Recombinant Human TRANCE (RANKL) (Animal-Free)

Pricing & Availability
Regulatory Status
RUO
Other Names
Tumor necrosis factor ligand superfamily, member 11 (TNFSF11), Osteoprotegerin ligand (OPGL), Receptor activator of NF-kappa-B ligand (RANKL), TNF-related activation-induced cytokine (TRANCE), Osteoclast differentiation factor (ODF), CD254
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717502 10 µg 253 CHF
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Description

Human TRANCE gene, also known as RANKL, encodes a type II membrane protein of 317 amino acids with a predicted molecular mass of 35.4 kD. RANKL is cleaved to produce a soluble form with biological activity. The shedding of membrane-bound RANKL appears to be mediated by expression of matrix metalloproteinase 14 (MMP-14) and ADAM10. Suppression of MMP-14 in primary osteoblasts increased membrane-bound RANKL and promoted osteoclastogenesis in cocultures with macrophages. Therefore, RANKL shedding seems to be an important process that downregulates local osteoclastogenesis. Conversely, increased production of RANKL by osteoblastic cells leads to osteoclast differentiation, activation, and survival, which results in increased bone resorption. Binding of RANKL to its receptor RANK activates TNF receptor-associated factor 6 (TRAF6), which is linked to downstream pathways including NF-κB, c-jun N-terminal kinase (JNK), and Src. TRAF6 in particular has been shown to be necessary for the differentiation of osteoclastic cells by enhancing Src kinase, essential for osteoclast function. Activation of JNK and NF-κB by RANKL induces the expression of IL-1, IL-6, IL-12, and IL-15 in dendritic cells. In addition, RANKL stimulates proliferation, adhesion, and IL-7 expression of thymic epithelial cells. RANKL can mediate bone loss in arthritis and periodontal disease.

Product Details
Technical Data Sheet (pdf)

Product Details

Source
Human TRANCE, amino acids Glu70-Asp244 (Accession# AF013171) with N terminus Met, was expressed in E. coli.
Molecular Mass
The 176 amino acid N-terminal methionylated recombinant protein has a predicted molecular mass of 20 kD. The predicted N-terminal amino acid is Met.
Purity
>98%, as determined by Coomassie stained SDS-PAGE and HPLC analysis.
Formulation
Lyophilized, carrier-free.
Endotoxin Level
Less than 0.1 ng per µg of protein.
Storage & Handling
Unopened vial can be stored at -20°C or -70°C. For maximum results, quick spin vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. It is recommended to further dilute in a buffer, such as 5% Trehalose, and store working aliquots at -20°C to -80°C. Avoid repeated freeze/thaw cycles.
Activity
The expected ED50 is 10.0 - 25.0 ng/ml, corresponding to a specific activity of 0.4 - 1.0 x 105 units/mg as determined by its ability to induce NF-κB in RAW264.7 cells in the absence of any cross-linking.
Application

Bioassay

Antigen Details

Structure
Cytokine
Distribution
T cells, osteoblasts, bone marrow stromal cells, hypertrophic and prehypertrophic chondrocytes, stromal fibroblasts, synovial cells, mammary gland epithelial cells, and megakaryocytes.
Function
RANKL induces osteoclast formation, bone-resorbing activity in mature osteoclasts, lymphocyte development, and lymph node organogenesis. RANKL augments the ability of dendritic cells to stimulate naive T-cell proliferation and dendritic cell survival. RANKL expression is stimulated by various cytokines (IL-1, TNF-α and IL-11), calciotrophic hormones including PTH, 1,25dihydroxyvitamin D3 (1,25D3), and prostaglandin E2.
Interaction
T cells, dendritic cells, bone marrow derived macrophages, osteoclast precursors and mature osteoclasts.
Ligand/Receptor
TNFRSF11A (Tumor necrosis factor receptor superfamily, member 11A) also called RANK and TNFRSF11B (OPG) which acts as a decoy receptor for RANKL.
Cell Type
Embryonic Stem Cells
Biology Area
Immunology, Stem Cells
Molecular Family
Growth Factors, Cytokines/Chemokines
Antigen References

1. Dehm SM, et al. 2004. Biochem. Cell Biol. 82:263.
2. Hikita A, et al. 2006. J. Biol. Chem. 281:36846.
3. Kim NS, et al. 2006. Mol. Cell Biol. 26:1002.
4. Wada T, et al. 2006. TRENDS Mol. Med. 12:17.
5. Lee HW, et al. 2008. Exp. Mol. Med. 40:59.
6. Ha J, et al. 2010. J. Immunol. 184:4717.
7. Hasturk H, et al. 2012. Front. Immunol. 3:118.
8. Tanaka S. 2013. World J. Orthop. 4:1.

Gene ID
8600 View all products for this Gene ID
UniProt
View information about TRANCE on UniProt.org

Related FAQs

Why choose BioLegend recombinant proteins?

     • Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
     • Greater than 95% Purity or higher, tested on every lot of product.
     • 100% Satisfaction Guarantee for quality performance, stability, and consistency.
     • Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
     • Bulk and customization available. Contact us.
     • Learn more about our Recombinant Proteins.

How does the activity of your recombinant proteins compare to competitors?

We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!

What is the specific activity or ED50 of my recombinant protein?

The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.

Have your recombinants been tested for stability?

Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.

Does specific activity of a recombinant protein vary between lots?

Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?

Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)

Go To Top Version: 3    Revision Date: 05.06.2014

For Research Use Only. Not for diagnostic or therapeutic use.

 

This product is supplied subject to the terms and conditions, including the limited license, located at www.biolegend.com/terms) ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.

 

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