| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | Alpha-A-conotoxin PIVA, Alpha-conotoxin PIVA |
| 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
αA-Conotoxin PIVA is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to α1/β1/γ/δ nAChR 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: 2649 Da, Formula: C103H150N34O37S6.
- Source / origin: Conus purpurascens (Purple cone).
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys2-Cys16, Cys3-Cys11 and Cys14-Cys23 X = Hydroxyproline Gln25 - 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
αA-Conotoxin PIVA is the first member of a new family of nAChR-targeted Conus peptides, named short αA-conotoxins1. It is a peptide toxin originally isolated from Conus Purpurascens (Purple cone) venom1.This peptide reversibly blocks postsynaptic muscle fetal α1/β1/γ/δ nicotinic ACh receptor1,2 . It also blocks postsynaptic muscle adult α1/β1/ε/δ nicotinic ACh receptor, with lower affinity (IC50 of 22 nM to the adult compared to 2.3 nM to the fetal nAChR)2.αA-conotoxin PIVA has a strikingly different amino acid sequence and a Cys framework from all other nAChR-targeted peptides previously characterized from Conus venoms. Despite the striking structural divergence, the peptide blocks the ACh binding site of the nAChR at the neuromuscular junction, similar to the well known typical of a-conotoxins1.The characterization of the short αA-conotoxins revealed diverse kinetics of a block of the fetal muscle nAChR, particularly in dissociation rates. The structure-function relationships of native αA-conotoxins revealed a single amino acid locus (alternatively either His or Pro) that is a critical determinant of the dissociation kinetics2.
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.
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
Luo, S.
et al. (2010) The J. Biol. Chem. 285, 12355.
Hopkins, C.
et al. (1995) J. Biol. Chem. 270, 22361.
Teichert, R.W.
et al. (2006) Biochemistry 45, 1304.
Hopkins, C.
et al. (1995) J. Biol. Chem. 270, 22361.
