Sclerostin (human, recombinant)

Sclerostin is a secreted glycoprotein and a member of the DAN/Cerberus protein family involved in Wnt signaling in bone. It contains a cystine-knot motif and heparin binding site and is expressed by osteocytes and cementocytes. Sclerostin competes with Wnt ligands for binding to LDL receptor-related protein 5/6 (LRP5/6), where it acts as a Wnt inhibitor and inhibits osteoblast activity. It also acts as an antagonist against several members of the bone morphogenetic protein (BMP) family. Inhibition of sclerostin via monoclonal antibodies increases bone mineral density in mice. Loss-of-function mutations in the gene encoding sclerostin, SOST, are associated with sclerosteosis, craniodiaphyseal dysplasia (CDD), and van Buchem disease. Formulations containing a monoclonal antibody against sclerostin have been used in the treatment of osteoporosis. Cayman's Sclerostin (human, recombinant) protein can be used for binding assays. This protein consists of 197 amino acids and has a calculated molecular weight of 22. kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 30 kDa due to glycosylation.