Recombinant Human Osteoprotegerin/TNFRSF11B Protein
Recombinant Human Osteoprotegerin/TNFRSF11B Protein Summary
Product Specifications
Met1-Leu401
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
6945-OS
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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6945-OS/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: Osteoprotegerin/TNFRSF11B
Osteoprotegerin (OPG), also called OCIF (osteoclastogenesis inhibitory factor) is a secreted 55-60 kDa protein that regulates bone density (1-3). As a member of the tumor necrosis factor receptor (TNFR) superfamily of proteins, it is designated TNFRSF11B (1-4). Human OPG cDNA encodes 401 amino acids (aa) including a 21 aa signal peptide and a 380 aa mature soluble protein with four TNFR domains, two death domains and a heparin-binding region (4). The cysteine-rich TNFR domains are essential for ligand interaction, while a cysteine at the C-terminus mediates homodimerization (4). Mature human OPG shares 86%, 87%, 92%, 92% and 88% amino acid sequence identity with mouse, rat, equine, canine and bovine OPG, respectively. OPG is widely expressed and constitutively released as a homodimer by mesenchymal stem cells, fibroblasts and endothelial cells (1, 2, 5, 7). Regulation of its expression by estrogen, parathyroid hormone and cytokines is complex and changes with age (2). OPG has been called a decoy receptor for the TNF superfamily ligands, TRANCE (tumor necrosis factor-related activation-induced cytokine), also called RANK L (receptor activator of NF kappa B ligand), and TRAIL (TNF-related apoptosis-inducing ligand), which also bind TNF family receptors RANK and TRAIL receptors 1-4, respectively (2, 6). TRAIL decreases the release of OPG from cells that express it, while OPG inhibits TRAIL-induced apoptosis (5, 6). Expression of RANK L on the cell surface, and thus its ability to stimulate osteoclastogenesis, is regulated by OPG by intracellular and extracellular mechanisms (7). Within osteoblasts, interaction of the basic domain of OPG with RANK L in the Golgi inhibits RANK L secretion (7). Extracellularly, OPG binding to RANK L results in
clathrin-mediated internalization and degradation of both proteins (7, 8). Binding of OPG by syndecan-1 heparin sulfates on multiple myeloma cells also results in OPG internalization and degradation, contributing to bone loss (8, 9). OPG deficiency can cause juvenile Paget’s disease in humans, and insufficient OPG to balance with RANK L and RANK can produce osteoporosis and vascular calcification in both mice and humans (2, 10, 11).
- Simonet, W.S. et al. (1997) Cell 89:309.
- Trouvin, A-P. and V. Goeb 2010) Clin. Interv. Aging 5:345.
- Yasuda, H. et al. (1998) Proc. Natl. Acad. Sci. USA 95:3597.
- Yamaguchi, K. et al. (1998) J. Biol. Chem. 273:5117.
- Corallini, F. et al. (2011) J. Cell. Physiol. 226:2279.
- Emery, J.G. et al. (1998) J. Biol. Chem. 273:14363.
- Aoki, S. et al. (2010) J. Bone Miner. Res. 25:1907.
- Tat, S.K. et al. (2006) Bone 39:706.
- Standal, T. et al. (2002) Blood 100:3002.
- Whyte, M.P. et al. (2002) N. Engl. J. Med. 347:175.
- Van Campenhout, A. and J. Golledge (2009) Atherosclerosis 204:321.
FAQs
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Why does the product insert for Recombinant Human Ostepprotergerin/TNFRSF11B, Catalog # 6945-OS, describe the protein structure as an oligomer? The protein structure is said to be a dimer in Uniprot.
Recombinant Human Ostepprotergerin/TNFRSF11B, Catalog # 6945-OS, runs as a dimer under non-reducing conditions on SDS-PAGE. In SEC analysis, however, the molecular weight determined suggested that the protein is a tetramer.
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