Mouse RANK/TNFRSF11A Antibody Summary
Leu29-Pro213 (Leu29Met)
Accession # O35305
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: RANK/TNFRSF11A
RANK (receptor activator of NF-kappa B, also known as TRANCE receptor, osteoclast differentiation factor receptor [ODFR] and TNFRSF11A) is a member of the tumor necrosis factor receptor family. The full length mouse RANK cDNA encodes a type I transmembrane protein of 625 amino acids (aa) with a predicted 184 aa extracellular domain and a 391 aa cytoplasmic domain. The extracellular domain contains two potential N-linked glycosylation sites. RANK shares significant amino acid homology with other members of the TNF R family in its extracellular four cysteine-rich repeats. Human and murine RANK share 81% aa identity in their extracellular domains. RANK is widely expressed with the highest levels in skeletal muscle, thymus, liver, colon, small intestine and adrenal gland. RANK is expressed in dendritic cells. In activated human peripheral blood T lymphocytes, RANK expression is induced by IL-4 and TGF-beta. Multiple tumor necrosis factor receptor-associated factors (TRAFs) are involved in the signaling of RANK. TRANCE (TNF-related activation-induced cytokines, also known as RANK ligand [RANKL], osteoprotegerin ligand [OPGL], and osteoclast differentiation factor [ODF]) is the ligand for RANK. The biological functions mediated through RANK include activation of NF-kappa B and c-jun N-terminal kinase, enhancement of T cell growth and dendritic cell function, induction of osteoclastogenesis, and lymph node organogenesis. Soluble RANK is able to block TRANCE induced biological activity.
- Anderson, D.M. et al. (1997) Nature 390:175.
- Nakagawa, N. et al. (1998) Biochem. Biophys. Res. Commun. 245:382.
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