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蚂蚁淘在线 / 品牌中心 / Smartox / Smartox/K_Ca²⁺ channel blocker/11CHA001-00500/0.5mg

Smartox/K_Ca²⁺ channel blocker/11CHA001-00500/0.5mg

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￥4867.20

货号：11CHA001-00500

浏览量：127

品牌：Smartox

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商品描述

CharyBDotoxin(ChTx) isa37aminoacidpeptideisolatedfromthevenomofthe scorpionLeiurusquinquestriatushebraeus thatblocks voltage-gatedandlargeconductanceCa²⁺activatedK⁺ channels K_Ca1.1 innanomolarconcentrations(IC₅₀~3nM).ThisblockadecauseshyperexcitABIlityofthenervoussystem.ThetoxinreversIBLyblockschannelactivitybyinteractingattheexternalporeofthechannelproteinwithanapparentKdof2.1nM.ChTXalsoblocksK_Ca3.1 (IC₅₀ 5nM), K_v1.2 (IC₅₀ 14nM), K_v1.3 (IC₅₀ 2.6nM)and K_v1.6 (IC₅₀2nM)channels.

Description:

Productcode:N/A.Categories:KCachannels,Kvchannels,Potassiumchannels.Tags:95751-30-7,kv,SK.

AAsequence:Pyr-Phe-Thr-Asn-Val-Ser-Cys⁷-Thr-Thr-Ser-Lys-Glu-Cys¹³-Trp-Ser-Val-Cys¹⁷-Gln-Arg-Leu-His-Asn-Thr-Ser-Arg-Gly-Lys-Cys²⁸-Met-Asn-Lys-Lys-Cys³³-Arg-Cys³⁵-Tyr-Ser-OH
(DisulfidebondsbetweenCys⁷-Cys²⁸,Cys¹³-Cys³³,andCys¹⁷-Cys³⁵)
Length(aa): 37
Formula: C₁₇₆H₂₇₇N₅₇O₅₅S₇
MolecularWeight: 4295.90Da
Appearance: Whitelyophilizedsolid
Solubility: waterandsalinebuffer
CASnumber: 95751-30-7
Source: Synthetic
Purityrate: >97%

Reference:

Purification,sequence,andmodelstructureofcharybdotoxin,apotentselectiveinhibitorofcalcium-activatedpotassiumchannels.

Charybdotoxin(ChTX),aproteinpresentinthevenomofthescorpionLeiurusquinquestriatusvar.hebraeus,hasbeenpurifiedtohomogeneitybyacombinationofion-exchangeandreversed-phasechromatography.Polyacrylamidegelelectrophoresis,aminoacidanalysis,andcompleteaminoacidsequencedeterminationofthepureproteinrevealthatitconsistsofasinglepolypeptidechainof4.3kDa.PurifiedChTXisapotentandselectiveinhibitoroftheapproximately220-pSCa2+-activatedK+channelpresentinGH3anteriorpituitarycellsandprimarybovineaorticsmoothmusclecells.ThetoxinreversiblyblockschannelactivitybyinteractingattheexternalporeofthechannelproteinwithanapparentKdof2.1nM.TheprimarystructureofChTXissimilartoanumberofneurotoxinsofdiverseorigin,whichsuggeststhatChTXisamemberofasuperfamilyofproteinsthatmodifyion-channelactivities.Onthebasisofthissimilarity,thethree-dimensionalstructureofChTXhasbeenmodeledfromtheknowncrystalstructureofalpha-bungarotoxin.ThesestudiesindicatethatChTXisusefulasaprobeofCa2+-activatedK+-channelfunctionandsuggestthattheproposedtertiarystructureofChTXmayprovideinsightintothemechanismofchannelblock.

Gimenez-GallegoG.,etal.(1988)Purification,sequence,andmodelstructureofcharybdotoxin,apotentselectiveinhibitorofcalcium-activatedpotassiumchannels.Proc.Natl.Acad.Sci.U.S.A.PMID:2453055

Mechanismofcharybdotoxinblockofavoltage-gatedK+channel.

CharybdotoxinblockofaShakerK+channelwasstudiedinXenopusoocytemacropatches.Toxinonrateincreaseslinearlywithtoxinconcentrationinanionicstrength-dependentfashionandiscompetitivelydiminishedbytetraethylammonium.OnrateisinsensitivetotransmembranevoltageandtoK+ontheoppositesideofthemembrane.Conversely,toxinoffrateisinsensitivetotoxinconcentration,ionicstrength,andaddedtetraethylammoniumbutisenhancedbymembranedepolarizationorK+(orNa+)inthetranssolution.ChargeneutralizationofcharybdotoxinLys27,however,rendersoffratevoltageinsensitive.Ourresultsarguethatblockofvoltage-gatedK+channelsresultsfromthebindingofonetoxinmolecule,sothatLys27enterstheporeandinteractswithK+(orNa+)intheionconductionpathway.

GoldsteinSA,MillerC.(1993)Mechanismofcharybdotoxinblockofavoltage-gatedK+channel.BiophysJ.PMID:7506068

ThecharybdotoxinreceptorofaShakerK+channel:peptideandchannelresiduesmediatingmolecularrecognition.

Charybdotoxin(CTX)isapeptideofknownstructurethatinhibitsShakerK+channelsbyapore-blockingmechanism.Pointmutagenesisofall30solvent-exposedresiduesidentifiedthepartoftheCTXmolecularsurfacemakingcontactwiththereceptorintheK+channel.Allclose-contactresiduesareclusteredinawell-definedinteractionsurface;theshapeofthissurfaceimpliesthattheouteropeningoftheShakerchannelconductionporeabruptlywidenstoa25x35Aplateau.AmutagenicscanoftheS5-S6linkersequenceoftheShakerK+channelidentifiedthosechannelresiduesinfluencingCTXbindingaffinity.TheShakerresiduesmakingthestrongestcontributiontotoxinbindingarelocatedclosetothepore-liningsequence,andmoredistantresiduesonbothsidesofthisregioninfluenceCTXbindingweakly,probablybyanelectrostaticmechanism.ComplementarymutagenesisofbothCTXandShakersuggeststhatShaker-F425contactsaspecificareanearT8andT9ontheCTXmolecularsurface.ThiscontactpointconstrainsShaker-F425tobelocatedata20ArADIaldistancefromtheporeaxisand10-15Aabovethe“floor”oftheCTXreceptor.

GoldsteinSA,etal.(1994)ThecharybdotoxinreceptorofaShakerK+channel:peptideandchannelresiduesmediatingmolecularrecognition.Neuron.PMID:7516689

Smartox生物素ProTx-I电压门控钠通道和T型Cav的阻断剂毒素I（ProTx-1；β-theraphotoxin-Tp1a）是一种毒素，最初是从Prixopelma pruriens（秘鲁绿色天鹅绒狼蛛）的毒液中分离出来的。此毒素可逆地抑制抗河豚毒素（TTX）的通道 Na v 1.8（IC 50 = 27 nM）和 Na v 1.2，Na v 1.5和Na v 1.7 ，IC 50 值为50至100 nM。此外， ProTx-I 改变了T型Ca v 3.1通道的电压依赖性活动（IC 50 = 50 nM），而不会影响灭活的电压依赖性。生物素ProTx-I是ProTx-I的生物素标签版本。

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