RANK Ligand (R2) Antibody

3959:

Immunoprecipitation , Western Blotting

RANK Ligand (R2) Antibody detects transfected levels of cellular RANK Ligand protein.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human RANK Ligand, within the cytoplasmic region. Antibody was purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of extracts from COS-7 cells, untransfected (-) or transfected (+) with a construct expressing human RANK Ligand, using RANK Ligand (R2) Antibody

RANK (receptor activator of NF-κB) is a member of the tumor necrosis factor (TNF) receptor subfamily that is activated by its ligand, RANKL (TRANCE/OPGL/ODF), to promote survival of dendritic cells and differentiation of osteoclasts (1-4). Although RANK is widely expressed, its cell surface expression may be more restricted to dendritic cells and foreskin fibroblasts (1). RANK contains a 383-amino acid intracellular domain that associates with specific members of the TRAF family to NF-κB and JNK activiation (1,5). RANKL/RANK signaling may also lead to survival signaling through activation of the Akt pathway and an upregulation of survival proteins, including Bcl-xL (2,6). RANK signaling has been implicated as a potential therapeutic to inhibit bone loss and arthritis (7,8).

RANKL (1), also named TNF-related activation-induced cytokine (TRANCE) (2,9), osteoprotegerin ligand (OPGL) (3), osteoclast differentiation factor (ODF) (4), and TNFSF11, is a type II transmembrane protein of the TNF family that exists as both a membrane-bound and soluble form. It is an essential regulator of immune function and bone development and homeostasis (7,10,11). RANKL is predominately expressed in activated T cells, as well as the thymus, lymph node, and bone marrow and promotes dendritic cell survival. Deletion of RANKL in mice leads to severe osteoporosis with a loss of osteoclasts, defects in T and B cell differentiation, loss of lymph node development, and mammary gland development during pregnancy (12-14).

1. Anderson, D.M. et al. (1997) Nature 390, 175-9.
2. Wong, B.R. et al. (1997) J. Exp. Med. 186, 2075-80.
3. Lacey, D.L. et al. (1998) Cell 93, 165-76.
4. Yasuda, H. et al. (1998) Proc. Natl. Acad. Sci. USA 95, 3597-602.
5. Darnay, B.G. et al. (1998) J. Biol. Chem. 273, 20551-5.
6. Wong, B.R. et al. (1999) Mol. Cell 4, 1041-9.
7. Walsh, M.C. and Choi, Y. Cytokine Growth Factor Rev. 14, 251-63.
8. Nakashima, T. et al. (2003) Curr. Opin. Rheumatol. 15, 280-7.
9. Wong, B.R. et al. (1997) J Biol Chem 272, 25190-4.
10. Hofbauer, L.C. (1999) Eur J Endocrinol 141, 195-210.
11. Theill, L.E. et al. (2002) Annu Rev Immunol 20, 795-823.
12. Mizuno, A. et al. (1998) Biochem Biophys Res Commun 247, 610-5.
13. Kong, Y.Y. et al. (1999) Nature 397, 315-23.
14. Fata, J.E. et al. (2000) Cell 103, 41-50.

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For Research Use Only. Not For Use In Diagnostic Procedures.