Recombinant Mouse Osteoprotegerin/TNFRSF11B Fc Chimera, CF

R&D Systems, part of Bio-Techne | Catalog # 459-MO

R&D Systems, part of Bio-Techne
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459-MO-100
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Key Product Details

Source

NS0

Accession #

Q6PI12

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

View all Osteoprotegerin/TNFRSF11B Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived mouse Osteoprotegerin/TNFRSF11B protein
Mouse OPG
Glu22-Leu401 (Gln138Arg)
Accession # Q6PI12		 IEGRMD Human IgG1
(Pro100-Lys330)
(Thr276Ala)		 6-His tag
N-terminus C-terminus

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Glu22

Predicted Molecular Mass

70.9 kDa (monomer)

SDS-PAGE

85-95 kDa, reducing conditions

Activity

Measured by its ability to inhibit TRAIL-mediated cytotoxicity using L-929 mouse fibroblast cells treated with TRAIL.
The ED50 for this effect is 3-15 ng/mL in the presence of 12 ng/mL of cross-linked Recombinant Human TRAIL/TNFSF10 (Catalog #s 375-TL and MAB050).

Reviewed Applications

Read 1 review rated 5 using 459-MO in the following applications:

Formulation, Preparation and Storage

459-MO
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 100 μg/mL in sterile PBS.

Reconstitution Buffer Available:
Size / Price
Qty
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.
  • 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.

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). Mouse 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 mouse OPG shares 86%, 94%, 86%, 86% and 83% amino acid sequence identity with human, 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 kappaB 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).

References

  1. Simonet, W.S. et al. (1997) Cell 89:309.
  2. Trouvin, A-P. and V. Goeb 2010) Clin. Interv. Aging 5:345.
  3. Yasuda, H. et al. (1998) Proc. Natl. Acad. Sci. USA 95:3597.
  4. Yamaguchi, K. et al. (1998) J. Biol. Chem. 273:5117.
  5. Corallini, F. et al. (2010) J. Cell. Physiol. Dec. 6 [Epub ahead of print].
  6. Emery, J.G. et al. (1998) J. Biol. Chem. 273:14363.
  7. Aoki, S. et al. (2010) J. Bone Miner. Res. 25:1907.
  8. Tat, S.K. et al. (2006) Bone 39:706.
  9. Standal, T. et al. (2002) Blood 100:3002.
  10. Whyte, M.P. et al. (2002) N. Engl. J. Med. 347:175.
  11. Van Campenhout, A. and J. Golledge (2009) Atherosclerosis 204:321.

Alternate Names

OCIF, TNFRSF11B

Entrez Gene IDs

4982 (Human); 18383 (Mouse)

Gene Symbol

TNFRSF11B

UniProt

Q6PI12

Additional Osteoprotegerin/TNFRSF11B Products

Product Documents for Recombinant Mouse Osteoprotegerin/TNFRSF11B Fc Chimera, CF

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