{"product_id":"ectatotoxin-rm4a-bhp21300275","title":"Ectatotoxin-Rm4a","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eEctatotoxin-Rm4a\u003c\/strong\u003e is a research-grade protein\/peptide reagent used in research settings. It is commonly applied as a tool reagent related to \u003cstrong\u003eNav1.6, Nav1.7 channels\u003c\/strong\u003e 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.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eMolecular identity:\u003c\/strong\u003e MW: 2994.6 Da, Formula: C148H225N33O33.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Rhytidoponera metallica (Australian green-headed ant) (Ponera metallica).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eQuality attributes:\u003c\/strong\u003e Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile \/ endotoxin-free: No.\u003c\/li\u003e \u003c\/ul\u003e \u003ch3\u003eModifications\u003c\/h3\u003e \u003cp\u003eAsn25 – C-terminal amidation\u003c\/p\u003e \u003cp\u003eWhen 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.\u003c\/p\u003e \u003ch2\u003eBiological background\u003c\/h2\u003e \u003cp\u003eEctatotoxin-Rm4a (Rm4a), originally isolated from the venom of Rhytidoponera metallica (Australian green-headed ant), is a 26-amino acid cysteine-free peptide toxin that modulates voltage-gated sodium (NaV) channels, particularly NaV1.6 and NaV1.7 subtypes. Rm4a toxin induces sustained sodium currents by delaying inactivation and causing a hyperpolarizing shift in activation voltage. It exhibits higher potency for human Nav1.6 channels (EC50 = 196 ± 23 nM) compared to Nav1.7 (EC50 = 1.9 ± 0.4 µM) and Nav1.8 (EC50 = 8.4 ± 1.0 µM)1. Rm4a toxin, along with other closely related ant venom peptides such as Delta-myrmicitoxin-Ta3a, Myrmicitoxin1-Pm1a, Myrmicitoxin1-Pm2a and Poneratoxin, represents a new class of NaV channel modulators. These toxins are structurally and functionally distinct from previously characterized peptide-based NaV modulators, offering valuable insights into the evolutionary adaptations of ant venom. The effects of these toxins on NaV channel currents more closely resemble those of “site 2” alkaloid toxins, such as batrachotoxin1,2. The toxin's ability to prevent channel inactivation and shift the voltage-dependence of activation can lead to increased neuronal excitability and prolonged action potentials, ultimately resulting in enhanced pain signaling. In mice, Rm4a causes dose-dependent spontaneous nocifensive behaviors, further supporting its potential to induce pain1.\u003c\/p\u003e \u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e \u003cul\u003e \u003cli\u003eUsing high-specificity ligands, toxins, and engineered peptides to dissect closely related receptor\/channel subtypes and signaling microdomains.\u003c\/li\u003e\n\u003cli\u003ePairing labeled (e.g., fluorescent) proteins\/peptides with advanced imaging to map surface expression, trafficking, and nanoscale organization.\u003c\/li\u003e\n\u003cli\u003eIncreasing emphasis on reproducibility through standardized characterization (identity, purity, and lot QC) and transparent reporting of reagent attributes.\u003c\/li\u003e \u003c\/ul\u003e \u003ch2\u003eCommon research applications\u003c\/h2\u003e \u003cul\u003e \u003cli\u003eElectrophysiology: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eAcross 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.\u003c\/p\u003e \u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e \u003cul\u003e \u003cli\u003eAssay context matters: binding assays, functional modulation, and detection workflows can yield different readouts even for the same target system.\u003c\/li\u003e\n\u003cli\u003eTarget complexity: closely related family members, splice variants, and post-translational modifications can influence apparent specificity and potency.\u003c\/li\u003e\n\u003cli\u003eMatrix and sample effects: buffer composition, detergents, and biological matrices may alter stability or apparent activity; interpret with appropriate controls.\u003c\/li\u003e\n\u003cli\u003eControl concepts: include negative controls and orthogonal validation (e.g., genetic perturbation or alternative reagents) to support robust interpretation.\u003c\/li\u003e \u003c\/ul\u003e \u003c!-- Sources (internal): - UniProt Knowledgebase (UniProtKB) — UniProt Consortium — https:\/\/www.uniprot.org\/ - NCBI Gene — National Center for Biotechnology Information (NCBI) — https:\/\/www.ncbi.nlm.nih.gov\/gene\/ - NCBI Protein — National Center for Biotechnology Information (NCBI) — https:\/\/www.ncbi.nlm.nih.gov\/protein\/ - PubChem — NIH\/NLM\/NCBI — https:\/\/pubchem.ncbi.nlm.nih.gov\/ - IUPHAR\/BPS Guide to Pharmacology — IUPHAR\/BPS — https:\/\/www.guidetopharmacology.org\/ - RCSB Protein Data Bank (PDB) — RCSB PDB — https:\/\/www.rcsb.org\/ - NCBI Bookshelf — NIH\/NLM — https:\/\/www.ncbi.nlm.nih.gov\/books\/ --\u003e","brand":"Alomone Labs","offers":[{"title":"Default Title","offer_id":53073021272429,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STR-010-Rm4a-3uM-on-HEK-Nav1.7-1_624.jpg?v=1772699896","url":"https:\/\/www.ebiohippo.com\/products\/ectatotoxin-rm4a-bhp21300275","provider":"BioHippo","version":"1.0","type":"link"}