noxiustoxin, Channel blocker of K v1.2;Channel blocker of K v1.3;Channel blocker of K v1.7, CAS No.85205-49-8, Channel blocker of K v1.2;Channel blocker of K v1.3;Channel blocker of K v1.7

CAS: 85205-49-8 Cat. No.: rp174653 PubChem CID: 133082056

GRADE & PURITY Moligand™

Specifications

Product Name

noxiustoxin, Channel blocker of K v1.2;Channel blocker of K v1.3;Channel blocker of K v1.7, CAS No.85205-49-8

Synonymes

NTx | potassium channel toxin α-KTx 2.1 | Toxin II.11

Grade

Moligand™

Spécifications et pureté

Moligand™

Type d'action

CHANNEL BLOCKER

Mécanisme d'action

Channel blocker of K v1.2;Channel blocker of K v1.3;Channel blocker of K v1.7

CAS

85205-49-8

Type de molécule

Peptide

Product Line

Produits biologiques

Stockage et expédition

Conditions de stockage de stockage

Room temperature

Cibles associées (humaines)

KCNA7 Tclin Potassium voltage-gated channel subfamily A member 7 (0 Activities)

Discover Target: KCNA7

Activity Type	Activity Value -log(M)	Mechanism of Action	Activity Reference	Publications (PubMed IDs)

KCNA3 Tclin Potassium voltage-gated channel subfamily A member 3 (0 Activities)

Discover Target: KCNA3

Activity Type	Activity Value -log(M)	Mechanism of Action	Activity Reference	Publications (PubMed IDs)

KCNA2 Tclin Potassium voltage-gated channel subfamily A member 2 (0 Activities)

Discover Target: KCNA2

Activity Type	Activity Value -log(M)	Mechanism of Action	Activity Reference	Publications (PubMed IDs)

