| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | K+ channel toxin α-KTx 6.2, MTX, KV1 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
Maurotoxin is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to KCa and KV1 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: 188240-41-7, MW: 3612 Da, Formula: C145H232N46O46S8.
- Source / origin: Scorpio palmatus (Israeli golden scorpion) (Scorpio maurus palmatus).
- Quality attributes: Purity: >99% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys3-Cys24, Cys9-Cys29, Cys13-Cys19 and Cys31-Cys34 Cys34 - 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
Maurotoxin (MTX) is a 34 amino acid long toxin, isolated from the venom of the scorpion Scorpio Maurus palmatus, and is classified as α-KTx6.2 scorpion toxin family, having four disulfide bridges1,2.MTX activity was extensively assayed on a large array of K+ channels, including KCa (KCa1.1, KCa2.1, KCa2.2, KCa3.1), KV1 (KV1.1, KV1.2 and KV1.3) and Shaker-B K+ currents. MTX inhibits the binding of 125I-Apamin and 125I-Kaliotoxin to rat brain synaptosomal membranes with an IC50 of 5 nM and 30 pM, respectively3. Furthermore, MTX blocks KCNA1 (KV1.1), KCNA2 (KV1.2) and KCNA3 (KV1.3) expressed in Xenopus oocyes with an IC50 of 45 nM, 0.8 nM, and 180 nM, respectively3. Maurotoxin blocks Shaker-B K+ current with an IC50 of 2 nM4. In contrast to previous reports, MTX was recently shown to have no effect on KCa1.1, KCa2.1 and KCa2.2 small conductance KCa channels up to 300 nM in physiologically relevant ionic strength buffers, but rather produces a high and specific block towards KCa3.1 (IKca1, SK4) and KCNA2 (KV1.2) with IC50 of 1 nM and 0.1 nM, respectively5. Furthermore, MTX was shown to block Gardos channel in human red blood cells and to inhibit the KCa in activated human T-lymphocytes without affecting the voltage-gated K+ current encoded by KCNA35. Moreover, MTX inhibition was shown to be pH-dependent6,7.In conclusion, Maurotoxin seems to be a very potent blocker of both KCa3.1 and KV1.2 channels.
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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