{"title":"Neuroscience, Alzheimer","description":"","products":[{"product_id":"tau-pt217-elisa-kit-bhe21400001","title":"TAU pT217 ELISA KIT","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTAU pT217 ELISA KIT\u003c\/strong\u003e is an ELISA-based immunoassay designed for quantitative measurement of \u003cstrong\u003eTAU pT181\u003c\/strong\u003e in research samples. It is commonly used to generate traceable concentration data for biomarker discovery, pathway studies, and comparative analyses across experimental conditions.\u003c\/p\u003e\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eAssay format:\u003c\/strong\u003e Quantitative Colorimetric ELISA. The format defines how signal scales with analyte abundance and how results are interpreted across a standard curve.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eWorking range and sensitivity:\u003c\/strong\u003e dynamic range 1.17-800pg\/mL; analytical sensitivity 1.17 pg\/mL. Use these values to plan dilutions and keep readouts within the linear portion of the calibration curve.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSample compatibility:\u003c\/strong\u003e Intended for Plasma, Serum matrices. As with most immunoassays, matrix composition can influence apparent signal and should be evaluated with dilution linearity and spike-recovery concepts.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eRecovery reference:\u003c\/strong\u003e Typical recovery is reported as 80-120%. Recovery helps assess whether the sample matrix interferes with detection of spiked analyte.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eThis kit is supplied for research use in laboratory settings where defined, quantitative readouts are needed for experimental interpretation.\u003c\/p\u003e\u003ch2\u003eBiological background\u003c\/h2\u003e\u003cp\u003eThis gene encodes the microtubule-associated protein tau (MAPT) whose transcript undergoes complex, regulated alternative splicing, giving rise to several mRNA species. MAPT transcripts are differentially expressed in the nervous system, depending on stage of neuronal maturation and neuron type. MAPT gene mutations have been associated with several neurodegenerative disorders such as Alzheimer's disease, Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiomarker translation in RUO settings:\u003c\/strong\u003e Increasing use of quantitative immunoassays to stratify experimental cohorts, track longitudinal changes, and benchmark model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMatrix-aware assay design:\u003c\/strong\u003e Greater emphasis on dilution linearity, spike-recovery, and control concepts to reduce matrix-driven artifacts in serum\/plasma and complex lysates.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eIntegration with multi-omics:\u003c\/strong\u003e ELISA measurements are often used alongside transcriptomics and proteomics to connect abundance changes with pathway activity and phenotype.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eComparative quantification:\u003c\/strong\u003e Measure relative changes in analyte levels across treatments, time points, or genotypes to support mechanistic hypotheses.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAssay development and standardization:\u003c\/strong\u003e Generate reproducible concentration inputs for method qualification, inter-operator comparisons, or bridging studies across platforms.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eModel and sample characterization:\u003c\/strong\u003e Profile baseline and stimulated levels to help interpret immune, endocrine, neurodegenerative, or metabolic phenotypes (as relevant to the target).\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eInterpretation typically focuses on direction and magnitude of change in the context of controls and sample handling metadata, rather than single-point absolute values.\u003c\/p\u003e\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eMatrix effects:\u003c\/strong\u003e Hemolysis, lipemia, and high protein content can alter background and apparent concentration. Consider consistent collection\/processing and evaluate dilution behavior.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eIsoforms and modified forms:\u003c\/strong\u003e Some targets exist as isoforms, fragments, or post-translationally modified species. Ensure the measured form aligns with the biological question and the kit’s intended analyte definition.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eControl concepts:\u003c\/strong\u003e Use negative\/blank controls, replicate wells, and—when feasible—orthogonal confirmation (e.g., WB or MS) to strengthen conclusions.\u003c\/li\u003e\n\u003c\/ul\u003e\u003c!-- Sources (internal): - UniProt (search): https:\/\/www.uniprot.org\/uniprotkb?query=TAU+pT181 - NCBI Gene (search): https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=TAU+pT181 - Ensembl (search): https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=TAU+pT181 - PubMed (search): https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=TAU+pT181 - NCBI Bookshelf (background reviews): https:\/\/www.ncbi.nlm.nih.gov\/books\/?term=TAU+pT181 --\u003e","brand":"Biohippo Inc","offers":[{"title":"96 T","offer_id":53047344071021,"sku":"HY086028-96T","price":748.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ELISA_Kits_Display_Image_1_77bb7d88-6a9a-4d35-b5ea-0fd4540b84e3.png?v=1772020745"},{"product_id":"tau-pt181-elisa-kit-bhe21400002","title":"TAU pT181 ELISA KIT","description":"\u003ch2\u003eOverview\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTAU pT181 ELISA KIT\u003c\/strong\u003e is an ELISA-based immunoassay designed for quantitative measurement of \u003cstrong\u003eTAU pT181\u003c\/strong\u003e in research samples. It is commonly used to generate traceable concentration data for biomarker discovery, pathway studies, and comparative analyses across experimental conditions.\u003c\/p\u003e\u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eAssay format:\u003c\/strong\u003e Quantitative Colorimetric ELISA. The format defines how signal scales with analyte abundance and how results are interpreted across a standard curve.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eWorking range and sensitivity:\u003c\/strong\u003e dynamic range 1.56-600pg\/mL; analytical sensitivity 1.56 pg\/ml. Use these values to plan dilutions and keep readouts within the linear portion of the calibration curve.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSample compatibility:\u003c\/strong\u003e Intended for Plasma, Serum matrices. As with most immunoassays, matrix composition can influence apparent signal and should be evaluated with dilution linearity and spike-recovery concepts.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eRecovery reference:\u003c\/strong\u003e Typical recovery is reported as 80-120%. Recovery helps assess whether the sample matrix interferes with detection of spiked analyte.\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eThis kit is supplied for research use in laboratory settings where defined, quantitative readouts are needed for experimental interpretation.\u003c\/p\u003e\u003ch2\u003eBiological background\u003c\/h2\u003e\u003cp\u003eThis gene encodes the microtubule-associated protein tau (MAPT) whose transcript undergoes complex, regulated alternative splicing, giving rise to several mRNA species. MAPT transcripts are differentially expressed in the nervous system, depending on stage of neuronal maturation and neuron type. MAPT gene mutations have been associated with several neurodegenerative disorders such as Alzheimer's disease, Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.\u003c\/p\u003e\u003ch2\u003eResearch relevance and current trends\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiomarker translation in RUO settings:\u003c\/strong\u003e Increasing use of quantitative immunoassays to stratify experimental cohorts, track longitudinal changes, and benchmark model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMatrix-aware assay design:\u003c\/strong\u003e Greater emphasis on dilution linearity, spike-recovery, and control concepts to reduce matrix-driven artifacts in serum\/plasma and complex lysates.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eIntegration with multi-omics:\u003c\/strong\u003e ELISA measurements are often used alongside transcriptomics and proteomics to connect abundance changes with pathway activity and phenotype.