| Field | Specification |
|---|---|
| Accession Number | |
| Activity | |
| Alternative Names | RgIA, Alpha-conotoxin RgIA, α7, N-Type Ca2+ Channels |
| 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. The product is soluble in pure water at high micromolar concentrations (100 µM - 1 mM). For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in double-distilled water (ddH2O) 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 | Synthetic peptide |
| Species | |
| Storage | |
| Target |
Overview
α-Conotoxin RgIA is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to α9α10 nAChRs, α7, and N-Type Ca2+ Channels 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 Electrophysiology.
Key elements and design rationale
- Molecular identity: MW: 1571 Da, Formula: C59H95N25O18S4.
- Source / origin: Conus regius (Crown cone).
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys2-Cys8, Cys3-Cys12
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
α-conotoxin RgIA (RgIA) is a 13 amino acid peptidyl toxin cloned from a genomic DNA library of the marine worm-hunting sea snail, Conus regius1. RgIA belongs to the α4/3 subfamily of conotoxins (i.e., a family of peptides with four amino acids in the first loop and three in the second loop) and is a potent and selective antagonist of the α9α10 nicotinic acetylcholine receptor (nAChR) subtype, which also shows a weak activity towards α7 nAChR1,2. RgIA was also shown to inhibit high-voltage-activated (HVA) calcium channel currents in rat dorsal root ganglion (DRG) neurons3.The nAChRs are acetylcholine-gated ion channels. Given the important physiological roles of nAChRs in pain, inflammation, nicotine addiction, Alzheimer's disease, and Parkinson's disease, specific targeting of the relevant nAChR subtypes is an attractive pharmaceutical strategy. α-conotoxins are among the most promising drug development leads for treating these diseases4,5. RgIA was shown to be an effective analgesic agent in a rat model of nerve injury and also reduced the immune response contributing to peripheral nerve damage6,7. Furthermore, RgIA was shown to prevent neuropathic pain induced by oxaliplatin treatment8.
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
- Electrophysiology: 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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