T3573
RANK Ligand/TRANCE human
>90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder
Synonym(s):
Osteoclast Differentiation Factor (ODF), Osteoprotegerin Ligand (OPGL), Receptor Activator of NF-KB Ligand (RANKL), TNF-related activation-induced cytokines (TRANCE)
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About This Item
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biological source
human
Quality Level
recombinant
expressed in NSO cells
Assay
>90% (SDS-PAGE)
form
lyophilized powder
potency
1.5-7.5 ng/mL ED50
mol wt
glycolysylated recombinant product ~35 kDa by SDS-PAGE
calculated mol wt 23 kDa
packaging
pkg of 10 μg
storage condition
avoid repeated freeze/thaw cycles
impurities
endotoxin, tested
UniProt accession no.
application(s)
cell analysis
storage temp.
−20°C
Gene Information
human ... TNFSF11(8600)
General description
Tumor necrosis factor (ligand) superfamily, member 11 (Tnfsf11) is also known as receptor activator of nuclear factor-κB ligand (RANKL). It is a type II transmembrane signaling receptor. It has a molecular weight of around 35kDa. This protein contains an amino-terminal intracellular tail and a carboxy-terminal extracellular region, that bears a connecting stalk and a receptor-binding domain. Tnfsf11 is located on human chromosome 13q14.11.
Application
RANK Ligand/TRANCE human can be used in in vitro osteoclastogenic assays for osteoclast differentiation.
RANK Ligand/TRANCE human has been used to stimulate differentiation.
Biochem/physiol Actions
RANK Ligand (receptor activator of NF-kB ligand (RANKL) also referred to as TNF-related activation induced cytokines (TRANCE) or osteoprotegerin ligand is a protein that belongs to tumor necrosis factor (TNF) family. It stimulates the mature dendritic cells and induces the cytokine production. RANKL also facilitates bone remodelling and possess an angiogenic activity.
RANK Ligand/TRANCE, a member of the TNF superfamily, induces activation of the c-jun N-terminal kinase, enhances T-cell growth and dendritic cell function, induces osteoclastogenesis, and lymph node organogenesis. Mouse and human RANK Ligand share 85% amino acid identity. RANK is the cell surface receptor for RANK Ligand.
Physical form
Lyophilized from a 0.2 μm filtered solution in 20 mM MOPS and 500 mM NaCl, pH 6.5, with 50 μg BSA per 1 μg as a carrier protein.
Analysis Note
The biological activity is measured by its ability to induce osteoclast differentiation on mouse splenocytes.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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RANKL employs distinct binding modes to engage RANK and the osteoprotegerin decoy receptor
Nelson C A, et al.
Structure, 20(11), 1971-1982 (2012)
Cytosolic phospholipase A2 and eicosanoids modulate life, death and function of human osteoclasts in vitro
Allard-Chamard H, et al.
Prostaglandins, Leukotrienes, and Essential Fatty Acids, 90(4), 117-123 (2014)
R Josien et al.
Journal of immunology (Baltimore, Md. : 1950), 162(5), 2562-2568 (1999-03-11)
TNF-related activation-induced cytokine (TRANCE) is a member of the TNF family recently identified in activated T cells. We report here that TRANCE mRNA is constitutively expressed in memory, but not naive, T cells and in single-positive thymocytes. Upon TCR/CD3 stimulation
Soluble TRAIL is present at high concentrations in seminal plasma and promotes spermatozoa survival.
Giorgio Zauli et al.
Reproduction (Cambridge, England), 148(2), 191-198 (2014-05-16)
The expression of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL(TNFSF10)) and of its receptors (TRAILR1, TRAILR2, TRAILR3, and TRAILR4) have been documented in testis, but the presence of soluble TRAIL in seminal fluid, as well as the potential physiopathological role of
Harikiran Nistala et al.
The Journal of biological chemistry, 285(44), 34126-34133 (2010-08-24)
Mutations in fibrillin-1 or fibrillin-2, the major structural components of extracellular microfibrils, cause pleiotropic manifestations in Marfan syndrome and congenital contractural arachnodactyly, respectively. We recently found that fibrillin-1 and fibrillin-2 control bone formation by regulating osteoblast differentiation through the differential
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