| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | proBrain-Derived Neurotrophic Factor, Sortilin receptors |
| 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, E. coli |
| Storage | |
| Target |
Overview
Recombinant mouse proBDNF (cleavage resistant) protein is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to p75NTR, Sortilin receptors 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, Neurite outgrowth assay.
Key elements and design rationale
- Molecular identity: MW: 52 kDa (dimer).
- Source / origin: Recombinant, E. coli.
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: Yes.
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
BDNF is a neurotrophic factor produced by proteolytic cleavage of its precursor, proBDNF. The biologically relevant form of the protein was thought to be the mature form, BDNF, which has been shown to affect the development of motoneurons, modulate synaptic transmission and affect axonal branching, dendrite growth and synapse number.1 These actions are mediated via the binding of BDNF to TrkB. Different actions are mediated by the binding of BDNF to p75, such as neuronal process retraction2 and neuronal apoptosis.3 The precursor form of the neurotrophic factor was thought to be important for the correct folding, secretion and trafficking of the mature protein. A single-nucleotide polymorphism (Val66 to Met) in the pro-domain of the human BDNF gene impairs intracellular trafficking and regulated secretion of BDNF in primary cortical neurons and neurosecretory cells but not in endothelial and vascular cells.4 This has been shown to affect memory and lead to abnormal hippocampal function in humans.5The finding that proBDNF and not mature BDNF is the preferred ligand for p756 has ushered in a new era which reexamines the biological roles of the two forms. Contradictory biological roles for proBDNF have been proposed. It has been shown to be a pro-apoptotic ligand for sympathetic neurons7 expressing both p75 and sortlin, and to be involved in LTD8. On the other hand, it has also been shown to elicit prototypical TrkB responses in biological assays, such as TrkB tyrosine phosphorylation, and activation of ERK1/2.9 Binding of both proBDNF and mature BDNF to TrkB has been proposed to be via the R103 residue in the mature portion.9In addition, the question of the relative abundance of the precursor versus the mature form has been investigated. In brain homogenates a mixture of proBDNF and mature BDNF has been found.10,11 The secretion of proBDNF from cortical neurons has been shown.7 Most of the work showing secretion of proBDNF was done in cell lines overexpressing full length BDNF constructs.4, 6,12,13 It has been argued14 that this model misrepresents the authentic situation in vivo, since in the transfected systems the secretion of proBDNF results from overloading the limited capacity of the processing machinery. These authors argue that in fact proBDNF is a transient intermediate and is rapidly converted intracellularly to mature BDNF.
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.
- Neurite outgrowth assay: 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.
Woo, N.H.
et al. (2005) Nat. Neurosci. 8, 1069.
Bibel, M and Barde, Y.A.
(2000) Genes Dev. 14, 2929.
Cahoon-Metzger, S.M.
et al. (2001) Dev. Biol. 232, 246.
Troy, C.M.
et al. (2002) J. Biol. Chem. 277, 34295.
Chen, Z.Y.
et al. (2004) J. Neurosci. 24, 4401.
Egan, M.F.
et al. (2003) Cell112, 257.
Lee, R.
et al. (2001) Science294, 1945.
Teng, H.K.
et al. (2005) J. Neurosci. 25, 5455.
Woo, N.H.
et al. (2005) Nat. Neurosci. 8, 1069.
Fayard, B.
et al. (2005) J. Neurosci. Res.80, 18.
Michalski, B.
et al. (2003) Mol. Brain Res. 111, 148.
Zhou, X.F.
et al. (2004) J. Neurochem. 91, 704.
Mowla, S.J.
et al. (1999) J. Neurosci. 19, 2069.
Mowla, S.J.
et al. (2001) J. Biol. Chem. 276, 12660.
Matsumoto, T.
et al. (2008) Nat. Neurosci. 11, 131.
Tolkovsky, A.
(1997) Trends Neurosci. 20, 1.
Jing, S.
et al. (1992) Neuron 9, 1067.
Acheson, A.
et al. (1995) Nature 374, 450.
Morse, J.K.
et al. (1993) J. Neurosci. 13, 4146.
Hyman, C.
et al. (1991) Nature 350, 230.
Friedman, B.
et al. (1995) J. Neurosci. 15, 1044.
Meyer, M.
et al. (1992) J. Cell Biol. 119, 45.
Koliatsos, V.E.
et al. (1993) Neuron 10, 359.
Teng, H.K.
et al. (2005) J. Neurosci. 25, 5455.
