomer. IL-20 shares less than 40% aa sequence identity with other IL-10 family members. Mouse and human IL-20 are 77% aa identical in the mature segment. IL-20 production has been found in skin and trachea. In particular, activated keratinocytes and, possibly, monocytes are reported to express IL-20. There are two heterodimeric receptor complexes for IL-20. The first complex is composed of IL-20 R alpha and IL‑20 R beta. The second complex is composed of IL-22 R and IL‑20 R beta. Whereas the IL‑22 R/IL‑20 R beta complex is shared with IL-24/mda-7, the IL‑20 R alpha/IL‑20 R beta complex is shared with both IL-19 and IL-24. Little is known about the function of IL-20. It is reported to induce the proliferation of multipotential hematopoietic progenitor cells, direct the differentiation and expansion of keratinocytes, and promote the release of proinflammatory mediators in keratinocytes and other IL-20 receptor expressing cells (1‑6).