Recombinant Human TRANCE/RANK L/TNFSF11 (E. coli-expressed)

Analyzed by SEC-MALS

Carrier Free

Catalog # Availability Size / Price Qty
6449-TEC-010/CF

With Carrier

Catalog # Availability Size / Price Qty
6449-TEC-010
Best Seller
Recombinant Human TRANCE/TNFSF11/RANK L Protein SEC-MALS.
2 Images
Product Details
Citations (3)
FAQs
Reviews

Recombinant Human TRANCE/RANK L/TNFSF11 (E. coli-expressed) Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to induce osteoclast differentiation of RAW 264.7 mouse monocyte/macrophage cells. The ED50 for this effect is 2-12 ng/mL
Source
E. coli-derived human TRANCE/TNFSF11/RANK L protein
Arg85-Asp245, with an N-terminal Met
Accession #
N-terminal Sequence
Analysis
Met
Predicted Molecular Mass
18.3 kDa
SDS-PAGE
19 kDa, reducing conditions

Product Datasheets

You must select a language.

x

6449-TEC (with carrier)

You must select a language.

x

6449-TEC/CF (carrier free)

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

6449-TEC

Formulation Lyophilized from a 0.2 μm filtered solution in MES and NaCl with BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

6449-TEC/CF

Formulation Lyophilized from a 0.2 μm filtered solution in MES and NaCl.
Reconstitution Reconstitute at 100 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Scientific Data

SEC-MALS View Larger

Recombinant Human TRANCE/RANK L/TNFSF11 (Catalog # 6449-TEC) has a molecular weight (MW) of 55.4 kDa as analyzed by SEC-MALS, suggesting that this protein is a homotrimer.  MW may differ from predicted MW due to post-translational modifications (PTMs) present (i.e. Glycosylation).

Bioactivity Graph showing dose-dependent bioactivity of Human TRANCE protein View Larger

Recombinant Human TRANCE/RANK L/TNFSF11 (6449-TEC) induces osteoclast differentiation of the RAW264.7 mouse monocyte/macrophage cell line. The ED50 for this effect is 2-12 ng/mL.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

=
÷

Background: TRANCE/TNFSF11/RANK L

RANK L (receptor activator of NF-kappa B ligand), also called TRANCE (TNF-related activation-induced cytokines), OPGL (osteoprotegerin ligand), or ODF (osteoclast differentiation factor), is a 39‑45 kDa type II transmembrane (TM) protein in the tumor necrosis factor family, designated TNFSF11 (1‑5). RANK L, produced by osteoblasts and bone marrow stromal cells, is required for differentiation of osteoclasts and stimulates bone resorption (4, 6). It is also produced by activated T cells and augments dendritic cell stimulation; RANK L-/- mice lack lymph nodes and have impaired thymocyte development (1‑3, 6). The human RANK L cDNA encodes 317 amino acids (aa), including a 47 aa cytoplasmic domain, a 21 aa TM region, and a 249 aa extracellular domain (ECD) with two potential N‑linked glycosylation sites (note: Arg85‑Asp245 of Accession # AAC51762 is identical to Arg157‑Asp317 of SwissProt # O14788. This aa range contains the ECD trimerization and receptor‑binding motifs, but not ECD proteolytic cleavage sites). Within the ECD, human RANK L shares 89%, 89%, 93% and 95% aa identity with mouse, rat, bovine and porcine RANK L, respectively. Mouse RANK L can stimulate human osteoclast differentiation (4). Like most TNF family members, RANK L can form trimers (1). Soluble 31, 25 and 24 kDa forms of RANK L can be created by usage of alternate start sites at aa 74 or 146, or proteolytic cleavage by osteoblast- or stromal cell‑derived ADAM10 (after aa 139) or MMP14 (aa 146), or bone metastatic prostate tumor-derived MT1-MMP (aa 146) (5, 7, 8). Both TM and soluble extracellular RANK L act by engaging RANK receptors and are antagonized by the decoy receptor, OPG (osteoprotegrin) (2, 5). In resting cells, the majority of RANK L is stored in secretory lysosomes (9). In mammary epithelia, RANK L is upregulated by pregnancy hormones and is essential for the formation of a lactating mammary gland (10). In the brain, astrocyte RANK L mediates body temperature regulation (11). Pathologically, RANK L is thought to mediate post-menopausal osteoporosis, vascular calcification, progestin-induced breast cancer, cancer-induced bone disease, and osteopetrosis (in RANK L deficiencies) (12‑16).

