Login / Register 
United States ($) USD
Austria (€) EUR
Belgium (€) EUR
Finland (€) EUR
France (€) EUR
Germany (€) EUR
Ireland (€) EUR
Japan (¥) JPY
Luxembourg (€) EUR
Netherlands (€) EUR
Switzerland (CHF) CHF
United Kingdom (£) GBP
- Regulatory Status
- RUO
- Other Names
- p75TNFR, CD120b, TNF RII, tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), TNFBR, TNFR80, TNF receptor beta chain, p75 TNFR, p80 TNF-alpha receptor, tumor necrosis factor receptor 2
- Ave. Rating
- Submit a Review
- Product Citations
- publications
-
Inhibition of mouse TNF-α-induced cytotoxicity in L929 cells by mouse TNFRII (CD120b).
| Cat # | Size | Price | Quantity Check Availability | Save | ||
|---|---|---|---|---|---|---|
| 758904 | 25 µg | 278€ | ||||
| 758906 | 100 µg | 559€ | ||||
The biological effects of TNF are mediated by two cell surface TNF receptors: TNFRI (TNF-RI) and TNFRII (also known as TNFRII (CD120B) and TNF-RII). TNFRI and TNFRII are structurally related, but functionally distinct. Also, TNFRI is widely expressed on most cells, whereas TNFRII is more restricted and is primarily expressed in hematopoietic cells and cells of the immune system. The function of TNFRII is less understood and has fewer biological effects than TNFRI. Unlike TNFRI, TNFRII does not have a death domain and will induce NF-κB activation through a different pathway. It is generally accepted that TNFRI induces both apoptosis and survival pathways, while TNFRII induces only survival pathway. Only membrane-bound TNF can active TNFRII effectively. Soluble TNF can bind TNFRII, but can not induce TNFRII signaling. Upon binding of TNF, TNFRII will form a trimer and will recruit TRAF2, therefore leading to the activation of NF-κB. In T cells, TNFRII costimulation provides survival signals during the differentiation program triggered by TCR-mediated stimulation and also during clonal expansion in response to intracellular bacterial pathogens. Both TNFRI and TNFRII can be released from cell surface by ectodomain shedding. The resulting soluble TNFRI and TNF-RII can bind TNF with high affinity and modulate TNF effects. An in vitro study showed that both TNFRI and TNFRII are constitutively released from monocytes. LPS stimulation can further increase soluble TNFRII release. It has been reported that TNFRII polymorphism is associated with some lymphomas, solid tumors, and autoimmune diseases. The plasma level of soluble TNFRII is increased in obese people and is related to insulin resistance. In addition, recombinant Fc-tagged soluble TNFRII has been used to treat rheumatoid arthritis.
Product DetailsProduct Details
- Source
- Mouse TNFRII (CD120b), amino acids (Val23-Gly258) (Accession#: Q545P4), was expressed in E. coli.
- Molecular Mass
- The 236 amino acid recombinant protein has a predicted molecular mass of approximately 25.46 kD. The protein migrates at approximately 26 kD in DTT-reducing conditions and at approximately 25 kD in non-reducing conditions respectively by SDS-PAGE. The predicted N-terminal amino acid is Val.
- Purity
- >98%, as determined by Coomassie stained SDS-PAGE.
- Formulation
- 0.22 µm filtered protein solution is in 20 mM glycine, 150 mM NaCl, pH 3.0.
- Endotoxin Level
- Less than 0.01 ng per µg cytokine as determined by the LAL method.
- Concentration
- 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.
- Activity
- ED50 = 0.6 - 1.5 µg/mL as determined by a dose-dependent inhibition of 0.1 ng/mL mouse TNF-α induced cytotoxicity in L929 mouse fibroblast cells in the presence of 4 µg/mL actinomycin D.
- 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 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 tech@biolegend.com.
Antigen Details
- Structure
- Cytokine receptor.
- Distribution
-
TNFRII is expressed in T cells, astrocytes, oligodendrocytes, monocytes, endothelial cells, human mesenchymal stem cells, macrophages, and Langerhans cells. Soluble TNFRII can be detected in the urine and the blood.
- Function
- TNFRII transduces TNF signals through TRAF2. Soluble TNFRII can neutralize the biological activity of TNF, which dampens the inflammatory responses. The level of circulating soluble TNFRII is increased in patients with sepsis, cancer, HIV, and autoimmune diseases.
- Ligand/Receptor
- TNF.
- Biology Area
- Cell Biology, Immunology, Innate Immunity, Neuroinflammation, Neuroscience, Transcription Factors
- Molecular Family
- Soluble Receptors, Cytokine/Chemokine Receptors, CD Molecules
- Antigen References
-
1. Hehlgans T, Mannel DN. 2002. Biol. Chem. 383:1581.
2. Glossop JR, et al. 2005. Arthritis Res. Ther. 7:R1227.
3. Kollias G, Kontoyiannis D. 2002. Cytokine Growth Factor Rev. 13(4-5):315-21.
4. Gordon AC, et al. 2004. Genes Immun. 5:631.
5. Lantz M, et al. 1990. Cytokine 2:402.
6. Nophar Y, et al. 1990. EMBO. J. 9:3269.
7. Eisel UL, et al. 2011. FEBS. J. 278:888. - Gene ID
- 21938 View all products for this Gene ID
- UniProt
- View information about CD120b 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)
Follow Us