Informations génétiques

• Alternate Names: NTx | potassium channel toxin α-KTx 2.1 | Toxin II.11
• Reference:
  • 1. Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration., The Journal of biological chemistry, Steegborn, C C and 7 more authors.
  • 2. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences., Proceedings of the National Academy of Sciences of the United States of America, Strausberg, Robert L RL and 83 more authors.
  • 3. Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH)., Human genetics, Wang, Jian J and Hegele, Robert A RA.
  • 4. Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase., Biochemical and biophysical research communications, Lu, Y Y, O'Dowd, B F BF, Orrego, H H and Israel, Y Y.
  • 5. Single nucleotide polymorphism in CTH associated with variation in plasma homocysteine concentration., Clinical genetics, Wang, J J, Huff, A M AM, Spence, J D JD and Hegele, R A RA.
  • 6. Cystathionine gamma-lyase overexpression inhibits cell proliferation via a H2S-dependent modulation of ERK1/2 phosphorylation and p21Cip/WAK-1., The Journal of biological chemistry, Yang, Guangdong G, Cao, Kun K, Wu, Lingyun L and Wang, Rui R.
  • 7. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)., Genome research, Gerhard, Daniela S DS and 115 more authors.
  • 8. Towards a proteome-scale map of the human protein-protein interaction network., Nature, Rual, Jean-François JF and 37 more authors.
  • 9. The DNA sequence and biological annotation of human chromosome 1., Nature, Gregory, S G SG and 178 more authors.
  • 10. Polymorphisms in one-carbon metabolism and trans-sulfuration pathway genes and susceptibility to bladder cancer., International journal of cancer, Moore, Lee E LE and 14 more authors. more
  • 11. Toward a confocal subcellular atlas of the human proteome., Molecular & cellular proteomics : MCP, Barbe, Laurent L and 10 more authors.
  • 12. Kinetic properties of polymorphic variants and pathogenic mutants in human cystathionine gamma-lyase., Biochemistry, Zhu, Weidong W, Lin, Alexander A and Banerjee, Ruma R.
  • 13. Pathway-based evaluation of 380 candidate genes and lung cancer susceptibility suggests the importance of the cell cycle pathway., Carcinogenesis, Hosgood, H Dean HD and 12 more authors.
  • 14. Relationship between cystathionine gamma-lyase gene polymorphism and essential hypertension in Northern Chinese Han population., Chinese medical journal, Li, Yun Y and 8 more authors.
  • 15. Active cystathionine beta-synthase can be expressed in heme-free systems in the presence of metal-substituted porphyrins or a chemical chaperone., The Journal of biological chemistry, Majtan, Tomas T, Singh, Laishram R LR, Wang, Liqun L, Kruger, Warren D WD and Kraus, Jan P JP.
  • 16. MALDI-TOF MS genotyping of polymorphisms related to 1-carbon metabolism using common and mass-modified terminators., Clinical chemistry, Meyer, Klaus K, Fredriksen, Ase A and Ueland, Per Magne PM.
  • 17. Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S., The Journal of biological chemistry, Sun, Qingxiang Q and 10 more authors.
  • 18. Oral facial clefts and gene polymorphisms in metabolism of folate/one-carbon and vitamin A: a pathway-wide association study., Genetic epidemiology, Boyles, Abee L AL and 16 more authors.
  • 19. Large-scale proteomics and phosphoproteomics of urinary exosomes., Journal of the American Society of Nephrology : JASN, Gonzales, Patricia A PA and 7 more authors.
  • 20. An association study of 45 folate-related genes in spina bifida: Involvement of cubilin (CUBN) and tRNA aspartic acid methyltransferase 1 (TRDMT1)., Birth defects research. Part A, Clinical and molecular teratology, Franke, Barbara B and 7 more authors.
  • 21. Polymorphisms in innate immunity genes and lung cancer risk in Xuanwei, China., Environmental and molecular mutagenesis, Shen, Min M and 12 more authors.
  • 22. H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia., The Journal of biological chemistry, Chiku, Taurai T and 5 more authors.
  • 23. Variations in folate pathway genes are associated with unexplained female infertility., Fertility and sterility, Altmäe, Signe S and 7 more authors.
  • 24. Bile-acid-activated farnesoid X receptor regulates hydrogen sulfide production and hepatic microcirculation., World journal of gastroenterology, Renga, Barbara B, Mencarelli, Andrea A, Migliorati, Marco M, Distrutti, Eleonora E and Fiorucci, Stefano S.
  • 25. Cystathionine gamma-lyase: Clinical, metabolic, genetic, and structural studies., Molecular genetics and metabolism, Kraus, Jan P JP and 14 more authors.
  • 26. Relative contributions of cystathionine beta-synthase and gamma-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions., The Journal of biological chemistry, Singh, Sangita S, Padovani, Dominique D, Leslie, Rachel A RA, Chiku, Taurai T and Banerjee, Ruma R.
  • 27. PTEN identified as important risk factor of chronic obstructive pulmonary disease., Respiratory medicine, Hosgood, H Dean HD, Menashe, Idan I, He, Xingzhou X, Chanock, Stephen S and Lan, Qing Q.
