| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| 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 human NGF proDomain protein is a research-grade protein/peptide reagent used in research settings. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows.
Key elements and design rationale
- Molecular identity: MW: 11.6 kDa.
- Source / origin: Recombinant, E. coli.
- Quality attributes: Purity: ≥98% (HPLC); 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
NGF is a key factor in the survival and differentiation of neurons in the peripheral and central nervous systems. Like many other neurotrophins, mature NGF arises from the proteolytic cleavage of its precursor form (proNGF) by various proteases. It has been found that proNGF, and not mature NGF, is the predominant isoform found in the human brain as well as in a variety of cell types, including mast cells, sciatic nerve cells, thyroid gland, skeletal muscle, prostate gland, hippocampus and hair follicle.4 The mouse salivary gland is the most abundant source of mature NGF. NGF can be secreted as proNGF or mature NGF, each with distinct binding preferences for p75NTR, Trk-family receptors and sortilin.1-3In many cases, the full prodomain region derived from the precursor has biological functions, for instance; the prodomain of the transforming growth factor β (TGFβ) affects the dimerization and folding as well as the activity of the mature proteins via non-covalent association. The propeptide of the bone morphogenetic proteins BMP-4 and BMP-7 regulates the diffusion and distribution of these growth factors within the extracellular matrix.4,5 However, the role of the full NGF-prodomain, which is a proteolytic cleavage product of the proNGF, is not clearly understood. This region has been reported to give rise to several bioactive peptides that promote cell survival, probably through activation of Trk receptor pathway.6 Furthermore, binding competition studies suggest that binding sites for NGF prodomain and BDNF prodomain are located in the tunnel of the ten-bladed β-propeller domain of sortilin.7,8
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
- Assay development and optimization: used as a reference material or tool reagent in RUO workflows.
- Reagent validation: supports conceptual controls such as competition/neutralization, when relevant.
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.
- 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.
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