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eCommon research applications\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eComparative quantification:\u003c\/strong\u003e Measure relative changes in analyte levels across treatments, time points, or genotypes to support mechanistic hypotheses.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAssay development and standardization:\u003c\/strong\u003e Generate reproducible concentration inputs for method qualification, inter-operator comparisons, or bridging studies across platforms.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eModel and sample characterization:\u003c\/strong\u003e Profile baseline and stimulated levels to help interpret immune, endocrine, neurodegenerative, or metabolic phenotypes (as relevant to the target).\u003c\/li\u003e\n\u003c\/ul\u003e\u003cp\u003eInterpretation typically focuses on direction and magnitude of change in the context of controls and sample handling metadata, rather than single-point absolute values.\u003c\/p\u003e\u003ch2\u003eNotes for experimental interpretation\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eMatrix effects:\u003c\/strong\u003e Hemolysis, lipemia, and high protein content can alter background and apparent concentration. Consider consistent collection\/processing and evaluate dilution behavior.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eIsoforms and modified forms:\u003c\/strong\u003e Some targets exist as isoforms, fragments, or post-translationally modified species. Ensure the measured form aligns with the biological question and the kit’s intended analyte definition.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eControl concepts:\u003c\/strong\u003e Use negative\/blank controls, replicate wells, and—when feasible—orthogonal confirmation (e.g., WB or MS) to strengthen conclusions.\u003c\/li\u003e\n\u003c\/ul\u003e\u003c!-- Sources (internal): - UniProt (search): https:\/\/www.uniprot.org\/uniprotkb?query=TAU+pT181 - NCBI Gene (search): https:\/\/www.ncbi.nlm.nih.gov\/gene\/?term=TAU+pT181 - Ensembl (search): https:\/\/www.ensembl.org\/Multi\/Search\/Results?q=TAU+pT181 - PubMed (search): https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=TAU+pT181 - NCBI Bookshelf (background reviews): https:\/\/www.ncbi.nlm.nih.gov\/books\/?term=TAU+pT181 --\u003e","brand":"Biohippo Inc","offers":[{"title":"96 T","offer_id":53047344267629,"sku":"HY086018-96T","price":748.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ELISA_Kits_Display_Image_1_cb094c08-85ea-4a10-b124-c5c6a4f73ec9.png?v=1772020746"},{"product_id":"wrw4-bhp21300067","title":"WRW4","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eWRW4\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\u003eFPR2, FPR3 receptors\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 Calcium imaging assay.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eMolecular identity:\u003c\/strong\u003e CAS: 878557-55-2, MW: 1104.3 Da, Formula: C61H65N15O6.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Synthetic peptide.\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\u003eTrp6 - 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\u003eChemotactic factors from both Gram-positive and Gram-negative bacteria are short peptides with N-formyl methionine at the N-terminus (extensively reviewed in reference 1). These peptides are released from bacteria during infection and activate formyl peptide receptors (FPR), members of the G-protein coupled receptor (GPCR) superfamily. In humans, the FPR family consists mainly of three receptors, FPR1, FPR2\/ALX (formerly FPRL1), and FPR3 (formerly FPRL2) which all couple to the Gi subtype of G-proteins and ultimately lead to the activation of phospholipase C and intracellular Ca2+ increase1,2.WRW4 is a selective and potent antagonist of the Formyl peptide receptors (FPR2 and FPR3)3,4, which was identified by screening hexapeptide libraries that inhibit the binding of the FPR2 agonist WKYMVm to its specific receptor, in RBL-2H3 cells3. In human umbilical vein endothelial cells, WRW4 (10 mM), inhibited CCL2 production, which was stimulated by serum amyloid A5.FPR2 is expressed in the promyelocytic leukemia cell line HL-60 as well as in the chronic myelogenous leukemia cell line K5626. In human neutrophils, 10 µM WRW4 blocked the specific FPR2 agonist (MMK1) induced Ca2+ influx. In addition, at the same concentration WRW4 blocked Ca2+ influxes, generated by stimulation with the Alzheimer's diseases Amiloide β42 peptide, by lipoxin A4 and by fMLF3.\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\u003eCalcium imaging assay: 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":53073008755053,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/GPW-110_gr_20.gif?v=1772699878"},{"product_id":"recombinant-human-prongf-cleavage-resistant-protein-bhp21300084","title":"Recombinant human proNGF (cleavage resistant) protein","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eRecombinant human proNGF (cleavage resistant) protein\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\u003ep75NTR, VPS10 domain-containing receptors\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 Neurite outgrowth assay, Cell survival assay.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eMolecular identity:\u003c\/strong\u003e MW: 49.9 kDa (dimer).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Recombinant, E. coli.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eQuality attributes:\u003c\/strong\u003e Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile \/ endotoxin-free: Yes.\u003c\/li\u003e \u003c\/ul\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\u003eThe proneurotrophins (proNT) are, as their name suggests, the proform of the neurotrophins. The neurotrophins (NT) are a family of soluble, basic growth factors which regulate neuronal development, maintenance, survival and death in the CNS and the PNS.1 They exert their biological effects by binding to two types of receptors: the Trk receptors, and the p75NTR receptor.Like many other proteins, mature NT arise from the proteolytic cleavage of the precursor form by various proteases: plasmin, furin, MP7, PC1\/3, PC2, PC5\/6, PC7 and PACE4, which cut behind a pair or even a single basic residue.2 This has been known for many years, and it was thought that the roles of the prodomain were to aid in the folding of the mature protein and to sort the mature neurotrophin into the various secretion pathways.3 However, recently an assortment of papers have been published which suggest new roles for the proNT. It has been found that proNerve Growth Factor (proNGF), and not mature NGF, is the predominant isoform found in the human brain as well as in a variety of cell types, including mast cells, sciatic nerve cells, thyroid gland, skeletal muscle, prostate gland, hippocampus and hair follicle.4 Thus, the case of the mouse salivary gland, which is the most abundant source of mature NGF, seems to be the exception and not the rule.proNGF is the ligand preferred by p75NTR.5 Therefore, cleavage resistant proNGF (mutated at the cleavage site to insure that it retains the prodomain) induced apoptosis ten times more effectively than mature NGF in a vascular smooth muscle cell line expressing p75NTR but not Trk receptors.5 However, proNGF can also mediate survival. Rattenholl et al. have shown that proNGF was as effective as NGF in inducing survival of DRG neurons.3 Fahnestock et al. have shown that a mutated proNGF exhibits neurite outgrowth on both PC12 cells and mouse sympathetic cervical ganglions.6A neccesary but not sufficient partner for proNGF is sortilin, a 95 kDa member of the Vps10p domain receptor family which is expressed in a variety of tissues, notably brain, spinal tissue and muscle. However, not all cells expressing p75NTR and sortilin react to proNGF by becoming apoptotic. For example, in mature pig oligodendrocytes, which express p75NTR and sortilin, proNGF induces survival.7A close analysis of the literature shows that there are at least four types of proNGF which have been used in biological assays. One, produced in mammalian cell culture, contains two mutations at the furin cleavage site, two mutations at the C-terminus, and the addition of a C-terminal His tag.5 A second proNGF, produced in baculovirus, has only one mutation, at the cleavage site.6 A third proNGF has been purified from the brains of Alzheimer's patients, and is highly glycosylated.8 A fourth, with no mutations, has been expressed and purified from E.coli.3 The large variation between results obtained may be due to the different types of preparations assayed. Another crucial issue is the cell type and origin. Even in cells of the same type, for example, in oligodendrocytes: opposing effects of proNGF were seen in rat oligodendrocytes where it caused apoptosis,9 however, in pig oligodendrocytes it induced survival.7 It should be noted that rat and pig oligodendrocytes do not express the same panel of receptors: rat oligodendrocytes do not express TrkA whereas pig (and human) oligodendrocytes do.