  • 28. Genetic susceptibility to distinct bladder cancer subphenotypes., European urology, Guey, Lin T LT and 18 more authors.
  • 29. Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip., American journal of human genetics, Talmud, Philippa J PJ and 38 more authors.
  • 30. Integrative predictive model of coronary artery calcification in atherosclerosis., Circulation, McGeachie, Michael M and 13 more authors.
  • 31. Cystathionine beta-synthase 844Ins68 polymorphism is not associated with the levels of homocysteine and cysteine in an Indian population., Biomarkers : biochemical indicators of exposure, response, and susceptibility to chemicals, Kumar, Jitender J, Garg, Gaurav G, Karthikeyan, Ganesan G and Sengupta, Shantanu S.
  • 32. The expression and activity of cystathionine-γ-lyase and 3-mercaptopyruvate sulfurtransferase in human neoplastic cell lines., Amino acids, Jurkowska, Halina H, Placha, Wojciech W, Nagahara, Noriuki N and Wróbel, Maria M.
  • 33. Ancient origin of the CTH alelle carrying the c.200C>T (p.T67I) variant in patients with cystathioninuria., Clinical genetics, Espinós, C C and 8 more authors.
  • 34. Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study., Diabetes care, Bailey, Swneke D SD and 11 more authors.
  • 35. Maternal genes and facial clefts in offspring: a comprehensive search for genetic associations in two population-based cleft studies from Scandinavia., PloS one, Jugessur, Astanand A and 12 more authors.
  • 36. [Expression of cystathionine-γ-lyase/hydrogen sulfide pathway in CVB3-induced myocarditis in mice]., Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics, Hua, Wang W and 6 more authors.
  • 37. Folate-metabolizing gene variants and pregnancy outcome of IVF., Reproductive biomedicine online, Laanpere, M M and 5 more authors.
  • 38. Specificity protein-1 as a critical regulator of human cystathionine gamma-lyase in smooth muscle cells., The Journal of biological chemistry, Yang, Guangdong G, Pei, Yanxi Y, Teng, Huajian H, Cao, Qiuhui Q and Wang, Rui R.
  • 39. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium., Briefings in bioinformatics, Gaudet, Pascale P, Livstone, Michael S MS, Lewis, Suzanna E SE and Thomas, Paul D PD.
  • 40. Expression of cystathionine β-synthase and cystathionine γ-lyase in human pregnant myometrium and their roles in the control of uterine contractility., PloS one, You, Xing-Ji XJ and 8 more authors.
  • 41. MicroRNA-21 represses human cystathionine gamma-lyase expression by targeting at specificity protein-1 in smooth muscle cells., Journal of cellular physiology, Yang, Guangdong G, Pei, Yanxi Y, Cao, Qiuhui Q and Wang, Rui R.
  • 42. H2S-Induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response., Science signaling, Krishnan, Navasona N, Fu, Cexiong C, Pappin, Darryl J DJ and Tonks, Nicholas K NK.
  • 43. Characterization of hydrogen sulfide and its synthases, cystathionine β-synthase and cystathionine γ-lyase, in human prostatic tissue and cells., Urology, Guo, Hui H and 5 more authors.
  • 44. Sp1 is involved in regulation of cystathionine γ-lyase gene expression and biological function by PI3K/Akt pathway in human hepatocellular carcinoma cell lines., Cellular signalling, Yin, Peng P and 12 more authors.
  • 45. H₂S protects against pressure overload-induced heart failure via upregulation of endothelial nitric oxide synthase., Circulation, Kondo, Kazuhisa K and 14 more authors.
  • 46. Reduced cystathionine γ-lyase and increased miR-21 expression are associated with increased vascular resistance in growth-restricted pregnancies: hydrogen sulfide as a placental vasodilator., The American journal of pathology, Cindrova-Davies, Tereza T and 5 more authors.
  • 47. Dysregulation of hydrogen sulfide producing enzyme cystathionine γ-lyase contributes to maternal hypertension and placental abnormalities in preeclampsia., Circulation, Wang, Keqing K and 14 more authors.
  • 48. Regulation of cystathionine γ-lyase in mammalian cells by hypoxia., Biochemical genetics, Wang, Maoxian M, Guo, Zhanyun Z and Wang, Shilong S.
  • 49. A genome-wide association study of chemotherapy-induced alopecia in breast cancer patients., Breast cancer research : BCR, Chung, Suyoun S and 6 more authors.
  • 50. [Cystathionine γ-lyase]., Postepy higieny i medycyny doswiadczalnej (Online), Jurkowska, Halina H, Kaczor-Kamińska, Marta M, Bronowicka-Adamska, Patrycja P and Wróbel, Maria M.
  • 51. Decreased cystathionine-γ-lyase (CSE) activity in livers of type 1 diabetic rats and peripheral blood mononuclear cells (PBMC) of type 1 diabetic patients., The Journal of biological chemistry, Manna, Prasenjit P, Gungor, Neslihan N, McVie, Robert R and Jain, Sushil K SK.
  • 52. Hydrogen sulfide (H2S)/cystathionine γ-lyase (CSE) pathway contributes to the proliferation of hepatoma cells., Mutation research, Pan, Yan Y and 5 more authors.
  • 53. The cystathionine γ-lyase/hydrogen sulfide system maintains cellular glutathione status., The Biochemical journal, Lee, Zheng-Wei ZW, Low, Yi-Lian YL, Huang, Shufen S, Wang, Tianxiao T and Deng, Lih-Wen LW.
