| 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 TrkC-Fc Chimera is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to NT-3 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: ~100 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
TrkC-Fc chimera is a recombinant protein, a soluble fusion of the TrKC receptor which comprises the extracellular domains of the human TrkC fused to the IgG heavy chain. TrkC-Fc has the binding specificity and affinity of TrkC receptor that can block the biological activity of neurotrophin-31.The neurotrophin family includes four members- nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4). These are encoded by NGF, BDNF, NTF3, and NTF4 human genes, respectively2.Neurotrophins activate in part Trk family receptor protein-Tropomyosin related kinases. The Trk family includes three members: TrkA, TrkB, and TrkC, encoded by NTRK1, NTRK2, and NTRK3 human genes, respectively. TrkC has the highest affinity for NT-32.The Trk structure includes a cytoplasmic domain containing several sites of tyrosine phosphorylation which are responsible for activating intracellular signaling cascades. The extracellular domain consists of a cysteine-rich cluster followed by three leucine-rich repeats, another cysteine-rich cluster and two immunoglobulin-like domains3,4.
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.
Angrist, M.
et al. (1998) Genomics 48, 354.
Ramos, B.
et al. (2009) Mol. Cell. Neurosci. 42, 152.
Green, S.H.
et al. (2012) Anat. Rec. 295, 1877.
Huang, E.J.
et al. (2003) Annu. Rev. Biochem.72, 609.
Reichardt, L.F.
(2006) Philos. Trans. R. Soc. Lond. B Biol. Sci. 361, 1545.
Bouzas-Rodriguez, J.
et al. (2010) J. Clin. Invest.120, 850.
Palazzo, E.
et al. (2012) J. Cell. Physiol.227, 1017.
