b NGF Human, HEK
Description
Expression Systems and Production
HEK293 cells are preferred for producing bioactive b NGF due to:
-
Post-translational modifications: Native-like glycosylation enhances protein stability and receptor binding
-
Yield: Milligram-scale production with >95% purity via affinity chromatography
-
Xeno-free conditions: Serum-free media eliminate animal-derived contaminants
Comparative expression data:
| Host System | Disulfide Bonding | Glycosylation | Bioactivity (EC₅₀) |
|---|---|---|---|
| HEK293 | Non-covalent | Yes | 0.5-3.0 ng/mL |
| E. coli | Covalent | No | 1.31 ng/mL |
Neuronal Effects
-
Survival: Binds TrkA/p75NTR receptors to activate PI3K/Akt and Ras/MAPK pathways, preventing apoptosis in sympathetic/sensory neurons
-
Differentiation: Induces neurite outgrowth at EC₅₀ = 0.5-3.0 ng/mL
Non-Neuronal Roles
-
Immune modulation: Regulates cytokine production in T-cells and mast cells
-
Stress response: Mediates cross-talk between endocrine and CNS limbic systems
Therapeutic Applications
Recent studies demonstrate:
Product Specs
HEK293 cells.
Product Science Overview
Beta Nerve Growth Factor (β-NGF) is a crucial neurotrophic factor that plays a significant role in the development, maintenance, and survival of neurons. It belongs to the nerve growth factor protein superfamily and is involved in the regulation of growth and differentiation of sympathetic and certain sensory neurons .
The discovery of NGF dates back to the pioneering work of Nobel Prize winner Rita Levi-Montalcini, who identified its role in neuronal growth and survival. This groundbreaking research laid the foundation for understanding the complex mechanisms of neurotrophic factors and their therapeutic potential .
Human recombinant β-NGF is produced using HEK293 cells, a type of human embryonic kidney cell line. The recombinant form is a noncovalently disulfide-linked homodimer, glycosylated polypeptide chain containing 118 amino acids with a molecular mass of 26.5 kDa . This production method ensures high purity and biological activity, making it suitable for research and therapeutic applications .
β-NGF is a key mediator in neuronal and non-neuronal development, differentiation, and survival. It binds to the tyrosine kinase A receptor with high affinity and to the p75 neurotrophin receptor with low affinity . This binding triggers signaling pathways that promote neuronal growth, survival, and regeneration .
The clinical application of β-NGF has been explored in various therapeutic areas. One notable example is the FDA-approved drug cenegermin-bkbj, a recombinant human NGF used for the treatment of neurotrophic keratitis . This approval marks a significant milestone in translating NGF research into practical medical treatments.
Despite its potential, the clinical application of β-NGF has faced challenges, including determining appropriate dosing, administration strategies, and production complexities . However, ongoing research and advancements in biotechnology continue to address these challenges, paving the way for broader therapeutic applications.