  • 54. The binding site for the transcription factor, NF-κB, on the cystathionine γ-lyase promoter is critical for LPS-induced cystathionine γ-lyase expression., International journal of molecular medicine, Wang, Maoxian M, Guo, Zhanyun Z and Wang, Shilong S.
  • 55. Regulation of cystathionine gamma-lyase/H₂S system and its pathological implication., Frontiers in bioscience (Landmark edition), Zhao, Kexin K, Li, Hongzhu H, Li, Shuangshuang S and Yang, Guangdong G.
  • 56. Dysregulation of hydrogen sulphide metabolism impairs oviductal transport of embryos., Nature communications, Ning, Nannan N and 5 more authors.
  • 57. Wnt/β-catenin signaling induces the transcription of cystathionine-γ-lyase, a stimulator of tumor in colon cancer., Cellular signalling, Fan, Kun K and 7 more authors.
  • 58. miRNA-30 family inhibition protects against cardiac ischemic injury by regulating cystathionine-γ-lyase expression., Antioxidants & redox signaling, Shen, Yaqi Y and 7 more authors.
  • 59. Role of the cystathionine γ lyase/hydrogen sulfide pathway in human melanoma progression., Pigment cell & melanoma research, Panza, Elisabetta E and 11 more authors.
  • 60. A proteome-scale map of the human interactome network., Cell, Rolland, Thomas T and 69 more authors.
  • 61. Neurodegeneration in Huntington's disease involves loss of cystathionine γ-lyase., Cell cycle (Georgetown, Tex.), Paul, Bindu D BD and Snyder, Solomon H SH.
  • 62. The importance of MTHFR, MTR, MTRR and CSE expression levels in Caucasian women with preeclampsia., European journal of obstetrics, gynecology, and reproductive biology, Seremak-Mrozikiewicz, Agnieszka A and 6 more authors.
  • 63. The importance of rs1021737 and rs482843 polymorphisms of cystathionine gamma-lyase in the etiology of preeclampsia in the Caucasian population., Ginekologia polska, Mrozikiewicz, Przemysław M PM and 8 more authors.
  • 64. Cystathionine γ-lyase, a H2S-generating enzyme, is a GPBAR1-regulated gene and contributes to vasodilation caused by secondary bile acids., American journal of physiology. Heart and circulatory physiology, Renga, Barbara B and 9 more authors.
  • 65. Correlation between the cystathionine-γ-lyase (CES) and the severity of peptic ulcer disease., African health sciences, Chen, Xiong X, Wan, Ying-Chun YC, Guo, Tao T, Xu, Can-Xia CX and Wang, Fen F.
  • 66. MPST but not CSE is the primary regulator of hydrogen sulfide production and function in the coronary artery., American journal of physiology. Heart and circulatory physiology, Kuo, Maggie M MM and 10 more authors.
  • 67. Transcriptional Regulation of Cystathionine-γ-Lyase in Endothelial Cells by NADPH Oxidase 4-Dependent Signaling., The Journal of biological chemistry, Mistry, Rajesh K RK and 8 more authors.
  • 68. LPS Up-Regulates Cystathionine γ -Lyase Gene Expression in Primary Human Macrophages via NF-κB/ERK Pathway., Inflammation & allergy drug targets, Badiei, Alireza A, Gieseg, Steven S, Davies, Sian S, Izani Othman, Mohd M and Bhatia, Madhav M.
  • 69. Radiation Exposure Promotes Hepatocarcinoma Cell Invasion through Epithelial Mesenchymal Transition Mediated by H2S/CSE Pathway., Radiation research, Pan, Yan Y, Zhou, Cuiping C, Yuan, Dexiao D, Zhang, Jianghong J and Shao, Chunlin C.
  • 70. Cystathionine γ-lyase(CSE)/hydrogen sulfide system is regulated by miR-216a and influences cholesterol efflux in macrophages via the PI3K/AKT/ABCA1 pathway., Biochemical and biophysical research communications, Gong, Duo D and 15 more authors.
  • 71. MicroRNA-186 promotes macrophage lipid accumulation and secretion of pro-inflammatory cytokines by targeting cystathionine γ-lyase in THP-1 macrophages., Atherosclerosis, Yao, Yan Y and 9 more authors.
  • 72. Cystathionine γ-lyase is expressed in human atherosclerotic plaque microvessels and is involved in micro-angiogenesis., Scientific reports, van den Born, J C JC and 5 more authors.
  • 73. Dichotomous effects of isomeric secondary amines containing an aromatic nitrile and nitro group on human aortic smooth muscle cells via inhibition of cystathionine-γ-lyase., Biochimie, Ji, Yajing Y and 6 more authors.
  • 74. Distinctive expression pattern of cystathionine-β-synthase and cystathionine-γ-lyase identifies mesenchymal stromal cells transition to mineralizing osteoblasts., Journal of cellular physiology, Gambari, Laura L and 6 more authors.
  • 75. Age-Dependent Allergic Asthma Development and Cystathionine Gamma-Lyase Deficiency., Antioxidants & redox signaling, Wang, Peipei P and 6 more authors.
  • 76. Augmented H2S production via cystathionine-beta-synthase upregulation plays a role in pregnancy-associated uterine vasodilation., Biology of reproduction, Sheibani, Lili L and 7 more authors.
  • 77. Total sulfane sulfur bioavailability reflects ethnic and gender disparities in cardiovascular disease., Redox biology, Rajpal, Saurabh S and 12 more authors.
  • 78. Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides., Gene, Maruyama, K K and Sugano, S S.

