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

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Other Names
p75 neurotrophin receptor ( p75NTR), Gp80-LNGFR, CD271, TNFRSF16
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NGFR_TNFRSF16_FcChimera_Human_RECOM_BA_112415
Human NGFR inhibits the proliferation of TF-1 human erythroleukemia cells induced by β-NGF.
  • NGFR_TNFRSF16_FcChimera_Human_RECOM_BA_112415
    Human NGFR inhibits the proliferation of TF-1 human erythroleukemia cells induced by β-NGF.
Cat # Size Price Quantity Avail. Save
754002 10 µg $125
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754004 25 µg $215
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754006 100 µg $595
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754008 500 µg $1,595
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Description

Human nerve growth factor receptor (NGFR) is a type 1 transmembrane glycophosphoprotein of approximately of 75 kD and it belongs to the low affinity neurotrophin receptor and tumor necrosis factor receptor superfamily. It is characterized by an extracellular domain containing four 40 amino acid repeats with six cysteine residues at conserved positions, and disruption of these 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. Interacting with the neurotrophin tyrosine kinase receptors (Trks) promotes survival, axonal growth, and differentiation of neural cells. The presence of NGFR/CD271 defines a subset of multipotential mesenchymal stromal cells derived from bone marrow. It has been identified as a marker of tumor initiating cells in human melanoma, esophageal carcinoma, hypopharyngeal carcinoma, and head and neck squamous cell carcinomas. Also, NGFR has been associated with glioblastoma cell migration and invasion.

Product Details
Technical data sheet

Product Details

Reactivity
Human
Source
Human NGFR, amino acids (Lys29-Asn250) (Accession# NM_002507) was expressed in 293E cells. The C-terminus contains human IgG Fc-6 His-tag
Molecular Mass
The 462 amino acid recombinant protein has a predicted molecular mass of approximately 50.7 kD. The protein migrates at approximately 60 - 70 kD in DTT-reducing conditions and at approximately 150 kD in non-reducing conditions by SDS-PAGE. The predicted N-terminal amino acid is Lys.
Purity
>95%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution is in PBS, pH 7.2.
Endotoxin Level
Less than 0.1 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
ED50 = 0.4 - 2 µg/mL as measured by its ability to inhibit the proliferation of TF-1 human erythroleukemia cells induced by β-NGF.
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
Receptor.
Distribution
Neurons, Schwann cells, mesenchymal stem and stromal 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.
Interaction
Neurons and endothelial cells.
Ligand/Receptor
Interacts with neurotrophins: NGF, proNGF, brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT3), and neurotrophin-4 (NT4).
Biology Area
Apoptosis/Tumor Suppressors/Cell Death, Cell Biology, Immunology, Neuroscience, Stem Cells, Synaptic Biology
Molecular Family
CD Molecules, Postsynaptic proteins, Cytokine/Chemokine Receptors, Soluble Receptors
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. Negrini S, et al. 2013. Biol. Open. 2:855.
5. Murillo-Sauca O, et al. 2014. Oncotarget 5:6854.
6. Shanab A, et al. 2015. Mol. Ther. Methods Clin. Dev. 2:15013.

Gene ID
4804 View all products for this Gene ID
UniProt
View information about NGFR 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: 2    Revision Date: 04/04/2016

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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Toll-Free Phone: 1-877-Bio-Legend (246-5343) Phone: (858) 768-5800 Fax: (877) 455-9587

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