Recombinant Mouse TNFRSF21-Fc Chimera (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
Tumor necrosis factor receptor superfamily member 21, TNFRSF21, Death receptor 6, DR6, CD358
Ave. Rating
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Product Citations
publications
a.
Recom_Mouse-TNFRSF21-Fc-Chimera_1_CF
Recombinant mouse TNFRSF21-Fc Chimera binds to amyloid precursor protein (APP770) in a dose-dependent manner. EC50 of this effect is 12 - 84 ng/mL.
  • a.
Recom_Mouse-TNFRSF21-Fc-Chimera_1_CF
    Recombinant mouse TNFRSF21-Fc Chimera binds to amyloid precursor protein (APP770) in a dose-dependent manner. EC50 of this effect is 12 - 84 ng/mL.
  • b.
Recom_Mouse-TNFRSF21-Fc-Chimera_2_CF
    Stability testing for recombinant mouse TNFRSF21-Fc Chimera. Recombinant mouse TNFRSF21-Fc Chimera was aliquoted in 10 mM Sodium Phosphate, 0.3 M NaCl, pH 6.5, at 0.2 mg/mL and one aliquot was kept at 4°C (Control), and another was frozen and thawed four times (4x Freeze/Thaw). After this procedure, the samples were tested for their ability to bind to amyloid precursor protein (APP770) in a dose-dependent manner. EC50 of this effect is 12 - 84 ng/mL.
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558604 25 µg 288€
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558606 100 µg 540€
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Description

With roles in immunological, neurological, and oncological diseases, Tumor necrosis factor receptor (TNFR) superfamily members, have emerged as drug targets for the treatment of neurodegenerative diseases such as Alzheimer's and central nervous system (CNS) demyelination diseases. Eight death receptors have been identified and each regulates cell death in selected cell populations. TNFR21, also known as death receptor 6 (DR6), CD358, or BM-018 negatively regulates neuron, axon, and oligodendrocyte survival. It also hinders axon-dendrocyte and oligodendrocyte regeneration and its inhibition lead to neuroprotective effect in nerve injury. Mouse TNFRSF21/DR6 consists of a 308 amino acid extracellular domain (ECD) with four cysteine-rich motifs, a 21 amino acid transmembrane segment and a 285 amino acid palmityolated cytoplasmic region that contains one death domain. In the ECD domain of TNFRSF21/DR6 mouse and human share 82% amino acid sequence identity. In association with TNFRSF1A, TNFRSF21/DR6 activates nuclear factor kappa-B (NFk-B) and mitogen-activated protein kinase 8 (MAPK8, also called c-Jun N-terminal kinase 1) inducing cell apoptosis. TNFRSF21/DR6 plays a role in T-helper cell activation and may be involved in inflammation and immune regulation. Unnecessary or connectionless axons are removed when released alpha-amyloid precursor protein (APP) binds to TNFRSF21/DR6 in an autocrine/paracrine manner to activate a caspase-dependent self-destruction program. Increasing beta-catenin levels in brain endothelium upregulates TNFRSF21/DR6 and TNFRSF19, indicating that these death receptors are downstream target genes of Wnt/beta-catenin signaling, which has been shown to be required for blood-brain barrier development. TNFRSF21/DR6 is up-regulated in numerous solid tumors as well as in tumor vascular cells, including ovarian cancer and may be a clinically useful diagnostic and predictive serum biomarker for some adult sarcoma subtypes.

Product Details
Technical Data Sheet (pdf)

Product Details

Source
Mouse TNFRSF21, amino acids Gln42-His349 (Accession # Q9EPU5), with a C-terminal mouse-Fc tag, was expressed in 293E cells.
Molecular Mass
The 546 amino acid recombinant protein has a predicted molecular mass of approximately 60.5 kD. The DTT-reduced and non-reduced protein migrate at approximately 80 kD and 200 kD respectively in SDS-PAGE.
N-terminal
Sequence Analysis
The predicted N-terminal amino acid is Gln
Purity
> 95%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution 10 mM Sodium Phosphate, 0.3 M NaCl, pH 6.5
Endotoxin Level
Less than 0.1 EU per μg of cytokine as determined by the LAL method
Concentration
25 µg size is 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, 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.
Activity
Recombinant mouse TNFRSF21-Fc Chimera binds to amyloid precursor protein (APP770) in a dose-dependent manner. EC50 of this effect is 12 - 84 ng/mL.
Application

Bioassay

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 validated 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 tech@biolegend.com.

Antigen Details

Structure
Monomer
Distribution

T-cells, B-cells, monocytes, tumor vascular cells

Function
Negatively regulates neuron, axon, and oligodendrocyte survival, activates a caspase-dependent self-destruction program, T-helper cell activation
Interaction
NGFR, CASP8 and N-APP
Ligand/Receptor
N-APP
Bioactivity
Recombinant mouse TNFRSF21-Fc Chimera binds to amyloid precursor protein (APP770) in a dose-dependent manner. EC50 of this effect is 12 - 84 ng/mL.
Cell Type
B cells, Endothelial cells, Monocytes, T cells
Biology Area
Apoptosis/Tumor Suppressors/Cell Death, Cell Death, Neurodegeneration
Molecular Family
CD Molecules, Soluble Receptors
Antigen References
  1. Mahmood Z and Shukla Y. 2010. Exp Cell Res. 316::887-99.
  2. Vinay DS and Kwon BS. 2011. Clin Exp Immunol. 164::145-57.
  3. Mi S, et al. 2011. Nat Med. 17:816-21.
  4. Dechant G and Barde YA. 2002. Nat Neurosci. 5:1131-6.
  5. Bodmer JL, et al. 2002. J Trends Biochem Sci. 27:19-26.
  6. Naismith JH and Sprang SR. 1998. Trends Biochem Sci. 23:74-9.
  7. Zhao H, et al. 2001 J Exp Med. 194:1441-8.
  8. Klima M, et al. 2009. Biochim Biophys Acta. 1793:1579-87.
  9. Yang K, et al. 2012. PLoS ONE. 7:e36525.
  10. Qiu CW, et al. 2012. J Med Hypotheses. 79:853-5.
  11. Banner DW, et al. 1993. Cell. 73:431-45.
  12. Tam SJ, et al. 2012. Dev Cell. 22:403-17.
  13. Pan G, et al. 1998. FEBS Lett. 431:351-6.
  14. Zhao H, et al. 2001. J Exp Med. 194:1441-8.
  15. Zhang JY, et al. 2021. Cell Res. 31:980-997.
  16. Kuester M, et al. 2011. J Mol Biol. 409:189-201.
Gene ID
94185 View all products for this Gene ID
UniProt
View information about TNFRSF21 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: 1    Revision Date: 10-31-2024

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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