α-Pompilidotoxin , CAS No.202075-91-0

CAS: 202075-91-0 Cat. No.: P1440771 Formula: C₇₁H₁₂₄N₂₀O₁₇ Molecular Weight: 1529.87

Storage

Store at -20°C

Shipped In

Ice chest + Ice pads

Overview

α-Pompilidotoxin (α-PMTX) is a neurotoxin that can be obtained from the venom of Anoplius safnariensis. α-Pompilidotoxin reversibly and dose-dependently enhances excitatory postsynaptic currents (EPSCs). α-Pompilidotoxin is a useful tool in the field of neuroscience research.

Specifications

Storage

Store at -20°C

Shipped In

Ice chest + Ice pads

This product requires cold chain shipping. Ground and other economy services are not available.

Names and Identifiers

Molecular Weight

1529.87

Application Protocols

Item-specific validated applications and dilutions: Not specified for this item; refer to CoA/Spec Sheet.

General/literature protocols for α-PMTX in electrophysiology and ion-channel assays

• Stock preparation: Reconstitute the lyophilized material in sterile water or buffer to a convenient high-concentration stock. If solubility is limited, dissolve first in a minimal volume of DMSO, then dilute into buffer. Prepare single-use aliquots and freeze at −20°C or below.
• Working concentrations: Literature use spans low-nanomolar to micromolar ranges depending on preparation, Nav isoform, and temperature. Begin with a broad titration (e.g., 0.01–10 μM) to identify the active window, then refine.
• Application method: For whole-cell or slice recordings, bath perfusion is typical; allow adequate equilibration (several minutes) and monitor for reversible effects on inactivation kinetics. For single-channel studies, consider inside-out/outside-out patches with controlled solution exchange.
• Controls: Include vehicle-only controls, TTX or selective Nav blockers as mechanistic comparators, and washout to assess reversibility. Record series resistance and seal quality to distinguish pharmacology from recording artifacts.
• Adsorption management: Use low-bind tubes and consider 0.1% BSA if compatible. Avoid lengthy pre-incubations in plastic reservoirs at very low concentrations.
• Data reporting: Document temperature, ionic composition, holding potentials, pulse protocols, and exact peptide concentration and lot to ensure reproducibility.

Biological Roles

General/literature overview (no medical/clinical claims)

• Origin and class: α-Pompilidotoxin (α-PMTX) is a venom-derived peptide from pompilid (spider wasp) species. It belongs to a family of small peptides that modulate voltage-gated sodium channels (Nav) in excitable tissues.
• Mechanism of action: Characteristically slows or suppresses fast inactivation of Nav channels, prolonging sodium currents during depolarization. This increases neuronal excitability and can enhance synaptic transmission in controlled experimental settings.
• Research utility: Widely used as a pharmacological probe to dissect sodium channel gating kinetics, to separate activation from inactivation processes, and to evaluate contributions of Nav subtypes in neurons. In network-level studies, it serves as a tool to bias circuits toward heightened excitability for mechanistic evaluation of inhibitory control and plasticity, always within research frameworks.
• Selectivity considerations: Venom peptides often display preference for neuronal Nav isoforms over some peripheral/cardiac ones; exact isoform selectivity and potency depend on sequence and preparation and should be verified experimentally for each lot (consult literature and CoA).
• Complementarity: In comparative studies, α-PMTX is often evaluated alongside other inactivation modulators (e.g., sea anemone toxins, batrachotoxin analog probes) and pore blockers (e.g., TTX) to map state-dependent channel pharmacology.
• Assay systems: Employed in heterologous expression (e.g., Nav in HEK cells), isolated neurons, brain slices, and invertebrate preparations, with readouts including whole-cell and single-channel electrophysiology and calcium imaging.

Buffer Applications

Not typically applicable. α-Pompilidotoxin is not a buffering agent and is used at low concentrations in pre-existing physiological buffers.

Practical handling notes (general)

• Working media: Prepare and apply in established recording solutions such as artificial cerebrospinal fluid (ACSF), HEPES-buffered saline, or intracellular patch solutions as dictated by the experiment.
• Adsorption mitigation: For very low concentrations, consider 0.1% carrier protein (BSA) to limit surface losses if compatible with your assay.
• Compatibility: Confirm that magnesium, calcium, and ionic strength of your buffer match the electrophysiological protocol; additives (detergents, serum) can alter peptide availability and should be validated.

