RANK Ligand (L300) Antibody detects transfected levels of cellular RANK Ligand protein.

Rat, Monkey, Bovine, Pig

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

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 activation (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).