| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | Potassium channel toxin α-KTx 7.1, Pandinotoxin-α, Potassium channel-blocking toxin 2, Pi-2, Pi2, Toxin PiTX-K-α, PiTX-Kα, Shaker-related K+ channels |
| 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
Pandinotoxin Kα is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to A-type and Shaker-related K+ channels 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: 185529-64-0, MW: 4033.8 Da, Formula: C169H267N53O48S7.
- Source / origin: Pandinus imperator (Emperor scorpion).
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys4-Cys25, Cys10-Cys30, Cys14-Cys32
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
Scorpion venoms are a rich source of ion channel modulators. The scorpion toxins have been useful molecules in probing the K+ channel structures and functions1.Pandinotoxin Kα (PiTx-Kα) is a 35 amino acid peptidyl toxin isolated from the Pandinus imperator (Emperor scorpion) venoM It is a highly potent and selective blocker of voltage-activated K+ channels. PiTx-Kα preferentially blocks rapidly inactivating (A-type) K+ channels2. In general, channel inhibitors can be pore blockers or gating modifiers. Pore blockers bind to the channel in 1:1 stoichiometry and plug the pore of the channel impeding the flow of the ionic current. These toxins are small proteins that block the passage of K+ ions by binding at the pore entryway on the extracellular side of the channel, thereby inhibiting the ion flux3. The interactions of toxins with K+ channels are among the strongest and most specific known in protein-protein complexes4.
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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