Green Alternatives

Not applicable in the customary sense. α-Pompilidotoxin is a peptide research tool, not a solvent or bulk reagent where greener substitutes are typically evaluated.

General sustainability notes for handling peptide toxins

• Use minimal DMSO and prefer aqueous buffers where feasible.
• Prepare small aliquots to reduce waste from expired solutions.
• Choose low-binding, recyclable plastics where possible and consolidate cold-shipments to reduce transport footprint.
• Dispose according to local regulations for hazardous chemical waste; avoid discharge to drains.

Pharmaceutical Uses

No therapeutic or clinical uses are claimed or supported for this product. For research use only.

General formulation/analytical context (non-clinical)

• Reference standard: May be employed as a pharmacological reference tool in nonclinical studies to benchmark Nav channel assays, potency shifts, or to validate screening platforms.
• Matrix considerations: For in vitro assay development, formulate in assay-compatible buffers to minimize nonspecific binding and ensure reproducible exposure. Avoid excipients that may quench activity or alter membrane properties unless intentionally tested.
• Documentation: If your quality system requires, maintain chain-of-custody records and retain CoA and SDS with each lot used in regulated nonclinical method development (where applicable).

Physical Properties

Item-specific (from Product Data)

• Appearance: Not specified for this item; refer to CoA/Spec Sheet.
• Grade/Purity: Not specified for this item; refer to CoA/Spec Sheet.

General/literature guidance for peptide toxins

• Physical state: Typically supplied as lyophilized powder or film, or as a frozen aqueous aliquot, depending on manufacturing; verify your unit’s CoA.
• Solubility (literature/general): Peptides of this size class are generally soluble in water, dilute aqueous buffers (e.g., PBS, HEPES), or in minimal DMSO followed by dilution into recording buffer. Solubility can be sequence-dependent; gentle sonication and brief vortexing may help.
• pH considerations (literature): Solubility is often improved near neutral to mildly acidic pH; avoid strong bases that can promote deamidation/epimerization.
• Stability (literature): Peptide toxins are susceptible to hydrolysis and oxidation; minimize exposure to elevated temperature, high pH, and repeated freeze–thaw. Light sensitivity is usually low but store protected as a best practice.
• Partitioning (literature): Predominantly hydrophilic, but amphipathic surfaces can allow membrane association; logP is not applicable in the classical small-molecule sense.
• Spectral properties (literature): If aromatic residues are present, peptides may exhibit UV absorption near 280 nm enabling quantification by A280; extinction coefficient is sequence-dependent and should be calculated from the exact sequence (not provided here).

Quality and Grades

Item-specific (from Product Data)

• Grade/Purity: Not specified for this item; refer to CoA/Spec Sheet.

How we characterize peptide toxins (general guidance)

• Identity confirmation: Typically established by exact mass (ESI/MALDI-MS) and, where applicable, peptide mapping. Retention time on analytical RP-HPLC is often provided as a qualitative identity check.
• Purity reporting: For research peptides/toxins, purity is commonly specified as % area by RP-HPLC at 214/220 nm and/or 280 nm. Trace residual solvents/salts are reported when relevant. If purity is critical for electrophysiology, request the chromatogram.
• Counterions/form: Peptides may be provided as TFA, acetate, or chloride salts, which can influence solubility and bioactivity readouts. The specific counterion for this lot is not specified; see CoA.
• Endotoxin/bioburden: Not typically specified for chemical research-grade peptides; if you require low-endotoxin material for sensitive biological assays, contact us.
• Stabilizers: None are listed in the Product Data. If stabilizers (e.g., mannitol, trehalose, BSA) are used, they will appear on the CoA.
• Batch documentation: For each lot, request the CoA for: sequence, net peptide content, exact mass, HPLC trace, residual solvents, water content (if determined), and recommended reconstitution solvent.

Reaction and Applications

This section is primarily intended for synthetic reagents; α-Pompilidotoxin is a bioactive peptide tool rather than a synthetic building block.

