OPG Human, HEK
HEK293 Cells.
Greater than 90.0% as determined by SDS-PAGE.
Description
OPG Human Recombinant is a single, glycosylated polypeptide chain containing 393 amino acids (22-401a.a) and having a molecular mass of 45.0kDa (calculated). OPG is fused to a 13 a.a FLAG- tag at N-terminal.
Product Specs
HEK293 Cells.
PGDYKDDDDKPAGETFPPKYLHYDEETSHQLLCDKCPPGTYLKQHCTAKWKTVCAPCPDHYYTDSWHTSDECLYC
SPVCKELQYVKQECNRTHNRVCECKEGRYLEIEFCLKHRSCPPGFGVVQAGTPERNTVCKRCPDGFFSNETSSKAP
CRKHTNCSVFGLLLTQKGNATHDNICSGNSESTQKCGIDVTLCEEAFFRFAVPTKFTPNWLSVLVDNLPGTKVNAESV
ERIKRQHSSQEQTFQLLKLWKHQNKDQDIVKKIIQDIDLCENSVQRHIGHANLTFEQLRSLMESLPGKKVGAEDIEK
TIKACKPSDQILKLLSLWRIKNGDQDTLKGLMHALKHSKTYHFPKTVTQSLKKTIRFLHSFTMYKLYQKLFLEMIGNQ
Product Science Overview
Osteoprotegerin (OPG), also known as osteoclastogenesis inhibitory factor (OCIF) or tumor necrosis factor receptor superfamily member 11B (TNFRSF11B), is a cytokine receptor that plays a crucial role in bone metabolism. It is a member of the tumor necrosis factor (TNF) receptor superfamily and is encoded by the TNFRSF11B gene .
The OPG protein consists of seven distinct domains, four of which correspond to the extracellular cysteine-rich domains of TNF receptor proteins. This structure allows OPG to function as a soluble decoy receptor for receptor activator of nuclear factor kappa-B ligand (RANKL) . OPG is expressed in a wide variety of tissues, including the heart, lung, kidney, liver, spleen, prostate, lymph nodes, and bone marrow .
OPG’s primary function is to inhibit osteoclastogenesis, the process by which osteoclasts (bone-resorbing cells) are formed. It achieves this by binding to RANKL, preventing RANKL from interacting with its receptor RANK on the surface of osteoclast precursors. This inhibition is crucial for maintaining bone density and preventing excessive bone resorption .
In addition to its role in bone metabolism, OPG also binds to TNF-related apoptosis-inducing ligand (TRAIL) and inhibits TRAIL-induced apoptosis in specific cells, including tumor cells . Other ligands for OPG include syndecan-1, glycosaminoglycans, von Willebrand factor, and the factor VIII-von Willebrand factor complex .
Recombinant OPG is produced using various expression systems, including Escherichia coli (E. coli) and human embryonic kidney (HEK) cells. The recombinant OPG expressed in HEK cells is particularly significant because HEK cells provide a more human-like post-translational modification, which can be crucial for the protein’s stability and function in therapeutic applications .
