{"product_id":"heteropodatoxin-1-bhp21300223","title":"Heteropodatoxin-1","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eHeteropodatoxin-1\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\u003eNav1.9, Nav1.7 and Kv4.2\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: 3910.4 Da, Formula: C168H238N46O51S6.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Heteropoda venatoria (Brown huntsman spider) (Aranea venatoria).\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\u003eDisulfide bonds between: Cys2-Cys17, Cys9-Cys22, Cys16-Cys27 Trp33 - 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\u003eHeteropodatoxin-1 (HpTX1 or kappa-sparatoxin-Hv1a) is a peptide toxin originally isolated from Heteropoda venatoria, a spider species that is mostly present in tropical regions of the world. This toxin belongs to the Heteropoda toxins family that includes HpTX1, HpTX2 and HpTX3, all of which were shown to be Kv4.2 voltage gated potassium channel inhibitors1.Recently it has been found that HpTX1 is a Nav channel pharmacological tool as well. HpTX1 inhibits Nav1.7 and activates Nav1.9, but has no effect on Nav1.8 channel2.The voltage-gated sodium channels Nav1.7, Nav1.8 and Nav1.9, preferentially expressed in the peripheral terminals of sensory neurons and are critical for pain perception in peripheral nociceptors3. Loss of function of Nav1.7 leads to congenital insensitivity to pain in humans2. Genetic and functional studies have illustrated that mutations in Nav1.8 and Nav1.9 cause human pain disorders, providing direct clinical evidence linking these two channels to human pain. Considering that the three channels play distinct roles in the generation and propagation of action potentials, they might regulate pain signaling cooperatively. HpTx1-induced hypersensitivity is mediated by Nav1.9 activation and offers pharmacological insight into the relationship of the three Nav channels in pain signaling2.\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":53073018650989,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STH-320-Heteropodatoxin-1-4uM-on-Nav1.7-in-oocytes-1024x519_238.jpg?v=1772699890","url":"https:\/\/www.ebiohippo.com\/products\/heteropodatoxin-1-bhp21300223","provider":"BioHippo","version":"1.0","type":"link"}