• Not typically used as a reagent in organic transformations, catalysis, or materials synthesis.
• For practical uses, see Biological Roles, Target Specificity, and Application Protocols for electrophysiology and ion-channel pharmacology workflows.
• If chemical modification (e.g., biotinylation, fluorescent labeling) is planned for assay development, standard peptide conjugation chemistries (NHS-ester, maleimide) may be applicable depending on the sequence; consult the CoA for available functional handles and expect activity changes upon derivatization (general/literature note).

Reaction Conditions

Not applicable. This product is not used as a reagent in chemical reactions.

Experimental usage context (general guidance for bioassays; literature)

• Vehicle: Water or buffer, optionally with a minimal DMSO pre-wet if needed for dissolution.
• Temperature: Prepare and maintain solutions at 2–8°C during setup; equilibrate to experimental temperature (e.g., room temperature or 32–37°C) immediately before application to biological preparations.
• Light/oxygen: Routine ambient handling is acceptable; minimize prolonged exposure to air and elevated temperature to limit oxidation/hydrolysis.
• Time: Activity in bath applications typically manifests rapidly upon perfusion; steady-state effects depend on flow rate and tissue access and should be determined empirically.

Safety and Handling

Item-specific (from Product Data)

• GHS classification, pictograms, H-statements, signal word: Not specified for this item; refer to SDS.
• Research use: For research use only.
• Storage conditions: Store at -20°C.
• Shipping: Ice chest + ice pads.

General safety guidance for peptide neurotoxins (literature/practice)

• Hazard overview: α-Pompilidotoxin is a neuroactive peptide that modulates voltage-gated sodium channels. Avoid inhalation, ingestion, injection, and skin or eye contact. Handle as a potent bioactive laboratory chemical.
• PPE: Lab coat, safety glasses, and disposable nitrile gloves. Use a certified chemical fume hood or biosafety cabinet when weighing or reconstituting powders/aliquots to avoid aerosolization.
• Handling practices: Work with dilute solutions where possible. Prepare small aliquots to avoid repeated freeze–thaw. Clearly label containers with “Neurotoxin—research use only.”
• Incompatibilities: Avoid strong oxidants and bases that may degrade peptides. Do not mix with proteases or biological matrices containing high protease activity unless protease inhibitors are present.
• First aid (summary; defer to SDS): In case of skin/eye contact, rinse with water for ≥15 min and remove contaminated clothing. If inhaled, move to fresh air; if ingested or exposed parenterally, seek medical attention immediately. Provide SDS to responders.
• Waste: Collect solids and solutions as hazardous chemical waste according to institutional and local regulations.

Solvent Selection

Item-specific (from Product Data)

• No specific solvent recommendations are provided for this item; refer to CoA/Spec Sheet.

General/literature guidance for α-PMTX and similar peptide toxins

• Primary solvents: Water or physiological buffers (e.g., HEPES, PBS, artificial cerebrospinal fluid) are typically suitable. If initial dissolution is difficult, wet the peptide with a minimal volume of DMSO (e.g., 1–5% of final volume) and then dilute into aqueous buffer with gentle mixing.
• pH effects: Slightly acidic to neutral pH (≈6.0–7.4) helps maintain integrity and solubility for many peptides. Avoid strong base (>pH 9) which accelerates backbone/side-chain degradation.
• Additives: 0.1% carrier protein (e.g., BSA) or 0.05–0.1% Tween-20 is sometimes used to reduce nonspecific adsorption to plastic/glass in low-nanomolar assays; confirm that additives will not interfere with electrophysiology.
• Container choice: Use low-bind polypropylene tubes for working stocks; for long incubations or very low concentrations, silanized glass can minimize adsorption.
• Filtration: If sterile solutions are needed, use low protein-binding 0.22 μm PVDF or PES filters; avoid prolonged filtration of highly dilute solutions to limit analyte loss.
• Comparators: Versus hydrophobic peptide toxins that require higher DMSO, α-PMTX-class peptides are often adequately soluble in aqueous buffers, simplifying downstream patch-clamp or slice electrophysiology work.

Storage and Reconstitution

Item-specific (from Product Data)

• Storage conditions: Store at -20°C.
• Shipping: Ice chest + ice pads.

