| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | Mu-conotoxin SxIIIC, SxIIIC peptide, Nav1.3, Nav1.1, Nav1.6, Nav1.7 blocker |
| 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
µ-Conotoxin SxIIIC is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to Nav1.4, Nav1.3, Nav1.1, Nav1.6 and Nav1.7 blocker 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: 2437 Da, Formula: C90H142N42O27S6.
- Source / origin: Conus striolatus (Cone snail).
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys3-Cys15, Cys4-Cys21 and Cys10-Cys22 Cys22 - C-terminal amidation
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
µ-conotoxin SxIIIC (SxIIIC) is a 22 amino acid peptidyl toxin originally isolated from the venom of the cone snail, Conus striolatus1. SxIIIC is a potent and irreversible blocker of voltage-gated sodium (Nav) channels, which displays a unique µ-conotoxin selectivity profile of human (h)NaV1.4 > hNaV1.3 > hNaV1.1≈ hNaV1.6≈ hNaV1.7 > hNaV1.2 >> hNaV1.5≈ hNaV1.81.Voltage-gated sodium channels (VGSCs) are transmembrane proteins that control the voltage-dependent increase in sodium permeability. VGSCs play a fundamental role in normal neurological function, especially in the initiation and propagation of action potentials. Nav channels have been the topic of significant research and discussion for a considerable amount of time given their unique functions in electrical cell signaling. These channels are very important for homeostasis, thus specific genetic abnormalities in VGSC genes can result in a range of muscle, cardiac, and neurological disorders known as "channelopathies"2. Marine toxins appear to be an emerging source of therapeutic tools that can relieve pain or treat VGSC-related human channelopathies3.
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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Luo, S.
et al. (2013) J Med Chem., 56, 9655.
McMahon, K.L.
et al. (2020) Biomedicines, 8, 321.
Huang, W.
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Mackieh, R
. et al. (2021) Mar. Drugs, 19, 562.
