TNFRSF11B/OPG Protein, Human (CHO, Fc)

Osteoprotegerin (OPG), a TNF receptor superfamily, is expressed in many tissues including heart, kidney, liver, spleen, and bone marrow. Osteoprotegerin has osteoprotective effect and is critical in bone remodeling. Osteoprotegerin can bind to RANKL and inhibit the binding between TNFSF11 and RANKL, thereby neutralizing the RANKL function in osteoclastogenesis^[1]. OPG is also involved in multiple biological processes of cancers. TNFRSF11B/OPG Protein, Human (CHO, Fc) is a recombinant human TNFRSF11B/OPG (E22-L201) with C-terminal hFc tag, which is produced in CHO cell^[1][2].

Osteoprotegerin (OPG), a glycoprotein, belongs to TNF receptor superfamily. OPG is expressed in many tissues besides osteoblasts, including heart, kidney, liver, spleen, and bone marrow. Human osteoprotegerin shares <85% aa sequence identity with mouse and rat. Mouse OX40 shares 94.5% aa sequence identity with rat^[1].
Osteoprotegerin can bind to RANKL and inhibit the binding between TNFSF11 and RANKL, thereby neutralizing the RANKL function in osteoclastogenesis. Osteoprotegerin also protects large blood vessels from medial calcification. Increased osteoprotegerin levels have been consistently associated with the incidence and prevalence of coronary artery disease^[1][3]. Osteoprotegerin is also involved in multiple processes of cancers, such as tumor survival, epithelial to mesenchymal transition (EMT), neo-angiogenesis, invasion, and metastasis^[2].
Osteoprotegerin plays a critical role in bone remodeling, and has osteoprotective effect^[1].

RANKL (human, 0-100 pg/mL, 36 h) promotes the proliferation of VSMC^[5].

Osteoprotegerin (human, 5 mg/kg, i.v.) shows antiresorptive effects in rats^[4].

Human

CHO

C-hFc

O00300 (E22-L201)

4982  [NCBI]

Partial

ETFPPKYLHYDEETSHQLLCDKCPPGTYLKQHCTAKWKTVCAPCPDHYYTDSWHTSDECLYCSPVCKELQYVKQECNRTHNRVCECKEGRYLEIEFCLKHRSCPPGFGVVQAGTPERNTVCKRCPDGFFSNETSSKAPCRKHTNCSVFGLLLTQKGNATHDNICSGNSESTQKCGIDVTL

Approximately 50-80 kDa, based on SDS-PAGE under reducing conditions.

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Boyce BF, et al. Biology of RANK, RANKL, and osteoprotegerin. Arthritis Res Ther. 2007;9 Suppl 1(Suppl 1):S1.  [Content Brief]

  [2]. Simonet WS, et al. Osteoprotegerin: a novel secreted protein involved in the regulation of bone density. Cell. 1997 Apr 18;89(2):309-19.  [Content Brief]

  [3]. Wang Y, et al. The roles of osteoprotegerin in cancer, far beyond a bone player. Cell Death Discov. 2022 May 6;8(1):252.  [Content Brief]

  [4]. Udagawa N, et al. Osteoprotegerin produced by osteoblasts is an important regulator in osteoclast development and function. Endocrinology. 2000 Sep;141(9):3478-84.  [Content Brief]

  [5]. Venuraju SM, et al. Osteoprotegerin as a predictor of coronary artery disease and cardiovascular mortality and morbidity. J Am Coll Cardiol. 2010 May 11;55(19):2049-61.  [Content Brief]

  [6]. Baud'huin M, et al. Osteoprotegerin: multiple partners for multiple functions. Cytokine Growth Factor Rev. 2013 Oct;24(5):401-9.  [Content Brief]

  [7]. Capparelli C, et al. Sustained antiresorptive effects after a single treatment with human recombinant osteoprotegerin (OPG): a pharmacodynamic and pharmacokinetic analysis in rats. J Bone Miner Res. 2003 May;18(5):852-8.  [Content Brief]

  [8]. Candido R, et al. Human full-length osteoprotegerin induces the proliferation of rodent vascular smooth muscle cells both in vitro and in vivo. J Vasc Res. 2010;47(3):252-61.  [Content Brief]