Recombinant Mouse NGFR (TNFRSF16)-Fc Chimera (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
Nerve Growth Factor Receptor, NGF Receptor, TNFRSF16, CD271, CD271 Antigen, Low Affinity Neurotrophin Receptor P75NTR, P75NTR
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Mouse_NGFR-Fc_Chimera_CF_RECOM_1_043020.png
Recombinant mouse NGFR (TNFRSF16)-Fc chimera inhibits the proliferation of TF-1 human erythroleukemia cells induced by recombinant mouse β-NGF (Cat. No. 784002). The ED50 for this effect is 0.05 - 0.25 µg/mL.
  • Mouse_NGFR-Fc_Chimera_CF_RECOM_1_043020.png
    Recombinant mouse NGFR (TNFRSF16)-Fc chimera inhibits the proliferation of TF-1 human erythroleukemia cells induced by recombinant mouse β-NGF (Cat. No. 784002). The ED50 for this effect is 0.05 - 0.25 µg/mL.
  • Mouse_NGFR-Fc_Chimera_CF_RECOM_2_043020.png
    Stability Testing for Recombinant Mouse NGFR (TNFRSF16)-Fc chimera. Recombinant mouse NGFR (TNFRSF16)-Fc Chimera was aliquoted in PBS, pH 7.2 at 0.2 mg/mL. One aliquot was frozen and thawed four times (4x Freeze/Thaw) and compared to the control that was kept at 4°C (Control). The samples were tested for their ability to inhibit the proliferation of TF-1 human erythroleukemia cells induced by recombinant mouse β-NGF (Cat. No. 784002). The ED50 for this effect is 0.05 - 0.25 µg/mL.
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791208 500 µg 1032€
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791202 10 µg 76€
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791204 25 µg 137€
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791206 100 µg 526€
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Description

Mouse nerve growth factor receptor (NGFR) is a type 1 transmembrane glycophosphoprotein of approximately 75 kD. It belongs to the low affinity neurotrophin receptor and tumor necrosis factor receptor superfamily. NGFR possesses an extracellular domain containing four 40 amino acid repeats with six cysteine residues at conserved positions, followed by a serine/threonine rich domain, a transmembrane, and an intracellular domain with 155 amino acids without kinase activity. Disruption of the cysteine-rich repeats leads to loss of ligand binding. NGFR induces different effects depending on its interaction with other proteins. Its interaction with sortilin induces apoptotic responses, while its interaction with Lingo-1 and Nogo-A participates in the myelin-dependent inhibition of axonal growth. Interaction with the neurotrophin tyrosine kinase receptors (Trks) promotes survival, axonal growth, and differentiation of neural cells. NGFR interaction with TrkA induces neural cell death, neurite growth, neuronal differentiation, and synaptic plasticity. The presence of NGFR/CD271 defines a subset of multipotential mesenchymal stromal cells derived from bone marrow. NGFR is identified as a marker of tumor initiating cells in human melanoma, esophageal carcinoma, hypopharyngeal carcinoma, and head and neck squamous cell carcinomas. In addition, NGFR has been associated with glioblastoma cell migration and invasion.

Product Details
Technical Data Sheet (pdf)

Product Details

Source
Mouse NGFR, amino acid Gly30-Asn253 (Accession # Q9Z0W1), with mIgG-Fc tag in the carboxi terminus, was expressed in CHO cells.
Molecular Mass
The 464 amino acid recombinant protein has a predicted molecular mass of approximately 50.9 kD. The DTT-reduced and non-reduced protein migrates at approximately 75 kD and 140 kD by SDS-PAGE, respectively. The predicted N-terminal amino acid is Gly.
Purity
> 95%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution in PBS
Endotoxin Level
Less than 0.1 EU 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
Recombinant mouse NGFR-Fc Chimera inhibits the proliferation of TF-1 human erythroleukemia cells induced by recombinant mouse β-NGF (Cat. No. 784002). The ED50 for this effect is 0.05 - 0.25 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 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
Dimer
Distribution

Neurons, Schwann cells, mesenchymal stem and stromal cells, dermal stem cells, follicular dendritic cells, and melanocytes.

Function
In the nervous system, NGFR induces survival, differentiation, and migration of neuronal cells. ProNGF binds and activates NGFR resulting in cell death of endothelial cells. Epidermal CD271+ stem cells play an important role in wound healing.
Interaction
Neurons and endothelial cells
Ligand/Receptor
NGF, proNGF, BDNF, proBDNF, NTF3, and NTF4
Bioactivity
Mouse NGFR inhibits the proliferation of TF-1 human erythroleukemia cells induced by β-NGF.
Cell Type
Mesenchymal cells, Neural Stem Cells, Neurons
Biology Area
Cancer Biomarkers, Cell Biology, Cell Death, Cell Proliferation and Viability, Immunology, Neurodegeneration, Neuroscience, Neuroscience Cell Markers, Stem Cells, Synaptic Biology
Molecular Family
CD Molecules, Growth Factors
Antigen References
  1. Johnson D, et al. 1986. Cell. 47:545.
  2. Bibel M and Barde YA. 2000. Genes Dev. 14:2919.
  3. Barker PA. 2004. Neuron. 4:529.
  4. Iwata Y, et al. 2013. J Dermatol Sci. 71:122.
  5. Negrini S, et al. 2013. Biol. Open. 2:855.
  6. Murillo-Sauca O, et al. 2014. Oncotarget 5:6854.
  7. Fahnestock M and Shekari A. 2019. Front Neurosci. 13:129.
  8. Speidell A, et al. 2019. Front Cell Neurosci. 13:398.
Gene ID
18053 View all products for this Gene ID
UniProt
View information about NGFR 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: 2    Revision Date: 04/30/2024

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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