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Recombinant Human, Mouse, Rat, Cynomolgus, Canine BDNF Protein

Cat # Size Price Quantity
63290120 μg$235
632902100 μg$725
632903500 μg$1450

  Bulk/Custom

Product Details

ApplicationBioassay
FormatLyophilized from sterile 20 mM HEPES, 500 mM NaCl, pH7.5.
Expression HostE.coli
Target NameBDNF, Brain-derived neurotrophic factor
SpeciesHuman, Mouse, Rat, Cynomolgus, Canine
accession numberP23560-1
SourcesA DNA sequence encoding the Human / Mouse / Rat / Cynomolgus / Canine BDNF (P23560-1) (His129-Arg247) was expressed.
Molecular WeightThe recombinant Human / Mouse / Rat / Cynomolgus / Canine BDNF comprises 119 amino acids and has a predicted molecular mass of 13.51 KDa.
Affinity TagNone
Purity≥95% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC
Regulatory StatusRUO
Endotoxin level< 0.1 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

Brain-derived neurotrophic factor (BDNF) is a member of the neurotrophin family of growth factors and plays a critical role in neuronal development, survival, differentiation, and synaptic plasticity. It is widely expressed in the central nervous system, particularly in the hippocampus, cerebral cortex, and other regions involved in learning, memory, and emotion. BDNF supports the growth and maintenance of neurons, promotes dendritic development, and regulates synaptic strength, making it essential for experience-dependent changes in neural circuits. It also contributes to adult neurogenesis and activity-dependent neuronal adaptation.



BDNF is encoded as a precursor protein, preproBDNF, which undergoes proteolytic processing to generate proBDNF and mature BDNF. Mature BDNF is a small, approximately 27-kDa homodimer composed of two polypeptide chains, each containing about 119 amino acids. It adopts the characteristic cysteine-knot structure of neurotrophins. BDNF primarily binds to tropomyosin receptor kinase B (TrkB, encoded by NTRK2), a receptor tyrosine kinase that activates intracellular pathways including MAPK/ERK, PI3K/AKT, and PLCγ signaling. ProBDNF can preferentially interact with the p75 neurotrophin receptor (p75NTR), often together with sortilin, and may promote synaptic remodeling or cell-death pathways depending on cellular context. Thus, the biological effects of BDNF depend partly on its processing and receptor engagement.



Altered BDNF expression or signaling has been associated with several neurological and psychiatric conditions, including depression, anxiety disorders, schizophrenia, Alzheimer's disease, and other neurodegenerative disorders. These relationships are complex, and changes in BDNF are not necessarily causal or consistent across diseases, brain regions, or stages of illness. BDNF signaling is also important in pain processing and neuronal recovery after injury.



Therapeutically, BDNF and TrkB signaling are being investigated as targets for promoting neuronal survival, synaptic repair, and functional recovery in neurodegenerative diseases, stroke, and nerve injury. Direct BDNF delivery is challenging because of limited blood-brain barrier penetration and restricted distribution. Consequently, research includes TrkB agonists, gene-based approaches, and strategies to enhance endogenous BDNF production.

Data Sheets

Recombinant Human, Mouse, Rat, Cynomolgus, Canine BDNF 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.

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