| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | ω-Theraphotoxin-Hg1a, ω-TRTX-Hg1a, SNX 482, CaV2.1, KV4.2, KV4.3 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 | Recombinant, E. coli |
| Species | |
| Storage | |
| Target |
Overview
SNX-482 is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to CaV2.3, CaV2.1, KV4.2, KV4.3 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, Electrophysiology.
Key elements and design rationale
- Molecular identity: CAS: 203460-30-4, MW: 4495 Da, Formula: C192H274N52O60S7.
- Source / origin: Hysterocrates gigas (Cameroon red baboon tarantula).
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
Modifications
Disulfide bonds between: Cys7-Cys21, Cys14-Cys26, and Cys20-Cys33
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
SNX-482 is a peptidyl toxin originally isolated from venom of the spider Hysterocrates gigas. Native SNX-482 blocks specifically CaV2.3 (α1E, R-type) channels1 in a voltage-dependent manner. The block is reversible only upon application of strong voltage to facilitate unbinding.2 SNX-482 inhibits human CaV2.3 channels stably expressed in a mammalian cell line. An IC50 of 15-30 nM was obtained for block of CaV2.3 channel, using either patch clamp electrophysiology or K+-evoked Ca2+ flux. At low nanomolar concentrations, SNX-482 also blocked a native R-type Ca2+ current in rat neurohypophyseal nerve terminals, but concentrations of 200-500 nM had no effect on R-type Ca2+ currents in several types of rat central neurons.1 SNX-482 was also used to demonstrate the contribution of CaV2.3 channels to transmitter release.3 Recently it was shown that higher concentrations of SNX-482 also block CaV2.1 channels in chromaffin cells.4SNX-482 was found to be the most potent blocker to date for KV4.3 channel with IC50 < 3 nM5.
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.
- 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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Kimm, T. and Bean, B.P.
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Kimm, T. and Bean, B.P.
(2014) J. Neurosci.34, 9182.
