Recombinant Human Beta-NGF Protein

Cat # Size Price Quantity
63360120 μg$75
633602100 μg$220

Product Details


ApplicationBioassay
FormatLyophilized from sterile 40 mM His, 40 mM Arg, 150 mM NaCl, pH5.5
Expression HostStable CHO
Target Namebeta-NGF, Beta-nerve growth factor, Ngf, Ngfb, Nerve Growth Factor Beta Subunit
SpeciesHuman
accession numberNP_002497.2
SourcesA DNA sequence encoding the mature form of human β-NGF (NP_002497.2) (Ser 122-Arg 239) was expressed.
Molecular WeightThe mature recombinant human β-NGF consists of 118 amino acids and has a predicted molecular mass of 13.2 KDa. β-NGF exists as a non-disulfide linked homodimer in solution.The molecular weight of this protein is around 29.7KDa verified by SEC-MALS (Routinely tested).
Affinity TagNone
Purity≥95% as determined by SDS-PAGE. ≥90% as determined by SEC-HPLC.
Regulatory StatusRUO
Endotoxin level< 1.0 EU per μg protein
Protein ConcentrationLyophilized
Storage and HandlingSamples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Background Information


Human beta-nerve growth factor (β-NGF), also known as NGF, is a neurotrophin that plays a crucial role in the development, survival, maintenance, and function of neurons. It is particularly important for sympathetic and sensory neurons and contributes to neuronal differentiation, axonal growth, synaptic plasticity, and pain perception. NGF also influences immune responses and tissue repair by interacting with neuronal and non-neuronal cells.



Human β-NGF is synthesized as a precursor protein, prepro-NGF, which undergoes proteolytic processing to produce mature NGF. The mature protein consists of 120 amino acids per subunit and forms a biologically active homodimer stabilized by intermolecular interactions and disulfide bonds. Its structure features the characteristic cystine-knot fold shared by neurotrophins. NGF belongs to the neurotrophin family, which also includes brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4).



NGF exerts its effects primarily through two receptors: tropomyosin receptor kinase A (TrkA/NTRK1), a high-affinity receptor tyrosine kinase, and p75 neurotrophin receptor (p75NTR/NGFR), a member of the tumor necrosis factor receptor superfamily. TrkA activation promotes neuronal survival, growth, and differentiation through downstream signaling pathways such as MAPK/ERK, PI3K/AKT, and PLCγ. The p75NTR receptor can modulate TrkA signaling and, depending on the cellular context and available co-receptors, influence cell survival or apoptosis. ProNGF can also interact with p75NTR and sortilin, contributing to distinct biological responses.



Abnormal NGF signaling is associated with chronic inflammatory pain, neuropathic pain, osteoarthritis, and certain neurological conditions. Elevated NGF levels can sensitize sensory neurons and increase pain signaling. Therapeutically, recombinant NGF has been investigated for promoting nerve regeneration and treating selected neurological disorders, while anti-NGF monoclonal antibodies have been developed to reduce chronic pain. Because NGF also supports essential neuronal functions, therapeutic strategies must balance pain relief with potential neurological and musculoskeletal adverse effects.

Data Sheets


Recombinant Human Beta-NGF Protein TDS

Frequently Asked Questions


What are InnoCyto's Cytokines and Growth Factors?
These are recombinantly expressed signaling proteins, including interleukins, interferons, chemokines, and growth factors, that mediate cell communication, proliferation, differentiation, and immune activation. They are produced for use as research reagents to stimulate, modulate, or study cellular responses in vitro and in vivo.

What expression systems are these proteins produced in, and does it matter for my application?
Cytokines and growth factors may be produced in mammalian, insect, or E. coli expression systems depending on the protein, and the system affects properties like glycosylation, folding, and bioactivity. Non-glycosylated proteins from E. coli are often suitable for cell culture stimulation assays, while glycosylation-dependent proteins may require mammalian- or insect-expressed versions for full biological activity — check the product page for the expression system and recommended applications.

How is bioactivity measured and confirmed for each lot?
Bioactivity is typically confirmed using a functional cell-based assay (e.g., proliferation, differentiation, or reporter assay) relevant to the specific cytokine or growth factor, and is reported as an EC50/ED50 value or specific activity (units/mg) on the Certificate of Analysis. Always reference the lot-specific CoA rather than assuming activity is identical across lots or products.

Are these proteins carrier-free, and does that matter for my experiment?
Carrier-free formulations (without BSA or other stabilizing proteins) are available for applications where carrier protein could interfere with downstream analysis, such as certain in vivo studies or proteomic work, while carrier-containing formulations offer improved stability for routine cell culture use. Choose the format that matches your assay's sensitivity to background protein content.

Can these cytokines and growth factors be used for in vivo studies?
Mouse proteins may be used in vivo, but suitability depends on your endotoxin requirements for in vivo use. Endotoxin minimum threshholds vary by product and are indicated on the individual product page. Always confirm the endotoxin specification and formulation on the Certificate of Analysis before using a product in an in vivo setting.

Have a product or application question? Consult our FAQs or contact us.