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Growth Factors & Cytokines

Recombinant Human OPG

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Detalles del Producto

Nùmero de Catalogo 450-14
Descripcion
Recombinant Human OPG

Osteoprotegerin (OPG) is a member of the TNFR superfamily that can act as a decoy receptor for RANKL.  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.  OPG is expressed in a wide variety of tissues, including the adult heart, lung, kidney, liver, spleen, prostate, lymph node, and bone marrow.  OPG is secreted both as a monomeric and a dimeric protein.  Its primary structure consists of seven distinct domains, four of which correspond to the extracellular cysteine-rich domains of TNFR proteins and constitute the soluble OPG.  Recombinant Human OPG is a soluble 20.0 kDa protein containing 174 amino acid residues.

Source: E.coli

Synonyms: TNFRSF11B, Osteoprotegerin, OCIF (osteoclastogenesis inhibitory factor), TR1

AA Sequence: METFPPKYLH YDEETSHQLL CDKCPPGTYL KQHCTAKWKT VCAPCPDHYY TDSWHTSDEC LYCSPVCKEL QYVKQECNRT HNRVCECKEG RYLEIEFCLK HRSCPPGFGV VQAGTPERNT VCKRCPDGFF SNETSSKAPC RKHTNCSVFG LLLTQKGNAT HDNICSGNSE STQK

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to inhibit TRAIL-induced apoptosis of LN-18 glioblastoma cells.

Calculated Molecular Weight: 20 kDa

Accession Number: O00300

Gene ID: 4982

Endotoxin: Endotoxin level is < 0.1 ng/ug of protein (< 1 EU/ug)

crossreactivity:
Country Of Origin: USA

Not for human use.

Research Interest

product.subtitle.recentcitations

Primer autor
Brito, H O
Titulo
Immune-mediated febrile response in female rats: Role of central hypothalamic mediators.
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Scientific Reports; 10(1) pg4073
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Primer autor
Gooding, S
Titulo
Transcriptomic profiling of the myeloma bone-lining niche reveals BMP signalling inhibition to improve bone disease.
Citar
Nature Communications; 10(1) pg4533
PudMed id
Primer autor
Ochiai, N
Titulo
Murine osteoclasts secrete serine protease HtrA1 capable of degrading osteoprotegerin in the bone microenvironment.
Citar
Communications Biology; 2 pg86
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