\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\u003eNeurite outgrowth assay: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.\u003c\/li\u003e\n\u003cli\u003eCell survival assay: 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":53073009279341,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/N-285_gr_642.gif?v=1772699875"},{"product_id":"recombinant-human-prongf-protein-bhp21300083","title":"Recombinant human proNGF protein","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eRecombinant human proNGF protein\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\u003ep75NTR, VPS10 domain-containing receptors\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 Neurite outgrowth assay, Cell survival assay.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eMolecular identity:\u003c\/strong\u003e MW: 50.2 kDa (dimer).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Recombinant, E. coli.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eQuality attributes:\u003c\/strong\u003e Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile \/ endotoxin-free: Yes.\u003c\/li\u003e \u003c\/ul\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\u003eThe proneurotrophins (proNT) are, as their name suggests, the proform of the neurotrophins. The neurotrophins (NT) are a family of soluble, basic growth factors which regulate neuronal development, maintenance, survival and death in the CNS and the PNS.1 They exert their biological effects by binding to two types of receptors: the Trk receptors, and the p75NTR receptor.Like many other proteins, mature NT arise from the proteolytic cleavage of the precursor form by various proteases: plasmin, furin, MP7, PC1\/3, PC2, PC5\/6, PC7 and PACE4, which cut behind a pair or even a single basic residue.2 This has been known for many years, and it was thought that the roles of the prodomain were to aid in the folding of the mature protein and to sort the mature neurotrophin into the various secretion pathways.3 However, recently an assortment of papers have been published which suggest new roles for the proNT. It has been found that proNerve Growth Factor (proNGF), and not mature NGF, is the predominant isoform found in the human brain as well as in a variety of cell types, including mast cells, sciatic nerve cells, thyroid gland, skeletal muscle, prostate gland, hippocampus and hair follicle.4 Thus, the case of the mouse salivary gland, which is the most abundant source of mature NGF, seems to be the exception and not the rule.proNGF is the ligand preferred by p75NTR.5 Therefore, cleavage resistant proNGF (mutated at the cleavage site to insure that it retains the prodomain) induced apoptosis ten times more effectively than mature NGF in a vascular smooth muscle cell line expressing p75NTR but not Trk receptors.5 However, proNGF can also mediate survival. Rattenholl et al. have shown that proNGF was as effective as NGF in inducing survival of DRG neurons.3 Fahnestock et al. have shown that a mutated proNGF exhibits neurite outgrowth on both PC12 cells and mouse sympathetic cervical ganglions.6A neccesary but not sufficient partner for proNGF is sortilin, a 95 kDa member of the Vps10p domain receptor family which is expressed in a variety of tissues, notably brain, spinal tissue and muscle. However, not all cells expressing p75NTR and sortilin react to proNGF by becoming apoptotic. For example, in mature pig oligodendrocytes, which express p75NTR and sortilin, proNGF induces survival.7A close analysis of the literature shows that there are at least four types of proNGF which have been used in biological assays. One, produced in mammalian cell culture, contains two mutations at the furin cleavage site, two mutations at the C-terminus, and the addition of a C-terminal His tag.5 A second proNGF, produced in baculovirus, has only one mutation, at the cleavage site.6 A third proNGF has been purified from the brains of Alzheimer's patients, and is highly glycosylated.8 A fourth, with no mutations, has been expressed and purified from E.coli.3 The large variation between results obtained may be due to the different types of preparations assayed. Another crucial issue is the cell type and origin. Even in cells of the same type, for example, in oligodendrocytes: opposing effects of proNGF were seen in rat oligodendrocytes where it caused apoptosis,9 however, in pig oligodendrocytes it induced survival.7 It should be noted that rat and pig oligodendrocytes do not express the same panel of receptors: rat oligodendrocytes do not express TrkA whereas pig (and human) oligodendrocytes do.\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\u003eNeurite outgrowth assay: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.\u003c\/li\u003e\n\u003cli\u003eCell survival assay: 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":53073009377645,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/N-280_gr_990.gif?v=1772699880"},{"product_id":"recombinant-mouse-prongf-cleavage-resistant-protein-bhp21300080","title":"Recombinant mouse proNGF (cleavage resistant) protein","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eRecombinant mouse proNGF (cleavage resistant) protein\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\u003ep75NTR, VPS10 domain-containing receptors\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 Neurite outgrowth assay, Cell survival assay.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eMolecular identity:\u003c\/strong\u003e MW: 50.2 kDa (dimer).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Recombinant, E. coli.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eQuality attributes:\u003c\/strong\u003e Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile \/ endotoxin-free: Yes.\u003c\/li\u003e \u003c\/ul\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\u003eThe proneurotrophins (proNT) are, as their name suggests, the proform of the neurotrophins. The neurotrophins (NT) are a family of soluble, basic growth factors which regulate neuronal development, maintenance, survival and death in the CNS and the PNS.1 They exert their biological effects by binding to two types of receptors: the Trk receptors, and the p75NTR receptor.Like many other proteins, mature NT arise from the proteolytic cleavage of the precursor form by various proteases: plasmin, furin, MP7, PC1\/3, PC2, PC5\/6, PC7 and PACE4, which cut behind a pair or even a single basic residue.2 This has been known for many years, and it was thought that the roles of the prodomain were to aid in the folding of the mature protein and to sort the mature neurotrophin into the various secretion pathways.3 However, recently an assortment of papers have been published which suggest new roles for the proNT. It has been found that proNerve Growth Factor (proNGF), and not mature NGF, is the predominant isoform found in the human brain as well as in a variety of cell types, including mast cells, sciatic nerve cells, thyroid gland, skeletal muscle, prostate gland, hippocampus and hair follicle.4 Thus, the case of the mouse salivary gland, which is the most abundant source of mature NGF, seems to be the exception and not the rule.proNGF is the ligand preferred by p75NTR.5 Therefore, cleavage resistant proNGF (mutated at the cleavage site to insure that it retains the prodomain) induced apoptosis ten times more effectively than mature NGF in a vascular smooth muscle cell line expressing p75NTR but not Trk receptors.5 However, proNGF can also mediate survival. Rattenholl et al. have shown that proNGF was as effective as NGF in inducing survival of DRG neurons.3 Fahnestock et al. have shown that a mutated proNGF exhibits neurite outgrowth on both PC12 cells and mouse sympathetic cervical ganglions.6A neccesary but not sufficient partner for proNGF is sortilin, a 95 kDa member of the Vps10p domain receptor family which is expressed in a variety of tissues, notably brain, spinal tissue and muscle. However, not all cells expressing p75NTR and sortilin react to proNGF by becoming apoptotic. For example, in mature pig oligodendrocytes, which express p75NTR and sortilin, proNGF induces survival.7A close analysis of the literature shows that there are at least four types of proNGF which have been used in biological assays. One, produced in mammalian cell culture, contains two mutations at the furin cleavage site, two mutations at the C-terminus, and the addition of a C-terminal His tag.5 A second proNGF, produced in baculovirus, has only one mutation, at the cleavage site.6 A third proNGF has been purified from the brains of Alzheimers patients, and is highly glycosylated.8 A fourth, with no mutations, has been expressed and purified from E.coli.3 The large variation between results obtained may be due to the different types of preparations assayed. Another crucial issue is the cell type and origin. Even in cells of the same type, for example, in oligodendrocytes: opposing effects of proNGF were seen in rat oligodendrocytes where it caused apoptosis,9 however, in pig oligodendrocytes it induced survival.7 It should be noted that rat and pig oligodendrocytes do not express the same panel of receptors: rat oligodendrocytes do not express TrkA whereas pig (and human) oligodendrocytes do.