Application Protocols

Manufacturer-tested applications and protocols (Product Data only):

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

Because no item-specific protocols are provided, users may consider consulting primary literature and established electrophysiology resources for general procedures involving peptide K+ channel blockers. Any such procedures must be validated and optimized in-house for the intended assay platform.

Biological Roles

General/literature overview (no clinical claims):

• Origin: Noxiustoxin (NTX) is a peptide component of the venom of certain scorpions (literature), belonging to the KTx family of potassium channel toxins.
• Primary biochemical function: Acts as a high-affinity blocker of specific potassium channels by binding to the extracellular vestibule and occluding the pore (literature). This modulates membrane excitability and cellular signaling in excitable tissues.
• Selectivity themes (literature): Many KTx peptides preferentially target subsets of voltage-gated (Kv) and/or Ca2+-activated (KCa) K+ channels. Selectivity is governed by surface charge distribution, key lysine/aromatic residues, and the disulfide-stabilized scaffold.
• Structure–function relationships: The compact, disulfide-rich fold stabilizes the active conformation and positions a critical lysine/tyrosine dyad (or analogous motif) toward the channel selectivity filter (literature). Mutations in either the toxin or channel turret/outer vestibule alter affinity and specificity.
• Experimental utility:
  • Dissects contributions of K+ channel subtypes to action potential waveform, neurotransmitter release, smooth muscle tone, and secretion in vitro.
  • Serves as a probe in binding and footprinting experiments to map extracellular pore architecture.
• Metabolic fate (in vitro): Susceptible to proteolysis by broad-spectrum proteases; stability is markedly higher in serum-free buffers and at low temperature (literature).

Note: Exact target profile, potency (Kd/IC50), and sequence for this catalog item are not specified here; refer to the CoA/Spec Sheet and primary literature for quantitative parameters.

Buffer Applications

Applicability: Highly relevant. Noxiustoxin is typically prepared and used in buffered aqueous media for electrophysiology and biochemical assays.

General/literature guidance for buffer systems:

• Electrophysiology (patch clamp):
  • External (bath) solutions near physiological ionic strength (e.g., ~140 mM NaCl, 2–4 mM KCl, 1–2 mM CaCl2, 1 mM MgCl2, 10 mM HEPES, pH 7.3–7.4). Adjust K+ as required by the channel under study.
  • Internal (pipette) solutions tailored to the recording configuration; toxin is applied extracellularly via bath or fast perfusion.
• Biochemical/biophysical assays:
  • 10–50 mM HEPES or Tris, 100–150 mM NaCl, pH 7.4. Include 0.01–0.1% carrier protein (e.g., BSA) to mitigate adsorption at sub-nanomolar concentrations, if compatible.
  • For surface-based methods (SPR/BLI), use low-detergent running buffers (e.g., 0.005–0.05% Tween-20) and maintain constant ionic strength to stabilize baselines.
• Handling tips:
  • Avoid strong reducing agents (DTT/TCEP) that can cleave disulfide bonds; if reduction is experimentally required, expect loss of native activity.
  • Filter sterilize buffers (0.22 μm) when sterility is necessary; select low protein-binding membranes.

Item-specific buffering recommendations:

• Not specified for this item; refer to CoA/Spec Sheet. Validate final assay buffer composition empirically for potency and stability.

Green Alternatives

Context: Green chemistry considerations for noxiustoxin pertain to its use as a biological probe rather than as a process solvent or bulk reagent.

Opportunities to improve sustainability (general):

• Minimize solvent use: Prepare high-concentration stocks (as solubility allows) to reduce total DMSO volume introduced into assays; promptly dilute into aqueous buffers.
• Aqueous-first approach: Favor water-based buffers at neutral pH; avoid unnecessary organic co-solvents. Validate solubility and stability empirically.
• Recombinant/synthetic sourcing: Where feasible, recombinant expression or solid-phase peptide synthesis with greener coupling strategies (e.g., less hazardous coupling reagents, solvent recycling) can reduce environmental footprint versus venom extraction (literature, general industry trend).
• Waste reduction: Plan experiments to use minimal amounts at effective concentrations. Collect DMSO-containing waste separately for proper disposal.

Comparison (general considerations):

• Metric | Less-green practice | Greener practice
  • Stock solvent | Neat DMSO at large volumes | Minimal DMSO with rapid dilution to aqueous buffer
  • Sterilization | Single-use plastic filters | Reusable low-binding glassware where compatible, or bulk-sterile prep
  • Sourcing | Animal-derived venom extraction | Recombinant/synthetic production with greener protocols

Trade-offs:

• High-purity peptide production may require specialized solvents/reagents; greener methods must still meet stringent purity and activity benchmarks. Always confirm that any process change preserves bioactivity and sequence integrity.

