Recombinant Human TNFRSF10D (TRAIL R4)-Fc Chimera (carrier-free)

Pricing & Availability
Regulatory Status
Other Names
Tumor necrosis factor receptor superfamily member 10D (TNFRSF10D), TNF-related apoptosis-inducing ligand receptor 4 (TRAIL R4), TRAIL receptor 4, Decoy receptor 2 (DcR2), CD264, TRAIL receptor with a truncated death domain (TRUNDD), APO-2L
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Product Citations
Human TNFRSF10D inhibits the cytotoxic effect induced by recombinant human TRAIL on mouse L929 cells.
  • Human_TNRFSF10D_TRAIL-R4_RECOM_1_111417
    Human TNFRSF10D inhibits the cytotoxic effect induced by recombinant human TRAIL on mouse L929 cells.
  • Human_TNRFSF10D_TRAIL-R4_RECOM_2_111417
    Human TNFRSF10D was aliquoted in PBS, pH7 at 0.1 mg/ml and one aliquot was kept at 4°C (control), and another was freeze/thawed four times (4X freeze/thaws). After this procedure, the samples were tested for their ability to inhibit the cytotoxic effect induced by recombinant human TRAIL on mouse L929 cells.
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768404 25 µg $194
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TNFRSF10D, also called TRAIL R4 and DcR2, is a member of the TNF receptor superfamily. It contains a cysteine-rich extracellular domain, a transmembrane domain and an intracellular truncated death domain, which is capable of inducing apoptosis. Its extracellular domain shows 60 % and 56% identity to the extracellular domain of human TNFRSF10A (TRAIL R1) and TNFRSF10B (TRAIL R2), respectively. TNFRSF10D, as one of decoy receptors, protects cells from TRAIL-induced apoptosis via competitive ligand binding with TNFRSF10A and TNFRSF10B. Some evidences indicated that TNFRSF10D blocks apoptosis via the association with TNFRSF10B. Its expression is widely expressed in several tissues but restricted to normal cells. It is considered as a reason for TRAIL sensitivity in tumors. The expression of TNFRSF10D is up-regulated upon p53 overexpression.

Product Details
Technical data sheet

Product Details

Human TNFRSF10D, amino acid (Ala56-His211) (Accession: # BC052270), with a linker (GSSR), a C-terminal human IgG (Pro100-Lys330) and a 6x His tag, was expressed in 293E cells.
Molecular Mass
The 397 amino acid recombinant protein has a predicted molecular mass of approximately 43.9 kD. The DTT-reduced and non-reduced protein migrates at approximately 56 and 98 kD respectively by SDS-PAGE. The predicted N-terminal amino acid is Ala.
> 95%, as determined by Coomassie stained SDS-PAGE.
0.22 µm filtered protein solution is in 1x PBS.
Endotoxin Level
Less than 0.1 EU per µg cytokine as determined by the LAL method.
10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
The ED50 is 1-6 ng/mL, as determined by inhibition of human TRAIL-mediated cytotoxicity on L929 cells in the presence of 12 ng/mL cross-linked human TRAIL and 1 µg/ml Actinomycin D.


Application Notes

BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at

Antigen Details

Homodimer, disulfide bond-linked

Membrane; liver, lung, kidney, testis, prostate, ovary, placenta intestine, thymus, spleen, heart; peripheral blood leukocytes.

TNFRSF10D block TRAIL-mediated apoptosis.
Biology Area
Apoptosis/Tumor Suppressors/Cell Death
Molecular Family
Cytokine/Chemokine Receptors, Soluble Receptors
Antigen References

1. Marsters SA, et al. 1997. Curr Biol. 7:1003.
2. Ashkenazi A. 2002. Nat. Rev. Cancer. 2:420.
3. Clancy L, et al. 2005. Proc. Natl. Acad. Sci. USA. 102:18099.
4. Mérino D, et al. 2006. Mol Cell Biol. 26:7046.
5. Walczak H, et al. 1997. EMBO J. 16:5386.
6. Daniels RA, et al. 2005. Cell. Res. 15:430.
7. Degli-Esposti MA, et al. 1997. Immunity. 7:813.
8. Meng RD, et al. 2000. Mol. Ther. 1:130-44.

Gene ID
8793 View all products for this Gene ID
View information about TNFRSF10D on

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)

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*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.


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