\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\u003eNeurite outgrowth assay: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.\u003c\/li\u003e\n\u003cli\u003eCell survival assay: 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":53073009705325,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/N-255_2_gr_953.gif?v=1772699879"},{"product_id":"alpha-conotoxin-rgia-bhp21300141","title":"α-Conotoxin RgIA","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eα-Conotoxin RgIA\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\u003eα9α10 nAChRs, α7, and N-Type Ca2+ 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: 1571 Da, Formula: C59H95N25O18S4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Conus regius (Crown cone).\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-Cys8, Cys3-Cys12\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\u003eα-conotoxin RgIA (RgIA) is a 13 amino acid peptidyl toxin cloned from a genomic DNA library of the marine worm-hunting sea snail, Conus regius1. RgIA belongs to the α4\/3 subfamily of conotoxins (i.e., a family of peptides with four amino acids in the first loop and three in the second loop) and is a potent and selective antagonist of the α9α10 nicotinic acetylcholine receptor (nAChR) subtype, which also shows a weak activity towards α7 nAChR1,2. RgIA was also shown to inhibit high-voltage-activated (HVA) calcium channel currents in rat dorsal root ganglion (DRG) neurons3.The nAChRs are acetylcholine-gated ion channels. Given the important physiological roles of nAChRs in pain, inflammation, nicotine addiction, Alzheimer's disease, and Parkinson's disease, specific targeting of the relevant nAChR subtypes is an attractive pharmaceutical strategy. α-conotoxins are among the most promising drug development leads for treating these diseases4,5. RgIA was shown to be an effective analgesic agent in a rat model of nerve injury and also reduced the immune response contributing to peripheral nerve damage6,7. Furthermore, RgIA was shown to prevent neuropathic pain induced by oxaliplatin treatment8.\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":53073009836397,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STC010-a-Conotoxin-RgIA-1uM-5uM-on-a7-nAChR-in-oocytes_202.jpg?v=1772699876"},{"product_id":"alpha-conotoxin-gic-bhp21300146","title":"α-Conotoxin GIC","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eα-Conotoxin GIC\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\u003eα3β2 nAChRs\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: 1609.8 Da, Formula: C61H92N24O20S4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Conus geographus (Geography cone) (Nubecula geographus).\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-Cys8, Cys3-Cys16 Cys16 - 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\u003eα-conotoxin GIC is a 16 amino acid peptidyl toxin originally isolated from a genomic DNA clone of the marine snail, Conus geographus1. This toxin potently and selectively blocks neuronal α3β2 nicotinic acetylcholine receptors (nAChRs) at very low concentrations (IC50 ~ 1.1 nM)1.α-conotoxin GIC has \u0026gt;100,000-fold selectivity for the neuronal α3β2 subtype versus the muscle subtype1. This toxin belongs to the α4\/7-CTx subfamily that primarily targets the vertebrate neuronal nAChRs.Neuronal nAChRs are a heterogeneous family of ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. These distinct receptor subtypes have a pentameric structure consisting of a homomeric or heteromeric combination of 12 different subunits (α2-α10, β2-β4)2.nAChRs are critically important for neuronal survival and cognitive function, as well as regulation of neurodegenerative diseases, including Alzheimer's and Parkinson's. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition. Thus, the subunit makeup of the nAChR subtypes is central to understanding their function in the nervous system and for discovering new subtype-selective drugs2-4.\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":53073009934701,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STC070_gr_983.jpg?v=1772699876"},{"product_id":"recombinant-mouse-prongf-protein-bhp21300079","title":"Recombinant mouse proNGF protein","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eRecombinant mouse proNGF protein\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\u003ep75NTR, VPS10 domain-containing receptors\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 Neurite outgrowth assay, Cell survival assay.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eMolecular identity:\u003c\/strong\u003e MW: 50.4 kDa (dimer).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Recombinant, E. coli.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eQuality attributes:\u003c\/strong\u003e Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile \/ endotoxin-free: Yes.\u003c\/li\u003e \u003c\/ul\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\u003eThe proneurotrophins (proNT) are, as their name suggests, the proform of the neurotrophins. The neurotrophins (NT) are a family of soluble, basic growth factors which regulate neuronal development, maintenance, survival and death in the CNS and the PNS.1 They exert their biological effects by binding to two types of receptors: the Trk receptors, and the p75NTR receptor.Like many other proteins, mature NT arise from the proteolytic cleavage of the precursor form by various proteases: plasmin, furin, MP7, PC1\/3, PC2, PC5\/6, PC7 and PACE4, which cut behind a pair or even a single basic residue.2 This has been known for many years, and it was thought that the roles of the prodomain were to aid in the folding of the mature protein and to sort the mature neurotrophin into the various secretion pathways.3However, recently an assortment of papers have been published which suggest new roles for the proNT. It has been found that proNerve Growth Factor (proNGF), and not mature NGF, is the predominant isoform found in the human brain as well as in a variety of cell types, including mast cells, sciatic nerve cells, thyroid gland, skeletal muscle, prostate gland, hippocampus and hair follicle.4 Thus, the case of the mouse salivary gland, which is the most abundant source of mature NGF, seems to be the exception and not the rule.proNGF is the ligand preferred by p75NTR.5 Therefore, cleavage resistant proNGF (mutated at the cleavage site to insure that it retains the prodomain) induced apoptosis ten times more effectively than mature NGF in a vascular smooth muscle cell line expressing p75NTR but not Trk receptors.5 However, proNGF can also mediate survival. Rattenholl et al. have shown that proNGF was as effective as NGF in inducing survival of DRG neurons.3 Fahnestock et al. have shown that a mutated proNGF exhibits neurite outgrowth on both PC12 cells and mouse sympathetic cervical ganglions.6A neccesary but not sufficient partner for proNGF is sortilin, a 95 kDa member of the Vps10p domain receptor family which is expressed in a variety of tissues, notably brain, spinal tissue and muscle. However, not all cells expressing p75NTR and sortilin react to proNGF by becoming apoptotic. For example, in mature pig oligodendrocytes, which express p75NTR and sortilin, proNGF induces survival.7A close analysis of the literature shows that there are at least four types of proNGF which have been used in biological assays. One, produced in mammalian cell culture, contains two mutations at the furin cleavage site, two mutations at the C-terminus, and the addition of a C-terminal His tag.5 A second proNGF, produced in baculovirus, has only one mutation, at the cleavage site.6 A third proNGF has been purified from the brains of Alzheimers patients, and is highly glycosylated.8 A fourth, with no mutations, has been expressed and purified from E.coli.3 The large variation between results obtained may be due to the different types of preparations assayed. Another crucial issue is the cell type and origin. Even in cells of the same type, for example, in oligodendrocytes: opposing effects of proNGF were seen in rat oligodendrocytes where it caused apoptosis,9 however, in pig oligodendrocytes it induced survival.7 It should be noted that rat and pig oligodendrocytes do not express the same panel of receptors: rat oligodendrocytes do not express TrkA whereas pig (and human) oligodendrocytes do.