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Key Documents

T3573

Sigma-Aldrich

RANK Ligand/TRANCE human

>90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder

Synonyme(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

Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Source biologique

human

Niveau de qualité

Produit recombinant

expressed in NSO cells

Pureté

>90% (SDS-PAGE)

Forme

lyophilized powder

Puissance

1.5-7.5 ng/mL ED50

Poids mol.

glycolysylated recombinant product ~35 kDa by SDS-PAGE
calculated mol wt 23 kDa

Conditionnement

pkg of 10 μg

Conditions de stockage

avoid repeated freeze/thaw cycles

Impuretés

endotoxin, tested

Numéro d'accès UniProt

Application(s)

cell analysis

Température de stockage

−20°C

Informations sur le gène

human ... TNFSF11(8600)

Description générale

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.

Actions biochimiques/physiologiques

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.

Forme physique

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.

Remarque sur l'analyse

The biological activity is measured by its ability to induce osteoclast differentiation on mouse splenocytes.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
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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