abstract |
A polypeptide dimer of two monomer fragments, the monomer fragment being composed of an extracellular position of glycoprotein (gp) 130 and a polypeptide spacer at the C-terminus having a length of 5 to 30 amino acids, The two monomer fragments are covalently linked to each other, and the spacer length determines the optimal binding of the resulting dimeric protein to the IL-6 / soluble IL-6 receptor complex, and the polypeptide dimer is homologous. A polypeptide dimer of two monomer fragments that exhibits a significantly reduced binding capacity to aggregates and molecular fragments, resulting in significantly higher production rates in host cells. |