\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\u003eNeurite outgrowth assay: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.\u003c\/li\u003e\n\u003cli\u003eCell survival assay: 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":53073009967469,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/N-250_pic_58.jpg?v=1772699876"},{"product_id":"recombinant-human-pleiotrophin-protein-bhp21300087","title":"Recombinant human Pleiotrophin protein","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eRecombinant human Pleiotrophin protein\u003c\/strong\u003e is a research-grade protein\/peptide reagent used in research settings. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eMolecular identity:\u003c\/strong\u003e MW: 15.4 kDa.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Recombinant, E. coli.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eQuality attributes:\u003c\/strong\u003e Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile \/ endotoxin-free: Yes.\u003c\/li\u003e \u003c\/ul\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\u003ePleiotrophin (PTN), is a heparin-binding neurotrophic factor. Cells that express either PTN or PTN mRNA include osteoblasts, fetal chondrocytes,1 astrocytes, oligodendroglia, neurons,2 Schwann cells,3 keratinocytes of the stratum basale,3 and selected tumor cell lines.4,5 The expression of PTN increases during the process of brain embryogenesis and reaches maximum levels at time of birth.The role of PTN in neurogenesis and neural plasticity has been revealed by various studies. Embryonic cortical neurons adhere to and extend neurites on PTN coated substratuM6 PTN also induces, in vitro, migration of osteoblasts. 7 PTN coated membrane enhances neuronal migration by haptotaxis.8 PTN bound to agarose beads induces clustering of acetylcholine receptors on embryonic myoblasts.9PTN is expressed in the CA1 region of rat hippocampus in an activity-dependent manner, and is suggested to be involved in the regulation of synaptic plasticity in the hippocampus.10Transfection with PTN cDNA, transforms murine 3T3 fibroblasts into cells that form extensively metastasizing tumors in nude mice.11 PTN is highly expressed in choriocarcinoma, melanoma and, prostate carcinoma. Serum PTN increase in patients with pancreatic and colon carcinomas.12After focal forebrain ischemia, PTN is expressed in astrocytes, OX-42 positive macrophages, and endothelial cells in areas of developing neovascularization.13 PTN is also deposited in senile plaques in Alzheimer's disease and Down's syndrome.14\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\u003eAssay development and optimization: used as a reference material or tool reagent in RUO workflows.\u003c\/li\u003e\n\u003cli\u003eReagent validation: supports conceptual controls such as competition\/neutralization, when relevant.\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\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":53073010164077,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}]},{"product_id":"alpha-conotoxin-mii-bhp21300144","title":"α-Conotoxin MII","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eα-Conotoxin MII\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\u003eα3β2, α6β2 nAChRs\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 CAS: 175735-93-0, MW: 1711 Da, Formula: C67H103N23O22S4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Conus magus (Magical cone).\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-Cys8, Cys3-Cys16 Cys16 - 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\u003eα-Conotoxin MII is a 16 amino acid peptidyl toxin originally isolated from the venom of the marine snail, Conus magus1. This toxin was initially thought to be a selective antagonist for α3β2 nicotinic acetylcholine receptors (nAChRs)1. Subsequently, it has been shown that α-conotoxin MII is also an α6β2* nAChR subtype selective antagonist2 and it potently blocks β3-containing neuronal nAChRs3.Neuronal nAChRs are a heterogeneous family of ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. These different receptor subtypes have a pentameric structure consisting of the homomeric or heteromeric combination of 12 different subunits (α2-α10, β2-β4)4.nAChRs are critically important for neuronal survival and cognitive function, as well as regulation of neurodegenerative diseases, including Alzheimer's and Parkinson's. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition. Thus, the subunit makeup of the nAChR subtypes is central to understanding their function in the nervous system and for discovering new subtype-selective drugs4-6.\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":53073010327917,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STC040-a-Conotoxin-MII-20-nM-on-a3b2-nAChR_341.jpg?v=1772699874"},{"product_id":"alpha-conotoxin-bt1-8-bhp21300142","title":"α-Conotoxin Bt1.8","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eα-Conotoxin Bt1.8\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\u003eα6\/α3β2β3, α3β2 nAChRs\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: 1646 Da, Formula: C63H100N22O22S4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Conus betulinus (Beech cone).\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-Cys8, Cys3-Cys16 Cys16 - 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\u003eα-conotoxin Bt1.8 (Bt1.8) is a 16 amino acid peptidyl toxin originally cloned from the venom duct of the worm-hunting cone snail, Conus betulinus1. This toxin potently and selectively blocks neuronal α6\/α3β2β3 and α3β2 nicotinic acetylcholine receptors (nAChRs), with IC50 values of 2.1 nM and 9.4 nM, respectively1. Bt1.8 belongs to the α4\/7-CTx subfamily that primarily targets the vertebrate neuronal nAChRs.Neuronal nAChRs are a heterogeneous family of ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. These distinct receptor subtypes have a pentameric structure consisting of a homomeric or heteromeric combination of 12 different subunits (α2-α10, β2-β4)2.nAChRs are critically important for neuronal survival and cognitive function, as well as regulation of neurodegenerative diseases, including Alzheimer's and Parkinson's. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition. Thus, the subunit makeup of the nAChR subtypes is central to understanding their function in the nervous system and for discovering new subtype-selective drugs2-4.\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":53073010393453,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STC020_gr_984.jpg?v=1772699879"},{"product_id":"alpha-conotoxin-txid-bhp21300148","title":"α-Conotoxin TxID","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eα-Conotoxin TxID\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\u003eα3\/β4 nAChR\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 CAS: 1496617-64-1, MW: 1489.8 Da, Formula: C58H92N18O18S5.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Conus textile (Cloth-of-gold cone).