$603.00 - $603.00
Conotoxin GS is a 34-amino-acid, disulfide-rich peptide originally isolated from Conus geographus. It acts at the extracellular region of voltage-gated sodium channels and has been characterized as an inhibitor of skeletal-muscle sodium-channel function.
Unlike the short α-conotoxins that inhibit nicotinic acetylcholine receptors, Conotoxin GS is used primarily as a probe of NaV channel pore pharmacology and sodium-channel subtype discrimination.
Product Information
| Property | Specification |
|---|---|
| Product Name | μ-Conotoxin GS / Conotoxin GS |
| Catalog No. | AS2581 |
| CAS No. | 115757-31-8 |
| Length | 34 amino acids |
| Natural Source | Conus geographus |
| Disulfide Bonds | 3 |
| Key Modifications | Hydroxyproline residues; γ-carboxyglutamate |
| Primary Target | Voltage-gated sodium channels |
| Major Research Area | Skeletal muscle NaV channel pharmacology |
| Form | Lyophilized peptide |
The mature sequence contains six cysteines, three disulfide bonds, two hydroxyproline residues, and a γ-carboxyglutamate residue.
Sodium Channel Blocking Activity
Conotoxin GS interacts with the extracellular entrance of skeletal-muscle sodium channels and prevents sodium ion conduction.
Classical binding experiments showed competition with tetrodotoxin and μ-Conotoxin GIIIA at sodium-channel receptor site 1. The peptide showed stronger interaction with skeletal-muscle preparations than with rat brain sodium-channel preparations, supporting its use as a probe for distinguishing muscle and neuronal NaV pharmacology.
Structural Difference from Classical μ-Conotoxins
Although GS overlaps pharmacologically with μ-Conotoxin GIIIA, its sequence and structural organization are substantially different.
NMR studies identified a compact structure containing a cystine-knot motif and a four-loop architecture. This makes the molecule particularly interesting for studies that relate three-dimensional toxin geometry to the extracellular pore region of voltage-gated sodium channels.
Sequence Features and Synthetic Considerations
The sequence contains several features that make synthesis and characterization more demanding than a standard linear peptide, including multiple cysteines, three disulfide bonds, hydroxyproline, and γ-carboxyglutamate.
For custom analogs or related sodium-channel probes, We recommend defining post-translational modifications and disulfide requirements before synthesis. These projects can be evaluated through Custom Peptide Synthesis.
Quality Control
For a multiply modified, folded peptide, final characterization should consider molecular identity, chromatographic purity, oxidation state, and the intended modified residues together.
Additional information on analytical HPLC and MS is available through Peptide Quality Control.
Conotoxin GS and other naturally derived ion-channel probes are included in our Bioactive Toxin-Derived Peptides collection.
Storage and Handling
Store according to the batch-specific product documentation. Reconstituted solutions should be handled according to solvent, concentration, temperature, and experimental requirements, with unnecessary freeze–thaw cycles minimized.
Research Use Only
μ-Conotoxin GS is supplied for research use only. It is not intended for therapeutic, or human use.