Pharmaceutical Uses

Scope: Research-use only peptide toxin; not for human or veterinary use.

Formulation/industry context (general, non-clinical):

• Reference standard/tool: Utilized as a reference ligand in discovery research to benchmark assay performance or validate target engagement of candidate modulators in vitro.
• Assay controls: Acts as a positive control in ion-channel screening cascades (binding or functional assays) to define dynamic range and assay Z’ factors.
• Stability considerations: For any formulated laboratory standard, excipients (e.g., mannitol, trehalose) may be used to improve lyophilized stability; specifics for this item are not provided and should be verified via CoA.
• Regulatory status: No pharmacopeial monograph or clinical-use designation is implied. Material is supplied for research applications only.

Item-specific pharmaceutical/excipient details:

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

Operational note:

• When qualifying this toxin as an internal control across sites, harmonize solvent, buffer composition, and thaw/aliquot practices to minimize inter-lab variability in apparent potency.

Physical Properties

Item-specific values (from Product Data):

• Appearance: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.

General/literature characteristics for disulfide-rich peptide toxins (context, not specifications):

• State/form: Typically supplied as a lyophilized solid or film; readily forms clear solutions upon reconstitution in water, buffer, or DMSO depending on formulation.
• Solubility (literature): Often soluble in aqueous buffers (neutral pH, low ionic strength) and in polar aprotic solvents (DMSO) at stock concentrations. Solubility can be sequence- and salt-dependent.
• pH stability (literature): Disulfide-stabilized folds usually tolerate near-neutral pH; strongly reducing or highly alkaline conditions can disrupt disulfide bridges and activity.
• Thermal behavior (literature): Enhanced conformational stability versus linear peptides due to disulfides; prolonged exposure to elevated temperatures still risks degradation or aggregation.
• LogP, refractive index, BP/MP: Not typically defined/relevant for peptides; no boiling/melting transitions in the classical sense (decompose on heating).

Notes for end users:

• For exact solubility, extinction coefficient, or peptide content for this specific lot, consult the CoA/Spec Sheet. Empirically confirm working concentration and solvent compatibility prior to critical assays (e.g., manual patch-clamp).

Quality and Grades

Item-specific grade:

• Moligand™ (as provided in Product Data)

What Moligand™ typically signals (general explanation):

• Intended use: Library/screening-grade ligand for discovery research, cheminformatics, and probe development workflows. For research use only.
• Identity/consistency: Typically emphasizes verified identity (e.g., sequence for peptides or structure for small molecules) appropriate for assay development and screening cascades.
• Documentation: Certificate of Analysis (CoA) and/or Spec Sheet generally provides item-specific identity data (e.g., peptide content, purity method), lot number, and handling notes.

Purity and analytical details for this item:

• Purity level, counter-ions, residual solvents/salts, water content, UV cutoff, and metal limits: Not specified for this item; refer to CoA/Spec Sheet.

Implications for use:

• Assay suitability: Moligand™-grade materials are typically suitable for biochemical and biophysical assays (binding, electrophysiology, fluorescence-based readouts) where consistent identity is critical; users should verify activity and potency in their in-house systems.
• Stabilizers/additives: If present, will be declared on the CoA/Spec Sheet. Some peptide toxins may be supplied with volatile salts or small amounts of excipients to aid stability and handling.

Compliance note:

• Not intended for human or veterinary use, clinical diagnostics, or household applications. Utilize according to institutional safety and quality procedures.

Reaction and Applications

Not a synthetic reagent: Noxiustoxin is not typically used as a stoichiometric reagent or catalyst in organic synthesis. Instead, it serves as a bioactive ligand/tool compound.

Research applications (general/literature):

• Ion-channel pharmacology: Employed to probe potassium channel function in patch-clamp experiments (whole-cell, excised patches) and in flux or fluorescence-based assays. Enables dissection of channel subtype contributions by reversible pore blockade.
• Biochemical binding studies: Utilized in radioligand displacement, SPR/BLI, or fluorescence polarization to quantify binding to purified or membrane-embedded channel proteins.
• Structure–activity investigations: Comparative studies with related scorpion toxins or site-directed mutants help map the pharmacophore and channel vestibule residues.
• Physiological pathway mapping: Applied to evaluate roles of specific K+ conductances in neuronal, muscular, or secretory systems in vitro or ex vivo (no clinical/therapeutic use implied).