\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-Cys8, Cys3-Cys15Cys15 - 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\u003eα-Conotoxin TxID (a-CTx TxID) is a 15 amino acid peptidyl toxin isolated from the mollusk-hunting cone snail, Conus textile. This toxin belongs to the α-4\/6 conotoxin (α-CTx) subfamily, that potently blocks the α3β4 nicotinic acetylcholine receptor (nAChR) subtype with high selectivity. In addition, α-CTx TxID blocks the closely related α6\/α3β4 nAChR but exhibits minimal activity towards other nAChR subtypes. α-CTx TxID is the most potent α3β4 nAChR antagonist characterized thus far and has a unique selectivity profile 1.Neuronal nAChRs are widely distributed throughout the central and peripheral nervous systems. These receptors play important roles in normal physiology and are involved in many diseases such as epilepsy, pain, addiction, Alzheimer's disease, Parkinson's disease, schizophrenia, as well as breast and lung carcinoma. The α3β4 nAChR is the most prevalent subtype in the brain and is associated with nicotine addiction, neuropathic pain and small cell lung cancer2. Given the diverse functions of the nAChRs, the a-CTx TxID may be a valuable tool for elucidating the distinct roles of the α3β4 nAChRs in a variety of normal and pathological processes1,3. a-CTx TxID has been used for these purposes and it was recently shown to exhibit anti-tumor activity, which may provide novel strategies for cancer treatment4.\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":53073010458989,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STC-110_gr._80.png?v=1772699876"},{"product_id":"alpha-conotoxin-buia-bhp21300143","title":"α-Conotoxin BuIA","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eα-Conotoxin BuIA\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\u003eα6\/α3β2β3, α3β2, and α3β4 nAChRs\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: 1311.6 Da, Formula: C54H82N14O16S4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Conus bullatus (Bubble cone).\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-Cys8, Cys3-Cys13 Cys13 - 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\u003eα-Conotoxin BuIA is a 13 amino acid peptidyl toxin that was originally isolated from the fish-eating snail, Conus bullatus1. This toxin exhibits strong antagonistic activity at α6\/α3β2β3, α3β2, and α3β4 nicotinic acetylcholine receptors (nAChRs) and has the unique ability to kinetically discriminate between the β2 and β4-containing receptor subtypes, as the off-rates are rapid for β2-subunit, but very slow for β4-containing nAChRs. α-Conotoxin BuIA is a member of the A-superfamily of conotoxins and possess an unusual 4\/4 disulfide scaffold. This toxin appears to be a valuable probe to distinguish among nAChRs containing different α and β subunits1-4.nAChRs are pentameric ligand-gated ion channels that are critically important for neuronal survival and cognitive function, as well as regulation of neurodegenerative diseases, including Alzheimer's and Parkinson's. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition. Thus, the subunit makeup of the nAChR subtypes is central to understanding their function in the nervous system and for discovering new subtype-selective drugs5-7.\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":53073011409261,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STC030-a-Conotoxin-BuIA-10-nM-100nM-on-a3b2-nAChR_585.jpg?v=1772699879"},{"product_id":"alpha-conotoxin-gexiva-bhp21300156","title":"α-Conotoxin GeXIVA","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eα-Conotoxin GeXIVA\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\u003eα9α10 nAChRs\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 CAS: 2010167-25-4, MW: 3453 Da, Formula: C139H227N55O41S4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Conus generalis (General cone).\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\u003eThe native disulfide bond pairing has not been studied.\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\u003eα-Conotoxin GeXIVA (αO-conotoxin GeXIVA or GeXIVA) is a 28 amino acid peptidyl toxin, which was discovered from a transcriptome analysis of the South China Sea mollusk, Conus generalis1. GeXIVA belongs to the O1-gene superfamily and is a potent and selective antagonist of the α9α10 nicotinic acetylcholine receptor (nAChR) subtype1. The toxin-mediated blockade of α9α10 nAChRs is voltage-dependent, suggesting that the toxin binding site might be allosterically coupled to a voltage-sensitive domain of the nAChR1,2. GeXIVA exhibits analgesic activity in animal models of pain without the development of tolerance1-4.nAChRs are involved in a wide range of physiological functions in the central and peripheral nervous systems. Alterations in nAChR expression and\/or function are associated with a number of pathophysiological conditions including pain, addiction, epilepsy, autism, schizophrenia, Alzheimer's and Parkinson's diseases, as well as many types of cancers2,6. The nAChRs are formed from the assembly of five homologous subunits and neuronal nAChRs are assembled from a combination of α- and β-subunits. They share a common basic structure, but their pharmacological and functional properties arise from the wide range of different subunit combinations which generate distinctive subtypes6. The α9α10 nAChR subtype is a potential target for treating chronic pain, wound healing, the pathophysiology of the auditory system, and various cancers4-7. GeXIVA potently alleviated neuropathic pain in several rat models1-4 and also exhibited an antitumor effect5,8.\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":53073015144813,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STC220-a-Conotoxin-GeXIVA-100nM-500nM-on-a7-nAChR-in-oocytes_926.jpg?v=1772699873"},{"product_id":"alpha-conotoxin-pia-bhp21300195","title":"α-Conotoxin PIA","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eα-Conotoxin PIA\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\u003eα6 nAChR\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 CAS: 669050-68-4, MW: 1981 Da, Formula: C79H125N27O25S4.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Conus purpurascens (Purple cone).\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: Cys4-Cys10 and Cys5-Cys18 Cys18 - 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\u003eα-Conotoxin PIA is a peptide toxin originally isolated from Conus purpurascens and belongs to the A superfamily of conotoxins. It is a selective antagonist for heteromeric α6 subunit -containing nicotinic acetylcholine receptors (nAChR). α-Conotoxin PIA binds on the extracellular portion of the nAChR and distinguishes α6 from α3 subunits due to its lower affinity for α3.The alpha-conotoxin PIA has an \"omega-shaped\" overall topology, containing spacing of Cys residues, disulfide connectivity, and the SNPV (serine, asparagine, proline, valine) sequence in the first peptide loop. The second loop demonstrates a kink in Pro15 that provides a distinct steric and electrostatic environment1-3.Evidence has shown that α-conotoxin PIA has the ability to potently block nicotine-stimulated dopamine release in rat striatal synaptosomes with low nanomolar potency1. Indeed, the IC50 value for α-conotoxin PIA of human chimeric α6\/α3\/β2\/β3 nAChRs is 1.7 nM1.Nicotinic acetylcholine receptors containing α6 subunits in the CNS are involved in a variety of physiological functions, and considered to play an important role in cognitive function, motor activity, pain perception, analgesia and the reinforcing properties of nicotine.They are implicated in the pathophysiology and treatment of diseases like chronic Parkinson's, and Alzheimer's1.\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":53073017373037,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STC-870_gr_402.gif?v=1772699888"},{"product_id":"hm1a-toxin-bhp21300229","title":"Hm1a Toxin","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eHm1a 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\u003eNaV1.1, KV2, KV4 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: 3997 Da, Formula: C170H239N47O54S6.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Heteroscodra maculata (Togo starburst tarantula) (Togo starburst baboon spider).\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-Cys16, Cys9-Cys21 and Cys15-Cys28\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\u003eDelta-theraphotoxin-Hm1a (Hm1a) is a peptide toxin originally isolated from Heteroscodra maculate tarantula venom. Initially described as a moderate-affinity KV4.1 blocker¹, later studies confirmed it primarily targets NaV1.1 voltage-gated sodium channels²,3. It interacts with extracellular loops connecting transmembrane segments 1-2 and 3-4 in domain IV voltage sensor of the channel to inhibit NaV1.1 fast inactivation2,3. Hm1a inhibits human NaV1.1 channel inactivation expressed in Xenopus oocytes with EC50 value of 38 ± 6 nM. Recent studies show Hm1a restores interneuron firing in Scn1a+\/- mice, improving inhibition in Dravet Syndrome models⁴. Electrophysiology confirms it prolongs NaV1.1 activation with minimal effects on NaV1.2 and Na­1.6⁵,⁶. NaV1.1 channel is a therapeutic target for brain disorders, such as epilepsy, Alzheimer's disease, and autism. It also contributes to mechanical pain by regulating excitability in a specific subset of sensory neurons within the peripheral nervous system. Hm1a is a valuable tool for neuroscience and pharmacology research⁴-⁷.