RANKL Protein, Human, Recombinant

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RANKL Protein, Human, Recombinant: Product Information

Purity
> 95 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
1. Immobilized human TNFSF11 at 10 μg/ml (100 μl/well) can bind biotinylated human TNFRSF11B-His (Cat:10271-H08H), The EC50 of biotinylated human TNFRSF11B-His (Cat:10271-H08H) is 5.7-13.4 ng/ml.
2. The bioactivity of hRANKL was determined by measuring the ability of hRANKL to induce TRAP activity in Raw 264.7 cells. The ED50 for this effect is typically 1.5-7.5 ng/mL.
Protein Construction
A DNA sequence encoding the human TNFSF11 (O14788-2) (Gly 63-Asp 244) was expressed.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Gly 63
Molecule Mass
The recombinant human TNFSF11 consists of 182 amino acids and has a calculated molecular mass of 20.5 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of the protein is approximately 27 kDa due to the glycosylation.
Formulation
Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -70℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

RANKL Protein, Human, Recombinant: Images

RANKL Protein, Human, Recombinant: Alternative Names

CD254 Protein, Human; hRANKL2 Protein, Human; ODF Protein, Human; OPGL Protein, Human; OPTB2 Protein, Human; RANKL Protein, Human; sOdf Protein, Human; TRANCE Protein, Human

RANKL Background Information

Tumor necrosis factor ligand superfamily member 11, also known as Receptor activator of nuclear factor kappa-B ligand, Osteoprotegerin ligand, TNFSF11, RANKL, TRANCE, OPGL and CD254, is a single-pass type II membrane protein which belongs to the tumor necrosis factor family. The receptor activator of nuclear factor-kappaB ligand (RANKL), its cognate receptor RANK, and its natural decoy receptor osteoprotegerin have been identified as the final effector molecules of osteoclastic bone resorption. RANK and RANKL are key regulators of bone remodeling and regulate T cell/dendritic cell communications, and lymph node formation. Moreover, RANKL and RANK are expressed in mammary gland epithelial cells and control the development of a lactating mammary gland during pregnancy. Genetically, RANKL and RANK are essential for the development and activation of osteoclasts and bone loss in response to virtually all triggers tested. Inhibition of RANKL function via the natural decoy receptor osteoprotegerin (OPG, TNFRSF11B) prevents bone loss in postmenopausal osteoporosis and cancer metastases. Importantly, RANKL appears to be the pathogenetic principle that causes bone and cartilage destruction in arthritis. RANK-RANKL signaling not only activates a variety of downstream signaling pathways required for osteoclast development, but crosstalk with other signaling pathways also fine-tunes bone homeostasis both in normal physiology and disease. In addition, RANKL and RANK have essential roles in lymph node formation, establishment of the thymic microenvironment, and development of a lactating mammary gland during pregnancy.
Full Name
tumor necrosis factor (ligand) superfamily, member 11
References
  • Takayanagi H, et al. (2002) Signaling crosstalk between RANKL and interferons in osteoclast differentiation. Arthritis Res. 4 Suppl 3: S227-32.
  • Nakashima T, et al. (2003) RANKL and RANK as novel therapeutic targets for arthritis. Curr Opin Rheumatol. 15(3): 280-7.
  • Schwarz EM, et al. (2007) Clinical development of anti-RANKL therapy. Arthritis Res Ther. 9 Suppl 1: S7.
  • Leibbrandt A, et al. (2008) RANK/RANKL: regulators of immune responses and bone physiology. Ann N Y Acad Sci. 1143: 123-50.
  • Factors that Affect the Osteoclastogenesis of RAW264.7 Cells
    Author
    Nguyen, J;Nohe, A;
    Year
    2017
    Journal
    J Biochem Anal Stud
    Application
    cell-based
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