General best practices for peptide toxins

• Upon receipt: Inspect packaging temperature and integrity. If lyophilized, allow the vial to equilibrate to room temperature in a desiccator before opening to prevent condensation.
• Reconstitution: Use sterile, buffered water (e.g., PBS, HEPES) or pure water. If needed, pre-wet with minimal DMSO prior to buffer dilution. Mix gently; brief sonication can assist dissolution.
• Aliquoting: Prepare single-use aliquots in low-bind tubes to avoid repeated freeze–thaw. Clearly label with concentration, buffer, date, and lot.
• Storage of solutions: Short-term (hours to 1–2 days) at 2–8°C; longer-term at −20°C or lower. Avoid frost-free freezers that cycle temperatures. Protect from prolonged exposure to air and elevated temperature.
• Stability: Exact shelf-life and stability of this lot are not specified; refer to CoA/Spec Sheet. As a precaution, discard working solutions after 24–48 h at 2–8°C and re-prepare as needed.
• Thawing: Thaw on ice, mix gently, and use promptly. Do not refreeze partially thawed aliquots.
• Documentation: Retain CoA and SDS with the stored material; track aliquot usage for reproducibility.

Structure and Identity

Item-specific (from Product Data)

• CAS: 202075-91-0
• SKU: P1440771
• Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
• SMILES: Not specified for this item; refer to CoA/Spec Sheet.
• InChIKey: Not specified for this item; refer to CoA/Spec Sheet.

General/literature description (peptide neurotoxin)

• α-Pompilidotoxin (α-PMTX) is a small venom-derived peptide toxin originally reported from pompilid (spider wasp) venom. It is classified among peptide modulators of voltage-gated sodium channels (Nav).
• Structural features (literature): peptides of this class typically comprise a short chain of L-amino acids without disulfide bonds, forming flexible, amphipathic conformations in aqueous media that enable interaction with membrane-embedded channel proteins.
• 2D description in words: A linear oligopeptide backbone composed of repeating amide linkages (–C(O)–NH–), with side chains projecting alternately, creating hydrophobic and polar patches that underlie channel-binding activity. No stereochemical centers beyond the canonical L-α-amino acid configurations are implied unless otherwise specified on the CoA.

Synthetic Utility

Not applicable in the traditional synthetic chemistry sense. α-Pompilidotoxin is a finished peptide tool compound used for ion-channel research, not as a synthon or catalyst.

General note (if derivatization is desired)

• Sequence-dependent modification (literature): If the peptide contains primary amines (N-terminus/Lys) or thiols (Cys), standard peptide conjugation chemistries (NHS-esters, isothiocyanates, maleimides) may be used to attach reporters. Such modifications can significantly alter target affinity and should be validated empirically.

Target Specificity

Item-specific data on isoform selectivity, potency (IC50/EC50), and binding site: Not specified for this item; refer to CoA/Spec Sheet.

General/literature description

• Primary target class: Voltage-gated sodium channels (Nav) in excitable cells (neurons, muscle), with functional modulation characterized by slowed/attenuated fast inactivation.
• Functional consequence: Prolonged inward Na+ current during depolarization, leading to enhanced action potential firing or broadened spikes in many neuronal preparations, under controlled research conditions.
• Isoform considerations: Many venom peptides show variable effects across Nav1.x isoforms in vertebrates and invertebrates; exact rank order of sensitivity for α-PMTX should be established experimentally for the specific preparation and conditions used.
• Off-targets: At sufficiently high concentrations, nonspecific membrane or channel effects can emerge; include vehicle controls and orthogonal blockers (e.g., TTX for Nav pore) to confirm mechanism.

Frequently Asked Questions

How should this product be stored?

Store at ?20 °C. Freezer storage is required to maintain the specified shelf life.

How is this product shipped?

This product ships in an insulated container with ice pads. Unpack on arrival and transfer it to the storage condition stated above.

What are the CAS number, molecular formula and molecular weight?

The CAS Number is 202075-91-0, the molecular formula is C71H124N20O17, and the molecular weight is 1529.87 g/mol.

What documentation is provided?

Available product documentation, including Certificates of Analysis (COA), Safety Data Sheets (SDS), and specification sheets, is shown in the product document area. Document availability and access follow the current site policy.