References
  1. Leibbrandt, A. and  J.M. Penninger 2008) Ann. N. Y. Acad. Sci. 1143:123.
  2. Wong, B.R. et al. (1997) J. Biol. Chem. 272:25190.
  3. Anderson, D.M. et al. (1997) Nature 390:175.
  4. Lacey, D.L. et al. (1998) Cell 93:165.
  5. Hikita, A. et al. (2006) J. Biol. Chem. 281:36846.
  6. Kong, Y-Y. et al. (1999) Nature 397:315.
  7. Accession #NP_143026 and EAX08679.
  8. Sabbota, A.L. et al. (2010) Cancer Res. 70:5558.
  9. Aoki, S. et al. (2010) J. Bone Miner. Res. 25:1907.
  10. Fata, J.E. et al. (2000) Cell 103:41.
  11. Hanada, R. et al. (2009) Nature 426:505.    
  12. Osako, M.K. et al. (2010) Circ. Res. 107:466.
  13. Schramek, D. et al. (2010) Nature 468:98.
  14. Gonzalez-Suarez, E. et al. (2010) Nature 468:103.
  15. Dougall, W.C. and M. Chaisson (2006) Cancer Metastasis Rev. 25:541.
  16. Sobacchi, C. et al. (2007) Nat. Genet. 39:960.
Long Name
TNF-related Activation-induced Cytokine
Entrez Gene IDs
8600 (Human); 21943 (Mouse); 117516 (Rat); 102137946 (Cynomolgus Monkey)
Alternate Names
CD254 antigen; CD254; ODF; OPGL; OPGLOPTB2; Osteoclast differentiation factor; Osteoprotegerin ligand; RANK L; RANKL; RANKLreceptor activator of nuclear factor kappa B ligand; Receptor activator of nuclear factor kappa-B ligand; sOdf; TNF-related activation-induced cytokine; TNFSF11; TRANCE; TRANCEODFhRANKL2; tumor necrosis factor (ligand) superfamily, member 11; tumor necrosis factor ligand superfamily member 11

Citations for Recombinant Human TRANCE/RANK L/TNFSF11 (E. coli-expressed)

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
Filter your results:

Filter by:

  1. Bacterial infections exacerbate myeloma bone disease
    Authors: R Liu, Y Zhong, R Chen, S Chen, Y Huang, H Liu
    Journal of Translational Medicine, 2022-01-06;20(1):16.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Plastrum testudinis extract suppresses osteoclast differentiation via the NF-&kappaB signaling pathway and ameliorates senile osteoporosis
    Authors: H Chen, G Shen, Q Shang, P Zhang, D Yu, X Yu, Z Zhang, W Zhao, Z Wu, F Tang, Liang, X Jiang, H Ren
    Journal of ethnopharmacology, 2021-05-08;276(0):114195.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Curcumin inhibits osteoclastogenic potential in PBMCs from rheumatoid arthritis patients via the suppression of MAPK/RANK/c-Fos/NFATc1 signaling pathways
    Mol Med Rep, 2016-08-25;14(4):3620-6.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay

FAQs

  1. What are the differences between the Recombinant Human TRANCE/RANK L/TNFSF11 Protein (Catalog # 390-TN) and the Recombinant Human TRANCE/RANK L/TNFSF11 (Catalog # 6449-TEC)?

    • 6449-TEC is the truncated version of 390-TN, and it contains a 10-His tag in the N-terminus. The bioactivity of 390-TN and 6449-TEC are measured in the same assay described in the datasheet, "Measured by its ability to induce osteoclast differentiation of RAW 264.7 mouse monocyte/macrophage cells." However, 390-TN utilizes a cross-linking antibody, MAB050, as it requires receptor trimerization which results in higher bioactivity. The ED50 for 390-TN is 1.5-7.5 ng/mL in the presence of MAB050, while the ED50 for 6449-TEC is 2-12 ng/mL.

View all Proteins and Enzyme FAQs

Reviews for Recombinant Human TRANCE/RANK L/TNFSF11 (E. coli-expressed)

There are currently no reviews for this product. Be the first to review Recombinant Human TRANCE/RANK L/TNFSF11 (E. coli-expressed) and earn rewards!

Have you used Recombinant Human TRANCE/RANK L/TNFSF11 (E. coli-expressed)?

Submit a review and receive an Amazon gift card.

$25/€18/£15/$25CAN/¥75 Yuan/¥2500 Yen for a review with an image

$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image

Submit a Review