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You are here:   Home Products and Services Proteins sRANK Ligand Human E. coli
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sRANK Ligand Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:Receptor Activator for Nuclear Factor κ B Ligand, osteoprotegerin ligand, TNF-related activation-induced cytokine, soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE (TNF-related activation-induced cytokine), OPGL, ODF (Osteoclast differentiation factor)
  • Species:Human
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Cat. No. Size Price

RBG10283002 2 µg
RBG10283010 10 µg
RBG10283100 100 μg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, promote the survival of RANK + T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells, including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. 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. Human RANKL is reactive on murine cells. Recombinant Human sRANKL is a 20.0 kDa polypeptide comprising the TNF-homologous region of RANKL (176 amino acid residues).

Amino Acid Sequence

MEKAMVDGSWLDLAKRSKLEAQPFAHLTINATDIPSGSHKVSLSSWYHDRGWAKISNMTFSNGKLIVNQDGFYYLYANICFRHHETSGDLATEYLQLMVYVTKTSIKIPSSHTLMKGGSTKYWSGNSEFHFYSINVGGFFKLRSGEEISIEVSNPSLLDPDQDATYFGAFKVRDID

Source

E. coli

Purity

98%

Biological Activity

Determined by its ability to induce NF-κB in RAW264.7 cells in the absence of any cross-linking. The expected ED 50 for this effect is 10.0–25.0 ng/ml.

Endotoxin

Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at-20°C to –80°C.

Storage/Expiration

 –20°C

Summary

Research topic

Bone and cartilage metabolism, Oncology

Summary

sRANKL, receptor activator of nuclear factor (NF)-κB ligand (also: osteoprotegerin ligand, OPGL), is a part of the TNF superfamily with high similarity to other members of that protein species. (SwissProt Nr. O14788). Three isoforms are produced by alternate splicing, two type II membrane proteins (ISOFORM 1, 317 AA, and ISOFORM 3, 270 AA), and a secreted molecule (ISOFORM 2, 244 AA). ISOFORM 1 is identical to previously reported RANKL and possesses intracellular, transmembrane, and extracellular domains; ISOFORM 2 does not have the intracellular and transmembrane domains, and ISOFORM 3 does not have the intracellular domain. A soluble form arises by proteolytic processing from membrane isoforms. Although all forms are bioactive, the membrane-bound proteins seem to be the homeostatic forms, while the production of soluble RANKL signals pathological conditions. RANKL, RANK, and osteoprotegerin (OPG) have been identified as the key molecular regulation system for bone remodelling. RANKL is the main stimulatory factor for the formation of mature osteoclasts and is essential for their survival. Therefore, an increase in RANKL expression leads to bone resorption and bone loss. RANKL is produced by osteoblastic lineage cells and activated T lymphocytes. It activates its specific receptor RANK, which is located on osteoclasts and dendritic cells. The effects of RANKL are counteracted by OPG, which is secreted by various tissues and acts as an endogenous soluble receptor antagonist. Imbalances of the RANKL/OPG system have been related to the pathogenesis of Paget’s disease, benign and malignant bone tumors, postmenopausal osteoporosis, rheumatoid arthritis, bone metastases and hypercalcemia. Several studies using animal models have shown that restoring the RANKL/OPG balance (e.g. by administering OPG) reduces the severity of these disorders. Indication - Postmenopausal and senile osteoporosis - Diseases with locally increased bone resorption activity - Paget´s disease - Periodontal disease - Cardiovascular disease, arterial calcification - Inflammatory diseases - Immunological disorders - Arthritis - Oncology

Summary References (14)

References to RANKL

  • Hofbauer L.C et al. Effect of oral contraceptives on circulatingosteoprotegerin and soluble RANK ligand serum levels in healthy young women. Clin Endocrinol (2004) 60: 214–219
  • Ito S. et al. Crystal structure of the extracellular domain of mouse ligand at2.2-A resolution. J Biol Chem (2002) 22: 6631–6636.
  • Lam J. et al. Crystal structure of the TRANCE/RANKL cytokine reveals determinants of receptorligand specifity. J Clin Invest (2001) 108: 971–979.
  • Lacey D.L, et al., Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation. Cell (1998), 93:165–176.
  • Kong Y.Y. et al., OPGL is a key regulator of osteoclastogenesis, lymphocyte development and lymph-node organogenesis. Nature (1999), 397: 315–323.
  • Hsu H. et al., Tumor necrosis factor receptor family member RANK mediates osteoclast differentiation and activation induced by osteoprotegerin ligand. Proc Natl Acad Sci (1999), 96:3540–3545.
  • Josien R. et al, TRANCE, a tumor necrosis factor family member, enhances the longevity and adjuvant properties of dendritic cells in vivo. J Exp Med (2000), 191: 495–502.
  • Fuller K. et al., TRANCE is necessary and sufficient for osteoblast-mediated activation of bone resorption in osteoclasts. J Exp Med (1998), 188: 997–1001.
  • Nakashima T. et. al., Protein expression and functional difference of membrane-bound and soluble receptor activator of NF-kappaB ligand: modulation of the expression by osteotropic factors and cytokines. Biochem Biophys Res Commun (2000), 275(3):768–775.
  • Kong Y.Y. et al., Activated T cells regulate bone loss and joint destruction in adjuvant arthritis through osteoprotegerin ligand. Nature (1999), 402: 304–309.
  • Hofbauer L.C. & A.E. Heufelder, Role of receptor activator of nuclear factor-KB ligand and osteoprotegerin in bone cell biology. J Mol Med (2001), 79: 243–253.
  • Hofbauer L.C. & A.E. Heufelder, The Role of Osteoprotegerin and Receptor Activator of Nuclear Factor κB Ligand in the Pathogenesis and Treatment of Rheumatoid Arthritis. Arthritis & Rheumatism (2001), 44:253–259.
  • Hofbauer LC, et al. The role of receptor activator of nuclear factor-kappaB ligand and osteoprotegerin in the pathogenesis and treatment of metabolic bone diseases. J Clin Endocrinol Metab (2000), 85: 2355–2363.
  • Teitelbaum S.L., Bone resorption by osteoclasts. Science (2000), 289: 1504–1508.
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