RANK/TNFRSF11A Protein, Human

RANK/TNFRSF11A protein is the receptor of TNFSF11/RANKL and is critical for RANKL-induced osteoclastogenesis. It interacts with EEIG1 to promote osteoclast formation by promoting NFATC1 transcription and activating PLCG2. RANK/TNFRSF11A Protein, Human is the recombinant human-derived RANK/TNFRSF11A protein, expressed by E. coli , with tag free.

The RANK/TNFRSF11A protein functions as the receptor for TNFSF11/RANKL/TRANCE/OPGL, playing a crucial role in the essential process of RANKL-mediated osteoclastogenesis. Interacting with EEIG1, it promotes osteoclast formation by facilitating the transcription of NFATC1 and activating PLCG2. Beyond its role in bone metabolism, RANK/TNFRSF11A is involved in regulating interactions between T-cells and dendritic cells. The protein binds to the clefts between the subunits of the TNFSF11 ligand trimer, forming a heterohexamer. It is also a key component of a complex comprising EEIG1, TNFRSF11A/RANK, PLCG2, GAB2, TEC, and BTK, with complex formation increasing in the presence of TNFSF11/RANKL. Additionally, RANK/TNFRSF11A interacts with TRAF family members (TRAF1, TRAF2, TRAF3, TRAF5, and TRAF6) and GAB2, further contributing to its regulatory functions in diverse cellular processes.

Human

E. coli

Tag Free

Q9Y6Q6-1 (Q29-K202)

8792  [NCBI]

Partial

QIAPPCTSEKHYEHLGRCCNKCEPGKYMSSKCTTTSDSVCLPCGPDEYLDSWNEEDKCLLHKVCDTGKALVAVVAGNSTTPRRCACTAGYHWSQDCECCRRNTECAPGLGAQHPLQLNKDTVCKPCLAGYFSDAFSSTDKCRPWTNCTFLGKRVEHHGTEKSDAVCSSSLPARK

Approximately 20 kDa, based on SDS-PAGE under reducing conditions.

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.