BDNF Protein Overview: Sequence, Structure, Function and Protein Interaction

BDNF Protein Overview

Jones and Reichardt (1990) noted that during normal vertebral development, up to 80% of the neurons in diverse cell populations within the forming nervous system die. This is thought to be a mechanism that ensures that adequate numbers of neurons establish appropriate innervation densities with effector organs or other neuronal populations. In several instances, the innervation target of a population of neurons has been shown to have a crucial role in regulating the number of surviving neurons. Targets of neuronal innervation produce a limited supply of neurotrophic factors, and competition between neurons responsive to these factors determines which neurons survive. In addition to nerve growth factor (NGF; 162030), BDNF has been purified and shown in vivo to reduce the amount of naturally occurring neuronal cell death in portions of the peripheral nervous system (Hofer and Barde, 1988). Jones and Reichardt (1990) cloned human BDNF, which encodes a deduced 247 preproprotein that is proteolytically processed into a mature 119-amino acid protein. The mature BDNF protein shares 100% identity with mature porcine Bdnf and 52% identity with mature human NGF. Northern blot analysis detected BDNF transcripts of 1.6 and 4.0 kb in all brain regions examined. Maisonpierre et al. (1991) cloned the human and rat genes encoding BDNF. They demonstrated that the mature form was identical in all mammals examined. Furthermore, the tissue distributions and neuronal specificities are conserved among mammals. By database analysis and RT-PCR, Liu et al. (2005) identified 9 alternatively spliced BDNF transcripts. The transcripts differ in their use of alternative promoters, alternative splice donor and acceptor sites, and alternative polyadenylation sites. Most transcripts encode the previously identified proBDNF; however, 2 transcripts contain additional in-frame methionines that may result in proteins with longer N termini, and another transcript encodes a protein with an internal deletion of 48 amino acids. RT-PCR revealed a complex pattern of BDNF transcripts in brain and a more simple pattern of expression in peripheral tissues. Liu et al. (2005) also identified noncoding RNAs transcribed from a gene that overlaps with BDNF on the opposite strand (BDNFOS; 611468). By in silico analysis, RT-PCR of adult frontal cerebral cortex, medulla, and hippocampus total RNA, and 5-prime RACE of adult hippocampus and cerebellum RNA, Pruunsild et al. (2007) identified numerous BDNF transcripts. The transcripts differ in the length of their 5-prime UTR, and most encode proBDNF. RT-PCR detected tissue-specific expression of BDNF variants. Most showed highest expression in brain, although several alternative transcripts showed relatively high expression in nonneural tissues. The BDNF variants showed variable expression in all specific brain regions examined, and all were expressed at high levels in mammillary body, pons, hippocampus, frontal cortex, colliculi, and olfactory tract. By examining expression of Bdnf transcripts in rat and mouse brain, An et al. (2008) found that mRNAs with short 3-prime UTRs were restricted to somata, whereas those with long 3-prime UTRs also localized to dendrites.

BDNF protein family

Belongs to the NGF-beta family.

BDNF protein name

Recommended name
Brain-derived neurotrophic factor
Short name
Alternative name

BDNF Gene family protein

BDNF Protein Sequence

Species Human BDNF protein
Length 247
Mass (Da) 27818
Sequence Human BDNF protein sequence
Species Mouse BDNF protein
Length 249
Mass (Da) 28123
Sequence Mouse BDNF protein sequence
Species Rat BDNF protein
Length 249
Mass (Da) 28109
Sequence Rat BDNF protein sequence

BDNF Protein Molecular Weight & PI

Brain-derived neurotrophic factor precursor (BDNF) (Abrineurin)Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 129-247 Brain-derived neurotrophic factor.

Molecular weight (Da)


Theoretical pI


BDNF Protein Structure

1999-02-01   Released:  1999-02-09
Deposition Author(s)
Robinson, R.C., Radziejewski, C., Stuart, D.I., Jones, E.Y., Choe, S.
Homo sapiens
Expression System
Escherichia coli
Experimental Data Snapshot
2.7500 Å
R-Value Free
R-Value Work
1B8M From PDB

Human BDNF protein Secondary structure

BDNF Protein Interaction

Recombinant BDNF Protein Feature

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

High Purity
> 95 % as determined by SDS-PAGE
Low Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
High Activity
1. Measured by its ability to bind biotinylated human TrkB-His (Cat:10047-H08H) in functional ELISA. 2. Measured by its ability to bind Human TrkB-Fch (Cat:10047-H03H) in functional ELISA. 3. Measured by its ability to bind biotinylated mouse TrkB-His (Cat:50132-M08H) in functional ELISA.

Recombinant BDNF protein citations

Three-dimensional hydrogel scaffolds facilitate in vitro self-renewal of human skin-derived precursors
Wang, X;Liu, S;Zhao, Q;Li, N;Zhang, H;Zhang, X;Lei, X;Zhao, H;Deng, Z;Qiao, J;Cao, Y;Ning, L;Liu, S;Duan, E;
Acta Biomater
Amyloid-Beta 1-42 Cross-Reactive Antibody Prevalent in Human Sera May Contribute to Intraneuronal Deposition of A-Beta-P-42
Vojdani, A;Vojdani, E;
International Journal of Alzheimer's Disease
Development of an innervated tissue-engineered skin with human sensory neurons and Schwann cells differentiated from iPS cells
Muller, Q;Beaudet, MJ;De Serres-Bérard, T;Bellenfant, S;Flacher, V;Berthod, F;
Acta Biomater
In vitro affinity optimization of an anti-BDNF monoclonal antibody translates to improved potency in targeting chronic pain states in vivo
Stack, E;McMurray, S;McMurray, G;Wade, J;Clark, M;Young, G;Marquette, K;Jain, S;Kelleher, K;Chen, T;Lin, Q;Bloom, L;Lin, L;Finlay, W;Suzuki, R;Cunningham, O;
Therapeutic potential of a TrkB agonistic antibody for Alzheimer's disease
Wang, S;Yao, H;Xu, Y;Hao, R;Zhang, W;Liu, H;Huang, Y;Guo, W;Lu, B;

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