Anti-RANK-L [AMG 162 (Denosumab)]

Catalogue Number: AB04909-3.0-BT-ABA

Manufacturer:Vector Laboratories, Inc (ABA)
Type:Recombinant Monoclonal
Alias:CD254; TRANCE; RANKL; ODF; OPGL; Tumor necrosis factor ligand superfamily member 11; Osteoclast differentiation factor; Osteoprotegerin ligand; Receptor activator of nuclear factor kappa-B ligand; TNF-related activation-induced cytokine
Shipping Condition:Blue Ice
Unit(s): 1 mg
Host name: Mouse
Clone: AMG 162 (Denosumab)
Isotype: IgG2b
Immunogen: The original antibody was produced using transgenic Xenomouse technology.
Application: ELISA, Inh, InVitroA, InVivoA

Additional Text

Gene ID

8600

Gene Name

TNFSF11

Uniprot ID

O14788

Purification

Purified

Antibody Clonality

Recombinant Monoclonal

Storage Note

Store at 4⁰C for up to 3 months. Note, this antibody is provided without added preservatives, it is therefore recommed this antibody be handled under sterile conditions. For longer storage, aliquot and store at -20⁰C.

Short Description

This chimeric mouse antibody was made using the variable domain sequences of the original Human IgG2 format, for improved compatibility with existing reagents, assays and techniques.

Application Notes

The original format of the antibody showed high affinity and specificity for human receptor activator of nuclear factor-κB ligand (RANKL). It is a potent inhibitor of osteoclastic bone resorption. By binding to RANKL in a manner similar to native osteoprotegerin (OPG), it prevents the interaction of RANKL and RANK (Lewiecki et al., 2008; PMID: 19707445). The specificity of the original format of the antibody was confirmed by ELISA analysis. In particular, it bound to a human RANKL fragment (143-317) that included the complete TNF-like domain encoded by exon 5 of the human RANKL gene. The original format of the antibody inhibited the ability of human RANKL (143-317) to stimulate the formation of osteoclasts derived from murine RAW 264.7 cells, with IC50 values of 1.64. The original format of the antibody prevented the resorptive response in mice challenged with a human RANKL fragment. Knock-in technology was used to replace exon 5 from murine RANKL with its human ortholog. The resulting ''huRANKL'' mice exclusively express chimeric RANKL that was measurable with a human RANKL assay and that maintained bone resorption at slightly reduced levels versus wildtype controls. In young huRANKL mice, the original format of the antibody reduced trabecular osteoclast surfaces by 95% and increased bone density and volume. In adult huRANKL mice, the original format of the antibody reduced bone resorption, increased cortical and cancellous bone mass, and improved trabecular microarchitecture (Kostenuik et al., 2009; PMID: 19016581). The original format of the antibody reduced biochemical markers of bone resorption in postmenopausal women with low bone mass (McClung et al. 2006; PMID: 16495394) and in patients with multiple myeloma or with bone metastases (Body et al., 2006; PMID: 16489077).