Practical tips (literature/practice):

• Stock preparation: Prepare concentrated stocks in water or DMSO; aliquot to avoid freeze–thaw (if frozen) and adsorption losses at low concentration.
• Assay controls: Include vehicle controls and, when possible, orthogonal blockers to validate specificity.
• Compatibility: Filter sterilize working solutions (0.22 μm) if sterility is required; avoid filters with high protein-binding membranes.

Item-specific application notes from manufacturer: Not specified for this item; refer to CoA/Spec Sheet.

Reaction Conditions

Interpretation: Here, “reaction conditions” are framed as practical conditions for functional assays and binding experiments rather than chemical reactions.

General/literature guidance for functional assays:

• Concentration ranges: Start with a broad titration (e.g., 0.1 nM to 1 μM) to bracket IC50/Kd values; refine based on literature and preliminary potency in your system.
• Temperature: Perform binding or electrophysiology at 20–25°C for stability and reduced drift; physiological temperature (32–37°C) can be used if required by the model, noting potential changes in kinetics/affinity.
• Equilibration times: Allow sufficient perfusion/association time to reach steady-state block; many peptide–channel interactions equilibrate within seconds to minutes depending on access and flow.
• Buffers: Neutral pH (7.2–7.4), physiological ionic strength. Avoid reducers and proteases. Add 0.01–0.1% carrier protein when working at picomolar–nanomolar concentrations to minimize adsorption.

General/literature guidance for binding assays (SPR/BLI/FP):

• Ligand immobilization: Maintain low densities to mitigate mass transport and rebinding; include surfactant to stabilize baselines.
• Kinetics: Fit association/dissociation phases with appropriate models (1:1 or heterogeneous) mindful of potential secondary sites.

Item-specific tested conditions and expected potencies:

• Not specified for this item; refer to CoA/Spec Sheet and primary literature for channel subtype-specific parameters.

Safety and Handling

GHS/SDS information (item-specific):

• Signal word: Not specified for this item; refer to SDS.
• H-statements/Pictograms/GHS classification: Not specified for this item; refer to SDS.

General safety guidance for bioactive peptide toxins (literature/practice):

• Hazard awareness: Although peptides are non-volatile and have low dermal absorption compared with small lipophilic toxins, noxiustoxin is a biologically active ion-channel modulator. Avoid ingestion, inhalation of powders/aerosols, and skin or eye contact. Treat as acutely bioactive.
• Engineering controls: Work in a clean area; for weighing/reconstitution of dry material, use a fume hood or ventilated enclosure to minimize aerosolization. Avoid generating dust.
• PPE: Lab coat, safety glasses, and disposable nitrile gloves. Double-glove and change outer gloves frequently during handling of dry powder or concentrated stocks.
• Hygiene: Do not pipette by mouth. Wash hands after handling. Decontaminate surfaces with suitable detergents; dispose of consumables as chemical/biological laboratory waste per institutional policy.
• Incompatibilities (general): Strong oxidants/reductants can chemically modify peptide residues or disulfide bonds. Avoid prolonged exposure to high pH, strong reducing agents (e.g., DTT/TCEP unless intended), and proteases.
• First aid (overview): If skin/eye contact occurs, rinse with water for ≥15 minutes and seek medical attention. If inhaled or ingested, seek immediate medical assistance; provide SDS to responders.

Always consult the official SDS for authoritative hazard classification and first-aid measures specific to this product/lot.

Solvent Selection

Applicability: As a peptide toxin, noxiustoxin is used as a biological probe rather than as a solvent or process reagent. Solvent selection here refers to reconstitution and working solutions.

General guidance (literature/practice):

• Primary solvents:
  • Water or physiological buffers (e.g., HEPES, Tris, or phosphate-buffered saline) at pH 7.2–7.4 for biological assays.
  • DMSO can be used to prepare concentrated stock solutions when aqueous solubility is limited; dilute into buffer immediately before use to minimize DMSO exposure to cells/patches.
• Additives: 0.1% carrier protein (e.g., BSA) or 0.05–0.1% nonionic detergents may reduce adsorption losses at low nanomolar concentrations (literature). Verify that additives do not interfere with readouts.
• Avoid: Strongly reducing buffers (DTT/TCEP) unless intentionally modifying disulfides; high-pH carbonate buffers that can promote deamidation; high chloride if studying Cl−-sensitive systems.

Polarity/miscibility context (literature):

• Peptide toxins are hydrophilic and generally prefer aqueous media; DMSO is miscible with water and commonly used as a co-solvent for concentrated stocks.

