Charybdotoxin Chtx - #11CHA001 - CAS : 95751-30-7 Product Information

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Charybdotoxin ChTx - #11CHA001 - CAS : 95751-30-7 Product information 2+ Animal toxins for life-sciences KCa channel blocker www.smartox-biotech.com Charybdotoxin (ChTx) is a 37 amino acid peptide isolated from the venom of the scorpion Leiurus quinquestriatus hebraeus that blocks voltage-gated and large conductance Phone : +33(0) 456 520 869 Ca2+ activated K+ channels K 1.1 in nanomolar concentrations (IC ~ 3 nM). This blockade Fax : +33(0) 456 520 868 Ca 50 [email protected] causes hyperexcitability of the nervous system. The toxin reversibly blocks channel activity by interacting at the external pore of the channel protein with an apparent Kd of Smartox Biotechnology 2.1 nM. ChTX also blocks KCa3.1 (IC50 5 nM), Kv1.2 (IC50 14 nM), Kv1.3 (IC50 2.6 nM) 570 rue de la chimie and Kv1.6 (IC50 2 nM) channels. 38400 Saint Martin d’Hères France Prices 50 µg – 80 € 100 µg – 135 € Technical information 500 µg – 390 € 1 mg – 540 € AA sequence: Pyr-Phe-Thr-Asn-Val-Ser-Cys7-Thr-Thr-Ser-Lys-Glu-Cys13-Trp-Ser-Val-Cys17- 28 33 35 Gln-Arg-Leu-His-Asn-Thr-Ser-Arg-Gly-Lys-Cys -Met-Asn-Lys-Lys-Cys -Arg-Cys -Tyr-Ser- Related products OH Disulfide bridges: Cys7-Cys28, Cys13-Cys33, and Cys17-Cys35 Apamin - #08APA001 Length (aa): 37 Solubility: water and saline buffer Maurotoxin - #08MAR001 Formula: C176H277N57O55S7 CAS number: 95751-30-7 Leiurotoxin-1 - # 10LEI001 Molecular Weight: 4295.90 Da Source: Synthetic Tamapin - # 10TAM001 Appearance: White lyophilized solid Purity rate: > 97 % Iberiotoxin - # 12IBX001 References Gimenez-Gallego G., et al. - Proc. Natl. Acad. Sci. Goldstein SA., Miller C. - Biophys J. Toxin of the month – free sample program Goldstein SA., et al. – Neuron. Each month, Smartox Biotechnology offers a sample of a selected toxin for absolutely free. To be informed, visit our website each Ordering information month, subscribe our newsletter or follow us on social networks. Clic HERE Smartox products are available worldwide. To place an order, please contact us by phone or email or find out your local distributor on our website. We accept credit card payment. Range of blockers Voltage-gated sodium channels Acid-sensing ion channels Voltage-gated calcium channels Chloride channels Potassium channels Nicotinic acetylcholine receptors Voltage-gated potassium channels Purinergic receptors Calcium activated potassium channels TRP channels hERG channel Mechanosensitive ion channels Inward rectifying potassium channels NMDA receptors All products are intended for research use only and are not intended for diagnostic or therapeutic use, not for use in humans Follow us on www.smartox - biotech.com About Smartox .

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Slow Inactivation in Voltage Gated Potassium Channels Is Insensitive to the Binding of Pore Occluding Peptide Toxins
Biophysical Journal Volume 89 August 2005 1009–1019 1009 Slow Inactivation in Voltage Gated Potassium Channels Is Insensitive to the Binding of Pore Occluding Peptide Toxins Carolina Oliva, Vivian Gonza´lez, and David Naranjo Centro de Neurociencias de Valparaı´so, Facultad de Ciencias, Universidad de Valparaı´so, Valparaı´so, Chile ABSTRACT Voltage gated potassium channels open and inactivate in response to changes of the voltage across the membrane. After removal of the fast N-type inactivation, voltage gated Shaker K-channels (Shaker-IR) are still able to inactivate through a poorly understood closure of the ion conduction pore. This, usually slower, inactivation shares with binding of pore occluding peptide toxin two important features: i), both are sensitive to the occupancy of the pore by permeant ions or tetraethylammonium, and ii), both are critically affected by point mutations in the external vestibule. Thus, mutual interference between these two processes is expected. To explore the extent of the conformational change involved in Shaker slow inactivation, we estimated the energetic impact of such interference. We used kÿconotoxin-PVIIA (kÿPVIIA) and charybdotoxin (CTX) peptides that occlude the pore of Shaker K-channels with a simple 1:1 stoichiometry and with kinetics 100-fold faster than that of slow inactivation. Because inactivation appears functionally different between outside-out patches and whole oocytes, we also compared the toxin effect on inactivation with these two techniques. Surprisingly, the rate of macroscopic inactivation and the rate of recovery, regardless of the technique used, were toxin insensitive. We also found that the fraction of inactivated channels at equilibrium remained unchanged at saturating kÿPVIIA.
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Glycine311, a Determinant of Paxilline Block in BK Channels: a Novel Bend in the BK S6 Helix Yu Zhou Washington University School of Medicine in St
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