| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | Alpha-conotoxin GeXIVA, Conotoxin Ge14.1, Conotoxin GeXIVAWT, Alpha-O-conotoxin GeXIVA |
| 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 GeXIVA is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to α9α10 nAChRs 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: 2010167-25-4, MW: 3453 Da, Formula: C139H227N55O41S4.
- Source / origin: Conus generalis (General cone).
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
The native disulfide bond pairing has not been studied.
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 GeXIVA (αO-conotoxin GeXIVA or GeXIVA) is a 28 amino acid peptidyl toxin, which was discovered from a transcriptome analysis of the South China Sea mollusk, Conus generalis1. GeXIVA belongs to the O1-gene superfamily and is a potent and selective antagonist of the α9α10 nicotinic acetylcholine receptor (nAChR) subtype1. The toxin-mediated blockade of α9α10 nAChRs is voltage-dependent, suggesting that the toxin binding site might be allosterically coupled to a voltage-sensitive domain of the nAChR1,2. GeXIVA exhibits analgesic activity in animal models of pain without the development of tolerance1-4.nAChRs are involved in a wide range of physiological functions in the central and peripheral nervous systems. Alterations in nAChR expression and/or function are associated with a number of pathophysiological conditions including pain, addiction, epilepsy, autism, schizophrenia, Alzheimer's and Parkinson's diseases, as well as many types of cancers2,6. The nAChRs are formed from the assembly of five homologous subunits and neuronal nAChRs are assembled from a combination of α- and β-subunits. They share a common basic structure, but their pharmacological and functional properties arise from the wide range of different subunit combinations which generate distinctive subtypes6. The α9α10 nAChR subtype is a potential target for treating chronic pain, wound healing, the pathophysiology of the auditory system, and various cancers4-7. GeXIVA potently alleviated neuropathic pain in several rat models1-4 and also exhibited an antitumor effect5,8.
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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Chen, J.
et al. (2021) Acta Pharm. Sin. B., 11, 2685.
Luo, S.
et al. (2015) PNAS, 112, E4026.
Zhangsun, D.
et al. (2017) Neuropharmacol., 127, 243.
Wang, H.
et al. (2019), Mar. Drugs,17, 265.
Li, X.
et al. (2016) Prog. Neuro-Psychopharmacol. Biol. Psych., 66, 112.
Sun, Z.
et al. (2020) Mar. Drugs, 18, 195.
Gotti, C.
et al. (2009) Biochem. Pharmacol., 78, 703.
Vincler, M.
et al. (2006) PNAS,103, 17880.
Liu, Y.
et al. (2019) Mar. Drugs, 17, 256.
Luo, S.
et al. (2015) PNAS, 112, E4026.
Li, X.
et al. (2016) Prog. Neuro-Psychopharmacol. Biol. Psych., 66, 112.
Zhangsun, D.
et al. (2017) Neuropharmacol., 127, 243.