When to choose alternatives:

• If non-specific binding or instability is observed, consider buffers with defined ionic strength (e.g., 140 mM NaCl) and mild chelators (e.g., 1 mM EGTA) appropriate for the electrophysiology configuration. For long incubations, include antioxidants-free formulations to preserve disulfide integrity.

Storage and Reconstitution

Item-specific storage (from Product Data):

• Storage condition: Room temperature
• Shipped in: Not specified for this item; refer to CoA/Spec Sheet.

Item-specific reconstitution details:

• Reconstitution solvent, concentration, and stabilizers: Not specified for this item; refer to CoA/Spec Sheet.

General guidance (literature/practice; verify against CoA for this lot):

• Upon receipt: If supplied lyophilized, store as indicated until first use. After opening/reconstitution, aliquot into low-binding tubes to avoid repeated freeze–thaw and adsorption losses.
• Solvents: Reconstitute in sterile water or assay buffer at neutral pH. If needed, prepare a concentrated DMSO stock and dilute into buffer immediately prior to use.
• Working stocks: Prepare single-use aliquots at convenient concentrations (e.g., 10–100× final assay concentration). Keep on ice during use and avoid prolonged room-temperature exposure.
• Storage of solutions: If freezing is compatible with the specific formulation, store aliquots at −20 to −80°C. Avoid multiple freeze–thaw cycles. Discard if turbidity, precipitation, or loss of activity is observed.

Always prioritize the CoA/Spec Sheet for item-specific instructions and stability information.

Structure and Identity

Brief description: noxiustoxin (NTX) is a scorpion-venom peptide toxin widely used as a pharmacological tool in ion-channel research.

Item-specific identifiers (from Product Data):

• SKU: rp174653
• CAS: 85205-49-8
• PubChem CID: 133082056
• Grade: Moligand™
• Storage (as provided): Room temperature
• SMILES: Not specified for this item; refer to CoA/Spec Sheet.
• InChIKey: Not specified for this item; refer to CoA/Spec Sheet.

Structure (general/literature description):

• Chemical class: Disulfide-rich peptide toxin (scorpion α/β-KTx family, literature)
• Backbone: Short polypeptide (~30–40 amino acids, literature), typically featuring a compact cystine-stabilized fold with multiple disulfide bridges that confer high stability.
• Functional features: Multiple basic residues and a defined surface pharmacophore that engages extracellular vestibules of K+ channels (literature). No defined stereocenters beyond the L-configuration of constituent amino acids (literature).

2D structural description in words (literature):

• A single polypeptide chain forming a compact, disulfide-crosslinked core. Side chains present a clustered basic patch (Lys/Arg) and hydrophobic/aromatic residues that facilitate high-affinity binding to voltage-gated or Ca2+-activated K+ channel pores.

Molecular formula and molecular weight:

• Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight: Not specified for this item; refer to CoA/Spec Sheet. (Peptide toxins of this class commonly fall in the 3–5 kDa range, literature).

Synthetic Utility

Not typically applicable. Noxiustoxin is a bioactive peptide tool compound rather than a building block or reagent for chemical synthesis.

General peptide chemistry context (literature):

• SPPS and folding: If preparing analogs, solid-phase peptide synthesis followed by oxidative folding yields the disulfide-stabilized scaffold. Side-chain protection and folding conditions control disulfide pairing.
• Mutagenesis and SAR: Alanine scanning, conservative substitutions, or backbone cyclization are common to probe structure–activity relationships and enhance stability.

For end users purchasing this catalog item:

• There is no conventional “synthetic transformation” use case. Focus on sections: Biological Roles, Buffer Applications, Reaction & Applications, and Reaction Conditions (assay conditions) for practical guidance.

Target Specificity

Item-specific, from Product Data only:

• Antigen/Target name(s): Not specified for this item; refer to CoA/Spec Sheet.
• Epitope/binding site: Not specified for this item; refer to CoA/Spec Sheet.
• Species reactivity / channel subtypes: Not specified for this item; refer to CoA/Spec Sheet.
• Affinity/IC50/Kd: Not specified for this item; refer to CoA/Spec Sheet.

Note: While scorpion peptide toxins often target subsets of K+ channels (literature), Aladdin provides no item-specific target profile here. Users should consult the CoA and validate specificity in their assay system.

Foire aux questions

What is Moligand??

Moligand? is one of Aladdin Scientific's premium product lines, formulated for high-purity applications across multiple workflows. Compared to standard grades in the same workflow, Moligand? products typically offer tighter specifications, more rigorous QC, and stronger lot-to-lot consistency.

How should this product be stored?

Store at room temperature.

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

The CAS Number is 85205-49-8.

What documentation is provided?

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