| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Concentration | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Purity | |
| 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. For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in sterile water at a concentration of at least 0.1 mg/mL. 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. It is recommended to prepare fresh solutions in working buffers just before use. Repeat freeze-thawing may result in loss of activity. |
| Source | Recombinant, HEK 293-6E cells. |
| Storage | |
| Target |
Overview
Human TrkB-Fc Chimera is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to BDNF biology and/or assay development. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows. Researchers commonly pair it with applications such as Western blot.
Key elements and design rationale
- Molecular identity: MW: ~120 kDa.
- Source / origin: Recombinant, HEK 293-6E cells..
- Quality attributes: Purity: >90% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: Yes.
Modifications
Glycosylation
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
TrkB is a receptor tyrosine kinase of the Trk family. It is activated by brain-derived neurotrophic factor (BDNF), neurotrophin-3, -4 and -5 and is involved in the development and maintenance of the nervous system1. TrkB-Fc is a fusion protein combining the extracellular binding domain of TrkB and the Fc domain of human IgG. TrkB-Fc is a tool for studying the biological actions of BDNF 2.A large number of in vitro studies support the notion that TrkB-Fc inhibits BDNF activity3. Addition of TrkB-Fc to hippocampal and cortical slices and cultured cortical, striatal, and dentate granule cells either abolishes or opposes the effect of BDNF. The TrkB-Fc fusion protein, a specific inhibitor of Trk kinase activity, K252, and a TrkB neutralizing antibody all have similar BDNF-blocking effects. In addition, administration of TrkB-Fc in vivo has consequences that are in accordance with decreased BDNF activity. Systemic nerve growth factor treatment, which leads to a condition resembling peripheral inflammation, raises BDNF levels in sensory neurons and increases nociceptive spinal reflex excitability. This increased central excitability is reduced by TrkB-Fc4. Moreover, intraventricular delivery of TrkB-Fc suppresses epileptogenesis, similar to what has been observed in heterozygous BDNF knockout mice and in transgenic mice overexpressing truncated TrkB receptors and with decreased endogenous BDNF levels5. In contrast to these data, Croll et al.2 reported that TrkB-Fc can potentiate BDNF-induced TrkB phosphorylation. However, this effect was observed only when TrkB-Fc and BDNF were coinfused intracerebrally in equimolar concentrations.
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.
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.
Baloh, R.H.
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Klein, R.
et al. (1990) Cell61, 647.
Croll, S.D.
et al. (1998) Exp. Neurol.152, 20.
Shelton, D.L.
et al. (1995) J. Neurosci. 15, 477.
Gustafsson, E.
et al. (2003) Stroke34, 2710.
Lahteinen, S.
et al. (2002) Eur J Neurosci. 15, 721.
Quadrato, G.
et al. (2012) Proc. Natl. Acad. Sci. U.S.A.109, E1499.
Boulle, F.
et al. (2012) Prog. Neurobiol.98, 197.
Duclot, F. and Kabbaj, M.
(2013) J. Neurosci. 33, 11048.
Cabelli, R.J.
et al. (1997) Neuron19, 63.
Kang, H.
et al. (1997) Neuron19, 653.
McAllister, A.K.
et al. (1997) Neuron18, 767.
Croll, S.D.
et al. (1998) Exp. Neurol.152, 20.
