| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | Brain-Derived Neurotrophic Factor, TrkB receptors |
| Concentration | |
| Conjugate | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Reconstitution | |
| Solubility | Centrifuge the vial before adding solvent (10,000 x g for 5 minutes) to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Tap the vial to aid in dissolving the lyophilized product. Tilt and gently roll the liquid over the walls of the vial. Avoid vigorous vortexing. Light vortexing for up to 3 seconds is acceptable if needed. The product is soluble in pure water at high micromolar concentrations (50 µM - 1 mM). For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in sterile water at a concentration between 100-1000x of the final working concentration. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. Centrifuge all product preparations before use. It is recommended to prepare fresh solutions in working buffers just before use. Avoid multiple freeze-thaw cycles to maintain biological activity. |
| Source | Modified recombinant protein, E. coli |
| Storage | |
| Target |
Overview
human BDNF-Biotin is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to p75NTR, TrkB receptors biology and/or assay development. The reagent is provided as a Biotin conjugate, supporting detection or imaging workflows where applicable. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows. Researchers commonly pair it with applications such as Western blot, Fluorescence staining, Live cell imaging, Immunofluorescence.
Key elements and design rationale
- Molecular identity: MW: ~28 kDa (dimer).
- Source / origin: Modified recombinant protein, E. coli.
- Quality attributes: Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
LC-Biotin
When used as a biochemical or pharmacological tool, results are best interpreted relative to the experimental system (species, expression level, and assay readout) and with appropriate negative and competition-style controls where relevant. This product is intended for research use only.
Biological background
Few examples in the literature emphasize the importance of using BDNF-biotin in living cells experiments. Pardridge, W.M et al. demonstrated that the delivery of BDNF to the brain is non-existent owing to the combined effects of neglible blood brain barrier (BBB) transport and rapid systemic clearance1. The brain delivery of BDNF may be increased by conjugating biotinylated BDNF to BBB drug delivery vectors, such as neutral avidin conjugated to murine monoclonal antibody to the rat transferrin receptor1. Zhang, Y. and Pardridge, W.M further showed that when BDNF is formulated to enable transport across the BBB, the intravenous administration of BDNF results in the reduction in stroke volume and improvement in functional outcome2.Du, J. et al. detected by using BDNF-biotin the ligand-induced TrkB internalization in cultured hippocampal neurons3.Bhattacharyya, A. et al. showed in mature sciatic nerves, that biotinylated BDNF activated Trk receptors function as rapid retrograde signal carriers to execute remote responses to target-derived neurotrophins4.Song, X.Y. et al. proved that exogenous BDNF-biotin is transported by the peripheral nerves following injection into the rat footpad and can be found in the sciatic nerves in fibres and vesicles5. Their data suggest that peripherally applied BDNF may have therapeutic effects on injured spinal cord. Xie, W. et al. followed the trafficking of QD-BDNF (Quantum Dot-BDNF) after its internalization at the axon terminal6. Their result showed that QD-BDNF could be used to track the movement of exogenous BDNF in neurons over long distances and to study the signaling organelles that contain BDNF6.
Research relevance and current trends
- Using high-specificity ligands, toxins, and engineered peptides to dissect closely related receptor/channel subtypes and signaling microdomains.
- Pairing labeled (e.g., fluorescent) proteins/peptides with advanced imaging to map surface expression, trafficking, and nanoscale organization.
- Increasing emphasis on reproducibility through standardized characterization (identity, purity, and lot QC) and transparent reporting of reagent attributes.
Common research applications
- Western blot: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Fluorescence staining: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Live cell imaging: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Immunofluorescence: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
Across these use cases, changes in signal or functional readout are generally interpreted as evidence of differences in target abundance, accessibility, or engagement, but alternative explanations (matrix effects, off-target interactions, or assay artifacts) should be considered.
Notes for experimental interpretation
- Assay context matters: binding assays, functional modulation, and detection workflows can yield different readouts even for the same target system.
- Target complexity: closely related family members, splice variants, and post-translational modifications can influence apparent specificity and potency.
- Matrix and sample effects: buffer composition, detergents, and biological matrices may alter stability or apparent activity; interpret with appropriate controls.
- Control concepts: include negative controls and orthogonal validation (e.g., genetic perturbation or alternative reagents) to support robust interpretation.
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
Koliatsos, V.E.
et al. (1993) Neuron 10, 359.
Zhang, Y. and Pardridge, W.M.
(2006) Brain Res.1111, 227.
Du, J.
et al. (2003) J. Cell Biol.163, 385.
Bhattacharyya, A.
et al. (1997) J. Neurosci. 17, 7007.
Song, X.Y.
et al. (2008) PLoS ONE3, e1707.
Xie, W.
et al. (2012) Integr. Biol.4, 953.
Xie, W.
et al. (2012) Integr. Biol.4, 953.
Pardridge, W.M.
et al. (1994) Pharmaceut. Res. 11, 738.
Jing, S.
et al. (1992) Neuron9, 1067.
Jing, S.
et al. (1992) Neuron9, 1067.
