3R-Pompilidotoxin

SKU:BHP21300090 Toxins and Venom Peptides
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    Overview
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    3R-Pompilidotoxin is a reagent targeting NaV. Key specifications include Source: Anoplius samariensis (Solitary wasp); Form: Lyophilized; Purity: ≥98% (HPLC); MW: 1558 Da. Commonly used in neuroscience studies, including measure nav modulation in patch-clamp electrophysiology (dose–response) and profile nav pharmacology in cell-based assays (concentration–response + time-course).
    Target NaV Na+ channels
    Species Anoplius samariensis (Solitary wasp)
    Purity ≥98% (HPLC)
    Molecular Weight 1558 Da
    Form Lyophilized
    Available Options

    Select the variant that best fits your experiment. Availability and lead time may vary by option.

    • Options:
      Size (3) - 1 mg, 10 mg, 5 mg
      Quantity: 1
    • Lead time: typically ships in ~1-2 business days; timing may vary by selected option.
    • Storage: Storage before reconstitution: The product is shipped as a lyophilized powder at room temperature. Upon receipt, store the product at -20°C. Protect from moisture. Storage after reconstitution: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles. Storage of solutions: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles.
    • Shipping: cold-chain shipment (typically with ice packs).
    • Upon receipt: store at the recommended temperature as soon as possible.
    • Sales terms and conditions: Please review prior to ordering.
    Field Specification
    Activity
    • 3Rα-Pompilidotoxin slows NaV channel inactivation without changing the peak current-voltage relationship or the activation time course of the TTX-sensitive Na+ currents in the neuromuscular synapse1-3.
    Alternative Names 3Rα-PMTX
    Concentration 100 - 200 µM
    Form Lyophilized
    Formulation Lyophilized from double distilled water (ddH2O). May contain TFA as a residual counter ion.
    Gene ID SCN1A,SCN2A,SCN3A,SCN8A,SCN9A
    Molecular Weight 1558 Da
    Product Type
    • Proteins & Peptides
    • Proteins
    • Toxins
    Purity ≥98% (HPLC)
    Reconstitution Centrifuge the vial (10,000 × g for 5 minutes) before adding solvent 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. Gently tap, tilt, and roll the vial to aid dissolution. 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.
    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 Anoplius samariensis (Solitary wasp)
    Storage Storage before reconstitution: The product is shipped as a lyophilized powder at room temperature. Upon receipt, store the product at -20°C. Protect from moisture. Storage after reconstitution: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles. Storage of solutions: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles.
    Target NaV Na+ channels

    Overview

    3R-Pompilidotoxin is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to NaV Na+ 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: MW: 1558 Da, Formula: C71H124N22O17.
    • Source / origin: Anoplius samariensis (Solitary wasp).
    • Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.

    Modifications

    Leu13 - 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

    3Rα-Pompilidotoxin is a mutated form of α-Pompilidotoxin (#P-170), originally isolated from the solitary wasp (Anoplius samariensis) venom and is a synthetic version of the peptide1.Pompilidotoxins (PMTX, α and β) are small peptides consisting of 13 amino acids.α-PMTX induces a unique pattern of repetitive action potentials previously seen with other neurotoxins and thus facilitate both excitatory and inhibitory synaptic transmission.Recently it was found that this toxin slows the Na+-channel inactivation, without changing the peak current-voltage relationship or the activation time course of the TTX-sensitive Na+ currents in the neuromuscular synapse of the lobster walking leg and in the rat trigeminal ganglion neurons2-4. Effective at concentrations of 10 nM in cultured rat cortical neurons5.3Rα-PMTX is mutated at position 3 with Lysine to Arginine transition, which enhances its activity on voltage-gated Na+ channels 5-fold relative to α-PMTX1,3.

    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.

    Konno, K.

    et al. (2000) Neurosci. Lett.285, 29.

    Schiavon, E.

    et al. (2010) FEBS J.277, 918.

    Sahara, Y.

    et al. (2000) Eur. J. Neurosci.12, 1961.

    Konno, K.

    et al. (2000) Neurosci. Lett.285, 29.

    Konno, K.

    et al. (1998) Biochem Biophys. Res. Commun.250, 612.

    Harsch, A.

    et al. (1998) Neurosci. Lett.252, 49.

    Schiavon, E.

    et al. (2010) FEBS J.277, 918.

    Sahara, Y.

    et al. (2000) Eur. J. Neurosci.12, 1961.

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