{"product_id":"hstx1-toxin-bhp21300221","title":"HsTx1 Toxin","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eHsTx1 Toxin\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\u003eKV1.3 K+ 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: 3818.5 Da, Formula: C149H246N54O46S9.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Heterometrus spinifer (Asia giant forest scorpion) (Malaysian black scorpion).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eQuality attributes:\u003c\/strong\u003e Purity: ≥99% (HPLC); Bioassay tested: Yes; Sterile \/ endotoxin-free: No.\u003c\/li\u003e \u003c\/ul\u003e \u003ch3\u003eModifications\u003c\/h3\u003e \u003cp\u003eDisulfide bonds between: Cys3-Cys24, Cys9-Cys29, Cys13-Cys31 and Cys19-Cys34 Cys34 - 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\u003eMany K+ channel blockers have been identified in the scorpion venom1. These peptide toxins consist of 29 to 39 amino acids, and commonly share three disulfide bonds. Their 3D structure comprises a helix and a double- or triple-stranded β-sheet2. The functional sites of the toxins are located either on the solvent exposed face of the β-sheet, or on the helix, depending on the type of K+ channel targeted3.Potassium channel toxin alpha-KTx 6.3 (HsTx1) is a 34 amino acid peptidyl toxin isolated from the Heterometrus spinifer (Asia giant forest scorpion, Malaysian black scorpion) venom4. HsTx1 is one of the most active peptidic inhibitors of rat KV1.3 channels ever described, with an IC50 of approx. 12 pM4. HsTX1 belongs to a structural class of scorpion K+ channel inhibitors which includes Pandinus imperator toxin 1 (Pi1) and Maurotoxin (MTX) (#STM-340), two toxins containing 35 residues and four disulphide bridges5.\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":53073018552685,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STH-300_gr_434.gif?v=1772699892","url":"https:\/\/www.ebiohippo.com\/products\/hstx1-toxin-bhp21300221","provider":"BioHippo","version":"1.0","type":"link"}