T3573
RANK Ligand/TRANCE human
>90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder
别名:
Osteoclast Differentiation Factor (ODF), Osteoprotegerin Ligand (OPGL), Receptor Activator of NF-KB Ligand (RANKL), TNF-related activation-induced cytokines (TRANCE)
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关于此项目
Form:
lyophilized powder
Assay:
>90% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in NSO cells
Mol wt:
glycolysylated recombinant product ~35 kDa by SDS-PAGE
calculated mol wt 23 kDa
calculated mol wt 23 kDa
产品名称
RANK Ligand/TRANCE human, >90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder
biological source
human
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
Quality Level
Gene Information
human ... TNFSF11(8600)
Analysis Note
The biological activity is measured by its ability to induce osteoclast differentiation on mouse splenocytes.
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
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; cell surface receptor for RANK Ligand.
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.
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.
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.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
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)
Jeong-Ki Min et al.
The Journal of biological chemistry, 278(41), 39548-39557 (2003-08-02)
Vascular endothelial growth factor (VEGF) is known as a key regulator of angiogenesis during endochondral bone formation. Recently, we demonstrated that TNF-related activation-induced cytokine (TRANCE or RANKL), which is essential for bone remodeling, also had an angiogenic activity. Here we
Matrine prevents bone loss in ovariectomized mice by inhibiting RANKL-induced osteoclastogenesis
Chen X, et al.
Faseb Journal, 31(11), 4855-4865 (2017)
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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