Glycoprotein 130 (gp130, also known as IL6ST, CD130 or IL6-beta) is a ubiquitously expressed, signal-transducing receptor that serves as the signal transduction unit for IL-6 family of cytokines, including IL-6, IL-11, IL-27, leukemia inhibitory factor (LIF), OSM, ciliary neurotrophic factor (CNTF), cardiotrophin 1 (CT-1), and cardiotrophin-like cytokine (CLC). These cytokines signal through the gp130/Jak/STAT pathway. Binding of IL-6 to IL-6R induces gp130 homodimerization and formation of a high-affinity receptor complex, which activates Jaks. That causes phosphorylation of gp130 tyrosine residues which in turn activates STAT3. gp130 is a type I transmembrane protein, and can also exist as a soluble form (sgp130). sgp130 binds to sIL-6R/IL-6 complexes and prevents their interactions with membrane-anchored gp130 on target cells.