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. These dendritic cells then stimulate naïve T-cell proliferation, and promote the survival of RANK + T-cells. RANK is also expressed in a variety of tissues, including skeletal muscle, thymus, liver, colon, small intestine, and adrenal gland. The RANK/RANKL interaction is important in the regulation of osteoclastogenesis, and in dendritic cell-mediated T-cell immune responses. Impairments in RANK signaling have been implicated in the induction of expansile osteolysis and Paget's disease of bone (PDB2). Recombinant Human sRANK Receptor is a 19.3 kDa polypeptide containing the TNFR-homologous, cysteine-rich portion of the extracellular domain of RANK receptor (175 amino acid residues).
Source: E.coli
Synonyms: TNFRSF11A, ODFR (osteoclast differentiation factor receptor), ODAR (osteoclast differentiation and activation receptor), TRANCE Receptor
AA Sequence: MQIAPPCTSE KHYEHLGRCC NKCEPGKYMS SKCTTTSDSV CLPCGPDEYL DSWNEEDKCL LHKVCDTGKA LVAVVAGNST TPRRCACTAG YHWSQDCECC RRNTECAPGL GAQHPLQLNK DTVCKPCLAG YFSDAFSSTD KCRPWTNCTF LGKRVEHHGT EKSDAVCSSS LPARK
Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.
Biological Activity: Determined by its ability to inhibit sRANKL induced NF-κB in RAW264.7 cells in the absence of any cross-linking. The expected ED50 for this effect in the presence of 15 ng/ml of recombinant sRANKL, is 30-50 ng/ml.
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