Recombinant Mouse sTNF-RI (TNFRSF1A) (carrier-free)

Pricing & Availability
Other Names
Tumor necrosis factor receptor 1, p75TNFR, cd120a, TNFRSF1A, Tnfrsf1, FPF, TNF-R, TNF-R-I, TNF R1, TNF-R55, TNF-alphaR1, TNFAR, TNFR60, TNFRI
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Product Citations
publications
Mouse_TNF-RI_TNFRSF1A_CF_RECOM_BA_011017
Inhibition of TNFα-induced cytotoxicity in L929 cells by soluble TNF-RI in the presence of actinomycin D.
  • Mouse_TNF-RI_TNFRSF1A_CF_RECOM_BA_011017
    Inhibition of TNFα-induced cytotoxicity in L929 cells by soluble TNF-RI in the presence of actinomycin D.
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Cat # Size Price Quantity Avail. Save
763202 10 µg $125
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763204 25 µg $215
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763206 100 µg $585
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763208 500 µg $1,585
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Description

The biological effects of TNF are mediated by two cell surface TNF receptors, TNF-RI and TNF-RII. TNF-RI and TNF-RII are structurally related but functionally distinct. Also, TNF-RI is widely expressed on most cells whereas TNF-RII is more restricted and is primarily expressed in hematopoietic cells and cells of the immune system. Most of the biological effects of TNF are mediated by TNF-RI. TNF-RI can be activated by both membrane bound and soluble TNF. TNF-RI contains a cytoplasmic death domain which mediates the induction of apoptosis or NF-kB activation. After TNF binding, the death domain can recruit TRADD which in turn will further recruit FADD or TRAF2. FADD will initiate apoptosis signal by mediating caspase-8 activation. TRAF2 will exert survival effects through NF-kB activation which will induce the expression of antiapoptotic genes such as BcL-2. Like TNFα, TNF-RI and TNF-RII also undergo ectodomain shedding. The resulting soluble TNF-RI and TNFR-II can bind TNF with high affinity and modulate TNF effects. TNF-RI shedding is catalyzed by TNF-alpha converting enzyme (TACE). Human soluble TNF-RI is constitutively released in the general circulation and its level increases in many diseases including rheumatoid arthritics and inflammatory bowel disease. Impaired TNF-RI shedding due to TNF-RI mutation will cause TNF receptor associated periodic syndrome (TRAPS). TNF-RI shedding also plays a protective role in TNF-alpha sensitization of hepatocytes to Fas-mediated death.

Product Details
Technical data sheet

Product Details

Reactivity
Mouse
Source
Mouse sTNF-RI, amino acids Ile22-Ala212 (Accession #: BC004599.1) was expressed in E. coli.
Molecular Mass
The 191 amino acid recombinant protein has a predicted molecular mass of approximately 21.1 kD. The protein migrates at approximately 22 kD in DTT-reducing conditions and at approximately 19 kD in non-reducing conditions by SDS-PAGE. The N-terminal amino acid is Ile.
Purity
>98%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution is in PBS.
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 (please contact technical support for concentration, or use our Lookup tool if you have a lot number.)
Please note, new lots of the 100 µg size will be lot-specific and may differ from previous lots that had a fixed concentration.
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
The ED50 is 0.3-1.5 µg/ml, as determined by a dose-dependent inhibition of the 0.1 ng/ml mouse TNF-α induced cytotoxicity in the L929 mouse fibroblast cells in the presence of 4 µg/ml actinomycin D.
Recommended Usage

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
Cytokine receptor
Distribution

TNF-RI is widely expressed and soluble TNF-RI can be detected in blood and urine.

Function
TNF-RI is a trimeric cytokine that binds TNF and is constitutively released into the body circulation by ectodomain shedding. Soluble TNF-RI level is elevated in various disease conditions. Shedding of TNF-RI can also be enhanced by chemical compounds including nitric oxide, hydrogen peroxide or phorbol myristate acetate.
Ligand/Receptor
TNF
Biology Area
Apoptosis/Tumor Suppressors/Cell Death, Cell Biology, Immunology, Innate Immunity, Mitochondrial Function
Molecular Family
Soluble Receptors, Cytokine/Chemokine Receptors
Antigen References

1. Hehlgans T and Mannel DN. 2002. Biol. Chem. 383:1581
2. Kollias G and Kontoyiannis D. 2002. Cytokine Growth Factor Rev. 13:315
3. Naude PJ, et al. 2011. FEBS J. 278:888
4. Huggins ML, et al. 2004. Arthritis Rheum. 50:2651
5. Hanai H, et al. 2004. Am. J. Gastroenterol. 99:1532.

Gene ID
21937 View all products for this Gene ID
UniProt
View information about sTNF-RI on UniProt.org

Related FAQs

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.

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.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)
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.

Go To Top Version: 1    Revision Date: 01/16/2017

For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). 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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