Recombinant Human Osteoprotegerin/TNFRSF11B Protein, CF Summary
Additional Information
A New and Improved rh OPG is Now Available! The new protein has ~2 fold better activity!
Details of Functionality
Measured by its ability to inhibit TRAIL-mediated cytotoxicity using L‑929 mouse fibroblast cells treated with TRAIL. The ED50 for this effect is 8‑24 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human Osteoprotegerin/TNFRSF11B protein Glu22-Leu401
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
43.5 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
55 kDa, reducing conditions
Publications
Read Publications using 185-OS/CF in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Osteoprotegerin/TNFRSF11B Protein, CF
OCIF
OCIFMGC29565
OPG
OPGtumor necrosis factor receptor superfamily member 11B
Osteoclastogenesis inhibitory factor
Osteoprotegerin
TNFRSF11B
TR1
tumor necrosis factor receptor superfamily, member 11b
Background
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. (2010) J. Cell. Physiol. Dec. 6 [Epub ahead of print].
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.
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