\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":53073017799021,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STH-600-Hm1a-250nM-on-Nav1.1-in-oocytes_281.jpg?v=1772699892"},{"product_id":"hm1a-toxin-bhp21300231","title":"Hm1a Toxin","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eHm1a 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\u003eNaV1.1, KV2, KV4 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, 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: 3996.4 Da, Formula: C170H240N48O53S6.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Heteroscodra maculata (Togo starburst tarantula) (Togo starburst baboon spider).\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-Cys16, Cys9-Cys21 and Cys15-Cys28 Ser35 - 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\u003eHm1a Toxin (δ-TRTX-Hm1a) is a peptide toxin originally isolated from Heteroscodra maculate tarantula venoM The toxin was originally described as a KV2 and KV4 channel blocker1 but has since been found to be a selective and specific activator of NaV1.1 voltage-gated sodium channels2,3. It interacts with extracellular loops connecting transmembrane segments 1-2 and 3-4 in domain IV voltage sensor of the channel to inhibit NaV1.1 fast inactivation2,3. Hm1a inhibits human NaV1.1 channel inactivation expressed in Xenopus oocytes with EC50 value of 38 ± 6 nMNaV1.1 channel is a therapeutic target for brain disorders, such as epilepsy, Alzheimer's disease, and autisM It also contributes to mechanical pain by regulating excitability in a specific subset of sensory neurons within the peripheral nervous systeM\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\n\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":53073018782061,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STH-601_gr.gif?v=1782151617"},{"product_id":"hm1b-toxin-bhp21300232","title":"Hm1b Toxin","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eHm1b 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\u003eNaV1.1, Nav1.3, Voltage-gated Na+ 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: 3895.4 Da, Formula: C169H241N45O50S6.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Heteroscodra maculata (Togo starburst tarantula) (Togo starburst baboon spider).\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-Cys16, Cys9-Cys21 and Cys15-Cys28\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\u003eδ-theraphotoxin-Hm1b (Hm1b) is a 34 amino acid peptidyl toxin originally isolated from the venom of the tarantula, Heteroscodra maculata1. Hm1b acts as a potent and highly selective activator of the voltage-gated sodium (NaV) 1.1 and NaV1.3 channels. This toxin inhibits the inactivation of the human NaV1.1 channel (expressed in HEK293 cells) with an EC value of 12 nM1,2.The Hm1b toxin has a high level of sequence similarity to the Hm1a toxin, which is also a selective and specific activator of NaV1.1 channels. Both toxins are members of the extended family of inhibitor cystine knot (ICK) peptides with C1-C4, C2-C5, and C3-C6 disulfide architecture. In addition, they share secondary structure characteristics, specifically an antiparallel β hairpin. Despite the high degree of sequence similarity between Hm1a and Hm1b, the latter is much more stable in biological fluids2.NaV channels are involved in a wide array of physiological processes and play a fundamental role in normal neurological function, especially in the initiation and propagation of action potentials. NaV1.1 channel has been utilized as a therapeutic target for various brain disorders, including epilepsy, Alzheimer's disease, and autisM The NaV1.1 channel also contributes to mechanical pain by regulating the excitability of a specific subset of sensory neurons within the peripheral nervous systeM\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":53073019011437,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STH-655-Hm1b-100nM-on-Nav1.1-in-oocytes_979.jpg?v=1772699892"},{"product_id":"jingzhaotoxin-34-bhp21300243","title":"Jingzhaotoxin-34","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eJingzhaotoxin-34\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\u003ehNav1.1 activator, Nav1.7 blocker\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: 4150.8 Da, Formula: C182H258N52O49S6.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao).\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: Cys2-16, Cys9-21 and Cys15-29\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\u003eJingzhaotoxin-34 (JZTX-34) is a 35 amino acid peptidyl toxin, originally isolated from the venom of the Chinese earth tiger tarantula, Chilobrachys guangxiensis1,2.JzTx-34 was reported first as a potent and selective blocker of the voltage-gated sodium (NaV) 1.7 channel and a weak blocker of the Nav1.3 channel3. Recently, it has been found that JzTx-34 has more potent activity as an activator of hNav1.14. In addition, at higher concentrations than hNav1.1, this toxin activated hNav1.3 and hNav1.6 channels and also blocked hNav1.2, hNav1.4, hNav1.5, hNav1.7, and hERG channels4. Moreover, JzTx-34 inhibited voltage-gated potassium (Kv) channels in rat DRG neurons3.Nav channels are transmembrane proteins that control the voltage-dependent increase in sodium permeability. They play a fundamental role in normal neurological function, especially in the initiation and propagation of action potentials. NaV1.1 channel has been utilized as a therapeutic target for various brain disorders, including epilepsy, Alzheimer's disease, and autisM The NaV1.1 channel also contributes to mechanical pain by regulating the excitability of a specific subset of sensory neurons within the peripheral nervous systeM Several studies, including the analysis of mutations associated with an increase or absence of pain sensitivity in humans, have revealed that Nav1.7, Nav1.8, and Nav1.9 are the most important contributors that control nociceptive neuronal electrogenesis5. JZTX-34 exhibited analgesic activity in three rodent pain models3.\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":53073019339117,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STJ-500-Jingzhaotoxin-34-0.5uM-on-Nav1.7-in-oocytes_778.jpg?v=1772699893"},{"product_id":"hm1a-atto-fluor-647n-bhp21300230","title":"Hm1a-ATTO Fluor 647N","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eHm1a-ATTO Fluor 647N\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\u003eNaV1.1, KV2, KV4 channels\u003c\/strong\u003e biology and\/or assay development. The reagent is provided as a ATTO Fluor-647N conjugate, supporting detection or imaging workflows where applicable. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows. Researchers commonly pair it with applications such as Electrophysiology, Live cell imaging, Immunofluorescence, Fluorescence staining, Direct flow cytometry.\u003c\/p\u003e \u003ch2\u003eKey elements and design rationale\u003c\/h2\u003e \u003cul\u003e \u003cli\u003e\n\u003cstrong\u003eMolecular identity:\u003c\/strong\u003e MW: 4625 Da.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Heteroscodra maculata (Togo starburst tarantula) (Togo starburst baboon spider).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eQuality attributes:\u003c\/strong\u003e Bioassay tested: Yes; Sterile \/ endotoxin-free: No.\u003c\/li\u003e \u003c\/ul\u003e \u003ch3\u003eModifications\u003c\/h3\u003e \u003cp\u003eATTO 647N (conjugated via amine group)\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\u003eDelta-theraphotoxin-Hm1a (Hm1a) is a peptide toxin originally isolated from Heteroscodra maculate tarantula venom. Initially described as a moderate-affinity KV4.1 blocker¹, later studies confirmed it primarily targets NaV1.1 voltage-gated sodium channels²,3. It interacts with extracellular loops connecting transmembrane segments 1-2 and 3-4 in domain IV voltage sensor of the channel to inhibit NaV1.1 fast inactivation2,3. Hm1a inhibits human NaV1.1 channel inactivation expressed in Xenopus oocytes with EC50 value of 38 ± 6 nM. Recent studies show Hm1a restores interneuron firing in Scn1a+\/- mice, improving inhibition in Dravet Syndrome models⁴. Electrophysiology confirms it prolongs NaV1.1 activation with minimal effects on NaV1.2 and Na­1.6⁵,⁶. NaV1.1 channel is a therapeutic target for brain disorders, such as epilepsy, Alzheimer's disease, and autism. It also contributes to mechanical pain by regulating excitability in a specific subset of sensory neurons within the peripheral nervous system. Hm1a is a valuable tool for neuroscience and pharmacology research⁴-⁷.