RANKL/TNFSF11 Protein, Mouse

RANKL (TNFSF11), a type II transmembrane protein, is a receptor activator of NF-κB (RANK) ligand. RANKL is an activator of RANK. When binding to RANK, it induces the differentiation of monocyte/macrophage-lineage cells into osteoclasts and leads to osteoclast precursor maturation. RANKL is critical for osteoclasts maturation, bone modeling, and bone remodeling, as well as the development of lymph nodes (LNs). RANKL/TNFSF11 Protein, Mouse is a recombinant mouse RANKL (Q137-D316) without tag, which is produced in E.coli^[1][2].

RANKL (TNFSF11) belongs to TNF family. RANKL is a type II transmembrane protein and is a receptor activator of NF-κB (RANK) ligand. RANKL is an activator of RANK. RANKL binds to RANK and induces the differentiation of monocyte/macrophage-lineage cells into osteoclasts and leads to osteoclast precursor maturation. In bone tissue, RANKL is expressed by osteoblasts, osteocytes and immune cells, especially in osteoblasts and osteocytes^[1]. RANKL is also expressed by T cells and increases proliferation and survival of dendritic cells^[2]. In mice, RANKL/RANK signaling attenuates inflammation in ischemic brains through a Toll-like receptor signaling pathway^[4].
RANKL consists of cytoplasmic domain (1-47), helical domain (48-68), and extracellular domain (69-317). The soluble chain (140-317) is released when cleaved by enzymes such as matrix metalloproteinases (MMP3 or 7) and ADAM^[1][3].
RANKL is critical for osteoclasts maturation, bone modeling, and bone remodeling, as well as the development of lymph nodes (LNs)^[1].

RANKL (mouse, 3 ng/mL, 4 days) induces osteoclast differentiation from RAW264.7 cells, and can be inhibited by Resveratrol^[5].
RANKL (mouse,10 ng/mL, 0-3 h) induces NF-κB activation in murine hepatocyte cell line (AML-12) ^[6].

RANKL (mouse, i.c.v., 5 ng in 2 μL) reduces IL-1β, MCP-1, IL-6 and TNFα expression in WT mice^[4].
RANKL (mouse, i.p., 1-10 μg) protects against hepatic ischemia/reperfusion liver injury in mice^[6].

1.Measured by its ability to induce osteoclast differentiation of RAW 264.7 mouse monocyte/macrophage cells. The ED₅₀ is ≤1.192 ng/mL as measured by RAW 264.7 mouse monocyte/macrophage cells, corresponding to a specific activity of ≥8.39 × 10⁵ units/mg.
2. Measured by its binding ability in a functional ELISA. Immobilized mouse TNFSF11 at 10 μg/mL (100μL/well) can bind biotinylated Human TNFRSF11B. The ED₅₀ for this effect is 0.0848 μg/mL.

• 
  Measured by its ability to induce osteoclast differentiation of RAW 264.7 mouse monocyte/macrophage cells. The ED₅₀ is <1.808 ng/mL as measured by RAW 264.7 mouse monocyte/macrophage cells, corresponding to a specific activity of >5.531 × 10⁵ units/mg.
• 
  Measured by its binding ability in a functional ELISA. Immobilized mouse TNFSF11 at 10 μg/mL (100 μL/well) can bind biotinylated Human TNFRSF11B. The ED₅₀ for this effect is 0.0848 μg/mL.

Mouse

E. coli

Tag Free

O35235-1 (Q137-D316)

21943  [NCBI]

Partial

QRFSGAPAMMEGSWLDVAQRGKPEAQPFAHLTINAASIPSGSHKVTLSSWYHDRGWAKISNMTLSNGKLRVNQDGFYYLYANICFRHHETSGSVPTDYLQLMVYVVKTSIKIPSSHNLMKGGSTKNWSGNSEFHFYSINVGGFFKLRAGEEISIQVSNPSLLDPDQDATYFGAFKVQDID

Approximately 20-29 kDa, based on SDS-PAGE under reducing conditions.

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 20 mM Tris, 150 mM NaCl, 1 mM EDTA, pH 8.0.
2.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1.0 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Ono T, et al. RANKL biology: bone metabolism, the immune system, and beyond. Inflamm Regen. 2020 Feb 7;40:2.  [Content Brief]

  [2]. Hofbauer LC, et al. Role of receptor activator of nuclear factor-kappaB ligand and osteoprotegerin in bone cell biology. J Mol Med (Berl). 2001 Jun;79(5-6):243-53.  [Content Brief]

  [3]. Li B, et al. Roles of the RANKL-RANK Axis in Immunity-Implications for Pathogenesis and Treatment of Bone Metastasis. Front Immunol. 2022 Mar 21;13:824117.  [Content Brief]

  [4]. Tobeiha M, et al. RANKL/RANK/OPG Pathway: A Mechanism Involved in Exercise-Induced Bone Remodeling. Biomed Res Int. 2020 Feb 19;2020:6910312.  [Content Brief]

  [5]. Shimamura M, et al. OPG/RANKL/RANK axis is a critical inflammatory signaling system in ischemic brain in mice. Proc Natl Acad Sci U S A. 2014 Jun 3;111(22):8191-6.  [Content Brief]

  [6]. He X, et al. Resveratrol prevents RANKL-induced osteoclast differentiation of murine osteoclast progenitor RAW 264.7 cells through inhibition of ROS production. Biochem Biophys Res Commun. 2010 Oct 22;401(3):356-62.  [Content Brief]