| Field | Specification |
|---|---|
| Mfr No | |
| Activity | |
| Alternative Names | Nerve Growth Factor 2.5S, TrkA 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 natural protein |
| Species | |
| Storage | |
| Target |
Overview
mouse NGF 2.5S-Biotin is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to p75NTR, TrkA 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 Neurite outgrowth assay, Cell survival assay, Live cell imaging, Immunofluorescence, Fluorescence staining.
Key elements and design rationale
- Molecular identity: MW: ~26 kDa.
- Source / origin: Native protein isolated from mouse submaxillary glands..
- 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
The neurotrophins ("neuro" means nerve and "trophe" means nutrient) are a family of soluble, basic protein growth factors which regulate neuronal development, maintenance, survival and death in the CNS and PNS1.NGF, the first member of the family to be discovered, was originally purified as a factor supporting and regulating survival, development, function and plasticity of sympathetic and sensory spinal neurons in central and peripheral nervous systems in vivo as well as in vitro2-4. It is synthesized and secreted by sympathetic and sensory target organs and provides trophic support to neurons as they reach their final target5.Neurotrophin secretion increases in the nervous system following injury. Schwann cells, fibroblasts, and activated mast cells normally synthesize NGF constitutively, however, direct trauma and induction of cytokines combine to increase neurotrophin production in these cells after injury6.NGF is purified in three forms: the 7S, 2.5S and β, in which the biologically active subunit is the β subunit. The structural hallmark of all the neurotrophins is the characteristic arrangement of the disulfide bridges known as the cysteine knot, which has been found in other growth factors such as Platelet-derived growth factor7.Additionally, the involvement of NGF was recently discovered in processes such as asthma8, psoriasis9 and wound healing10. The biological effects of NGF are mediated by two receptors: TrkA, which is specific for NGF, and p75NTR, which binds all the neurotrophins11.For the past three decades, biotinylated derivatives of NGF have been widely used in the literature as useful probes for the study of the binding and the initial intracellular processing of this growth factor by cells bearing TrkA NGF receptor12. First studies using 125I-NGF have visualized the intracellular location of NGF12. A biotinylated derivative of NGF that retains biological activity, in conjunction with the appropriate avidin conjugates and fluorescent or confocal microscopic techniques, improve the sensitivity and resolution in many applications. Some examples of applications are: targeting of liposomes containing biotinylated NGF to cells bearing TrkA NGF receptors13; elucidating the kinetics and route of ligand-induced internalization of the p75 receptor through signaling endosomes in cycling and differentiated PC12 cells using biotinylated derivative of NGF14; electrically controlled NGF-Biotin delivery from biotin-doped conductive polymer15; studying the retrograde axonal transport mechanism of NGF signals from the axon terminal to the cell body16,17.
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
- Neurite outgrowth assay: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
- Cell survival assay: 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.
- Fluorescence staining: 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.
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