Recombinant Human β-NGF (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
Nerve Growth Factor Beta Subunit, Ngf, Ngfb, Beta-NGF, Nerve GrowthFactor Beta Subunit
Ave. Rating
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Product Citations
publications
a.
Recom_Human-B-NGF_1_CF
Recombinant human β-NGF induces the proliferation of TF-1 cells in a dose-dependent manner. The ED50 for this effect is 0.4 – 4.0 ng/mL.
  • a.
Recom_Human-B-NGF_1_CF
    Recombinant human β-NGF induces the proliferation of TF-1 cells in a dose-dependent manner. The ED50 for this effect is 0.4 – 4.0 ng/mL.
  • b.
Recom_Human-B-NGF_2_CF
    Stability Testing for Recombinant Human β-NGF. Recombinant human β-NGF lyophilized was kept at -20°C (Control), and another sampler was reconstituted in 4 mM HCL and kept at 4°C for two weeks (2w 4°C). The samples were tested by their property to induce the proliferation of TF-1 cells in a dose-dependent manner. The ED50 for this effect is 0.4 – 4 ng/mL.
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788505 50 µg 145 CHF
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Description

Neurotrophins are growth factors that modulate growth, differentiation, and survival of neurons. These structurally related proteins include nerve growth factor (NGF/β-NGF), brain-derived neurotrophic factor (BDNF), neurotrophin-3, and neurotrophin-4/5. Highly homologous, Neurotrophins share a tertiary folded, cysteine rich "knot” region. Neurotrophins are critical to the development of the central and peripheral nervous systems. They also have important roles in injury-induced neuron regeneration. β-NGF is a member of the neurotrophin family which controls growth, survival, and maturation of neurons. In peripheral and central neurons, neurotrophins are important regulators for survival, differentiation, and maintenance of nerve cells. They are detectable throughout embryogenesis and into the adult stage in the central and peripheral nervous systems. In animal models, β-NGF prevents neuronal degeneration and has become a therapeutic target in neuron regeneration studies. β-NGF is also critical for the survival and maintenance of sympathetic and sensory neurons. It is the main neurotrophin that maintains homeostasis of neurogenesis. β-NGF also prevents neurons from undergoing apoptosis and promotes maturation while supporting axonal branching. Two receptors are known to interact withβ- NGF: p75NTR and TrkA. The β-NGF-TrkA signaling pathway induces two pathways through activation of PI3K-Akt or Ras-MAPK. To keep neurons alive, activation of these two pathways may lead to CREB phosphorylation and increase in expression of anti-apoptosis genes. Animal models of neurodegenerative diseases suggest that β-NGF can promote myelin repair of neurons in the peripheral nervous system. Clinical studies indicate that dysregulation of β-NGF signaling is related to Alzheimer's disease.

Product Details
Technical Data Sheet (pdf)

Product Details

Source
Human β-NGF, amino acids (Ser122-Ala241) (Accession# P01138), was expressed in CHO cells.
Molecular Mass
The 120 amino acid recombinant protein has a predicted molecular mass of approximately 13.5kD. The protein migrates at approximately 14.5 kD and 13.5 kD in DTT-reducing and non-reducing conditions respectively by SDS-PAGE. The predicted N-terminal amino acid is Ser.
Purity
> 95%, as determined by Coomassie stained SDS-PAGE.
Formulation
Lyophilized from 0.22 µm filtered protein solution in 0.1% Trifluoracetic Acid (TFA) 5% trehalose.
Endotoxin Level
Less than 0.1 EU per µg of cytokine as determined by the LAL method.
Concentration
50 µg size lyophilized
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C or colder until the expiration date. Reconstitute lyophilized protein in sterile 4 mM HCL. Before reconstitution, make sure the 4 mM HCL and product are at room temperature. Quickly spin the vial or gently tap down on the vial to make sure the lyophilized product is at the bottom of the vial before opening. Use aseptic techniques to add the required volume of reconstitution buffer (sterile 4 mM HCL) to the vial, to obtain the recommended stock concentration 250 µg/mL. Close the vial and leave at ambient temperature for 15-20 minutes. Then gently invert the vial several times or until all of the lyophilized product dissolves. Leave the vial at room temperature for another 15 minutes. If small particulates are still observed after 15 minutes, incubate at room temperature for an additional 30 minutes, and leave the vial at 2°C - 8°C overnight. Next day, invert the vial several times or gently pipette the solution up and down before use. If needed, transfer the reconstituted stock solution to a sterile container for additional dilution to no less than 100 µg/mL. Small working aliquots in polypropylene tubes can be made after reconstitution and store the vials at -20°C or lower. Avoid freeze/thaw cycles. Carrier protein such as 0.2 - 1% endotoxin-free BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to two weeks or stored at -20°C or colder for up to 3 months.
Activity
Recombinant human β-NGF induces the proliferation of TF-1 cells in a dose-dependent manner. The ED50 for this effect is 0.4 – 4.0 ng/mL.
Application

Bioassay

Application Notes

Our lyophilized proteins are validated in-house to maintain activity after shipping at ambient temperature and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.

Antigen Details

Structure
Homodimer
Distribution

Broad expression including hypothalamus, pituitary, thyroid gland, testes, epididymis, vascular smooth muscle cells, fibroblasts, myofibroblasts, mast cells, eosinophils.

Function
Important for the development and maintenance of the sympathetic and sensory nervous systems
Interaction
Neurons, astrocytes, eosinophils, B, T, and mast cells
Ligand/Receptor
Low-affinity NGF receptor (p75NTR), high-affinity NGF receptor (TrkA)
Bioactivity
Human β-NGF induces the proliferation of TF-1 cells.
Cell Type
Neurons
Biology Area
Cell Biology, Neuroscience, Synaptic Biology
Molecular Family
Cytokines/Chemokines, Growth Factors
Antigen References
  1. Ullrich A, et al. 1983. Nature. 303:821.
  2. Klein R, et al. 1991. Cell. 65:189.
  3. Welker P, et al. 2000. Immunology. 99:418.
  4. Fahnestock M, et al. 2004. Prog Brain Res. 146:101.
  5. Bruno MA and Cuello AC. 2006. Proc Natl Acad Sci USA. 103:6735.
  6. Aloe L, et al. 2015. Curr Neuropharmacol. 13:294.
Gene ID
4803 View all products for this Gene ID
UniProt
View information about beta-NGF 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: 06.23.2025

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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