| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | Alpha-conotoxin AuIB, GABA(B) receptor agonist |
| Cas No. | |
| 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 AuIB is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to α3/β4 nAChR, GABA(B) receptor agonist 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: CAS: 216299-21-7, MW: 1572.8 Da, Formula: C65H89N17O21S4.
- Source / origin: Conus aulicus (Princely cone).
- Quality attributes: Purity: ≥99% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys2-Cys8 and Cys3-Cys15 Cys15 - 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
α-Conotoxin AuIB is a 15 amino acid peptidyl toxin isolated from Conus aulicus1. This toxin inhibits mammalian neuronal α3/β4 nicotinic acetylcholine receptor (nAChR) channels expressed in Xenopus oocytes with an IC50 of 0.75 µM Furthermore, α-Conotoxin AuIB blocks the α3/β4 receptor with >100-fold higher potency than other receptor subunit combinations1.In accordance, α-Conotoxin AuIB (1-5 µM) blocks 20-35% of the nicotine-stimulated norepinephrine release from rat hippocampal synaptosomes1 and the nicotinic ACh receptors on dissociated neurons of the rat parasympathetic ganglia with IC50 of 1.2 nM2.α-Conotoxin AuIB also mediates inhibition of N-type calcium channels at nanomolar concentrations (IC50 = 1.5 nM in rat DRG neurons) via agonism of γ-aminobutyric acid (GABA) G protein-coupled (GABAB) receptors3. GABAB receptors are promising targets for the treatment of various neurological and psychiatric disorders, including pain, depression, and drug addiction. GABAB receptors are widely expressed and distributed in pain-processing pathways at all levels of the neuraxis and play an extensive role in editing and modulating nociceptive inputs. α-Conotoxin AuIB produced reversal of allodynia in the partial nerve ligation (PNL) model3,4.
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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Olivera, B.M.
et al. (1990) Science249, 257.
Luo, S.
et al. (1998) J. Neurosci.18, 8571.
Dutton, J.L.
et al. (2002) J. of Biol. Chem.277, 48849.
Klimis, H.
et al. (2011) Pain152, 259.
Kennedy, A.C.
et al. (2020) Toxins12, 505.
Luo, S.
et al. (1998) J. Neurosci.18, 8571.