\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\n\u003cli\u003eLive cell imaging: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.\u003c\/li\u003e\n\u003cli\u003eImmunofluorescence: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.\u003c\/li\u003e\n\u003cli\u003eFluorescence staining: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.\u003c\/li\u003e\n\u003cli\u003eDirect flow cytometry: 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":53073020060013,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STH-600-FRN_Live-imaging_1_350.png?v=1772699893"},{"product_id":"mu-omega-trtx-tap1a-bhp21300304","title":"µ\/ω-TRTX-Tap1a","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eµ\/ω-TRTX-Tap1a\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\u003eNaV channels and T-type Ca2+ 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: 4182.7 Da, Formula: C174H258N52O55S7.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Theraphosa apophysis (Goliath pinkfoot tarantula) (Pseudotheraphosa apophysis).\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 location: Cys3-Cys18, Cys10-Cys23, Cys17-Cys30\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\u003eµ\/ω-TRTX-Tap1a (Tap1a) is a 35 amino acid peptidyl toxin originally isolated from the venom of the tarantula, Theraphosa apophysis. Tap1a inhibits voltage-gated sodium (NaV) and voltage-gated calcium (CaV)3 channels by inducing a hyperpolarizing shift in both voltage-dependent activation and steady state inactivation1. Tap1a specifically inhibits NaV1.7, NaV1.2, and CaV3.1 with nanomolar potency and NaV1.3, NaV1.6, NaV1.1, and CaV3.2 at low micromolar concentrations1. These ion channels participate in neuron polarization, transmission of somatosensory signals, as well as neuronal cell differentiation, death, and survival. Thus, they are involved in many diseases, including pain disorders, epilepsy, and age-related neurodegeneration.Spider peptides modulate an array of ion channels and receptor proteins. Knottins, which are a subtype of spider peptides, are also referred to as inhibitor cystine knot (ICK) peptides. ICK peptides harbor a disulfide-rich structural motif that forms a \"knot\", which confers high structural, thermal, and proteolytic stability. The modelled structure of Tap1a revealed an ICK fold typical of spider venom peptides, as well as a hydrophobic patch involved in the binding of spider venom peptides to CaV3 and NaV channels1.CaV3 are T-type, low voltage-gated calcium channels. Their electrophysiological properties include low voltage thresholds for activation and inactivation, rapid inactivation, and rebound bursting. These properties are responsible for the CaV3-mediated fine-tuned regulation of neuronal excitability in both the central nervous system (CNS) and peripheral nervous system (PNS)2.CaV3.1 is highly expressed in the brain amygdala, subthalamic nuclei, cerebellum, and thalamus. In contrast, CaV3.1 is only moderately expressed in the heart. CaV3.1 participates in neuron polarization, synaptic transmission, as well as neuronal cell differentiation, death, and survival. CaV3.1 was implicated in the process of age-related neurodegeneration, Parkinson's disease, and Alzheimer's disease3. Moreover, mutations in CaV3.1 have been shown to induce cerebellar ataxia. CaV3.2 channels are expressed in the thalamus where they play a role in the pathophysiology of epilepsy. In addition, the constitutive deletion of the CaV3.2 gene alleviates acute pain, inflammatory pain, and chronic visceral pain in mice4.NaV1.1-1.9 are voltage-gated sodium channels. They open upon depolarization of the membrane and inactivate rapidly before returning to the closed state upon membrane hyperpolarization. The rapid influx of Na+ ions is vital to the generation and propagation of action potential (AP) as well as the transmission of somatosensory signals.NaV1.7 is expressed in the PNS, dorsal root ganglia neurons, visceral sensory neurons, olfactory sensory neurons, trigeminal ganglia, and sympathetic neurons. NaV1.7 gain-of-function mutations have been identified in patients with various pain disorders, such as inherited erythromelalgia (IEM), paroxysmal extreme pain disorder (PEPD), small fiber neuropathy (SFN), and painful diabetic peripheral neuropathy5.NaV1.2 is abundantly expressed at the nodes of Ranvier and in the axon initial segment (AIS) during early development. NaV1.2 plays a dominant role in the initiation and propagation of APs. In mature neurons, NaV1.6 takes the role of AP initiation, and NaV1.2 merely augments APs. Pathogenic variants of NaV1.2 are common causes of neurodevelopmental disorders such as episodic ataxia, schizophrenia, autism spectrum disorder, and intellectual disability with and without seizures6.\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":53073022189933,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STT-600-u-w-TRTX-Tap1a-100nM-on-HEK-Nav1.7_175.jpg?v=1772699896"},{"product_id":"vm24-toxin-bhp21300306","title":"Vm24 Toxin","description":"\u003ch2\u003eOverview\u003c\/h2\u003e \u003cp\u003e\u003cstrong\u003eVm24 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 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 CAS: 1373890-79-9, MW: 3863.6 Da, Formula: C157H253N51O45S9.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSource \/ origin:\u003c\/strong\u003e Vaejovis mexicanus smithi (Mexican scorpion) (Vaejovis smithi).\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: Cys6-Cys26, Cys12-Cys31, Cys16-Cys33, Cys21-Cys36 Cys36- 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\u003eThe Vm24 toxin, also known as Vaejovis mexicanus peptide 24, is a potent blocker of Kv1.3 in human lymphocytes. Isolated from the venom of the Mexican scorpion Vaejovis mexicanus smithi, Vm24 is a 36-residue peptide with a molecular mass of 3864 Da, and has been identified as the first example of a new subfamily of α-type K(+) ion channel blockers (α-KTx 23.1)1.Vm24, a natural immunosuppressive peptide, potently and selectively blocks Kv1.3 in human T cells with high affinity. The blockage of Kv1.3 channels in T cells is a promising therapeutic approach for the treatment of autoimmune diseases such as multiple sclerosis and type 1 diabetes mellitus2.The voltage-gated potassium channel known as Kv1.3 (KCNA3) is expressed by a subset of chronically activated memory T cells and plays an important role in their activation and proliferation, especially in primary malignant T cells. The potent Kv1.3 inhibitor Vm24 inhibits CD3\/CD28-induced proliferation and IL-9 expression, thus inhibiting activation-induced proliferation as well as cytokine and cytokine receptor expression in malignant T cells3.Due to its high specificity, the Vm24 toxin enables to define the downstream functions of Kv1.3 channels in human CD4+ TEM lymphocytes. Blocking Kv1.3 channels profoundly affects the mRNA synthesis machinery, the unfolded protein response and intracellular vesicle transport, impairing the synthesis and secretion of cytokines in response to TCR engagement. This underscores the role of Kv1.3 channels in regulating TEM lymphocyte function4.KV1.3 blockers change the course of Alzheimer's Disease (AD) development, reducing microglial cytotoxic activation and increasing neural stem cell differentiation. KV1.3 blockers inhibit microglia-mediated neurotoxicity in cell cultures, reducing the expression and production of the pro-inflammatory cytokines IL-1β and TNF-α via the NF-kB and p38MAPK pathway. Microglia activation correlates with an increase in KV1.3 channel expression and current density. Several studies highlight the importance of KV1.3 in the activation of the inflammatory response and the inhibition of neural progenitor cell proliferation and neuronal differentiation. Thus, KV1.3 blockers such as Vm24 possess potential therapeutic benefits for patients suffering from Alzheimer's disease5\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":53073024581997,"sku":null,"price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/STV-055-Vm24-amidated-10pM-on-Kv1.3-in-oocytes_805.jpg?v=1772699898"}],"url":"https:\/\/www.ebiohippo.com\/collections\/neuroscience-alzheimer.oembed","provider":"BioHippo","version":"1.0","type":"link"}