Osteoprotegerin (OPG) is a member of the TNFR superfamily that can act as a decoy receptor for RANKL. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. OPG is expressed in a wide variety of tissues including adult heart, lung, kidney, liver, spleen, prostate, lymph node and bone marrow. OPG is secreted both as a monomeric and a dimeric protein. Its primary structure consists of seven distinct domains, four of which corresponds to the extracellular cysteine-rich domains of TNFR proteins and constitutes the soluble OPG. Recombinant human OPG is a soluble 20.0 kDa protein containing 174 amino acid residues.
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