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商品详细Smartox//12PTB002-00500/0.5mg
Smartox//12PTB002-00500/0.5mg
Smartox//12PTB002-00500/0.5mg
商品编号： 12PTB002-00500
品牌： smartox-biotech
市场价： ¥13104.00
美元价： 10080.00
产地： 美国(厂家直采)
公司：
产品分类： 酸碱缓冲液
公司分类： acid_base_buffer_solution
联系Q Q： 3392242852
电话号码： 4000-520-616
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商品介绍

ProTx-II-Biotin,aselectiveblockerofNav1.7

ProTx-II(Protoxin-II) isatoxinthatwasoriginallyisolatedfromThrixopelmapruriens(Peruviangreenvelvettarantula).ProTx-II inhibitsbothtetrodotoxin-sensitiveandtetrodotoxin-resistant channels. ProTx-II inhibitsactivationbyshiftingthevoltage-dependenceofchannelactivationtomorepositivepotentials. ProTx-II potentlyinhibitsallsodiumchannelsubtypestested(Nav1.2/SCN2A,Nav1.5/SCN5A,Nav1.7/SCN9A,andNav1.8/SCN10A).Itisapproximately15-foldmorepotenton Nav1.7/SCN9A thanonNav1.5/SCN5AchannelsandactsonCav3.1/CACNA1GandinteractsmoreweaklywiththerelatedT-TypechannelCav3.2/CACNA1HbutpotentlyinhibitstheL-typecalciumchannelCav1.2/CACNA1C. ProTx-II alsobindstophospholipids. ProTx-II,aselectiveinhibitorofNav1.7sodiumchannels,blocksactionpotentialpropagationinnociceptors.

ProTx-II-Biotin isaN-terbiotinlabeledversionofthewild-type ProTx-II 

ProTx-II Biotin - Smartox Biotechnology

A,Recordingtracesoftransiently-expressedhumanNav1.7currentinthepresenceofProTxII-Biotin(100nM).Thecurrentwaselicitedbya50ms-depolarizingpulseto-10mVfromaholdingpotentialof-90mV.Inter-sweepperiodwas10s.Currentamplitudeswereplottedagainsttime.Notethattoxin-inducedinhibitionisresistanttowashout,howeveritcanbepartiallyrelievedbydepolarizingthecellmembrane.B,FamiliesofhNav1.7currenttracesincontrolandinthepresenceof100nMProTxII-Biotin.Currentswereevokedbydepolarizingpulsesfrom-60mVto40mV,whilethecellwasholdat-90mV.C,Amplitude-voltagerelationshipsobtainedfromB.

Description:

Productcode:N/A.Category:Sodiumchannels.Tags:Nav1.7,protoxin,prtx,tetrodotoxin,ttx.

AAsequence: Biotin-Tyr-Cys2-Gln-Lys-Trp-Met-Trp-Thr-Cys9-Asp-Ser-Glu-Arg-Lys-Cys15-Cys16-Glu-Gly-Met-Val-Cys21-Arg-Leu-Trp-Cys25-Lys-Lys-Lys-Leu-Trp-OH
Disulfidebonds: Cys2-Cys16,Cys9-Cys21 andCys15-Cys25
Length(aa): 30
Formula: C178H254N48O43S9
MolecularWeight: 4052.74Da
Appearance:Whitelyophilizedsolid
Solubility: waterandsalinebuffer
CASnumber:
Source: Synthetic
Purityrate: >95%

Reference:

EvidenceformultipleeffectsofProTx-IIonactivationgatinginNa(V)1.5
ThepeptidetoxinProTxII,recentlyisolatedfromthevenomofthetarantulaspiderThrixopelmapruriens,modifiesgatinginvoltage-gatedNa+andCa2+channels.ProTxIIisdistinctfromotherknownNa+channelgatingmodifiertoxinsinthatitaffectsactivation,butnotinactivation.Itshiftsactivationgatingpositivelyanddecreasescurrentmagnitudesuchthatthedose-dependenceoftoxinactionmeasuredatasinglepotentialreflectsbotheffects.Totesttheextenttowhichtheseeffectswereindependent,wetrackedseveraldifferentmeasuresofcurrentamplitude,voltage-dependentactivation,andcurrentkineticsinNa(V)1.5inarangeoftoxinconcentrations.ChangesinvoltagedependenceandadecreaseinG(max)appearedatrelativelylowconcentrations(40-100nM)whileapositiveshiftinthevoltagerangeofactivationwasapparentathighertoxinconcentrations(>or=500nM).BecauseProTxIIcarriesanet+4chargewetestedwhetherelectrostaticinteractionscontributedtotoxinaction.WeexaminedtheeffectsofProTxIIinthepresenceofhighextracellularBa2+,knowntoscreenand/orbindtosurfacecharge.Some,butnotallaspectsofProTxIImodificationweresensitivetothepresenceofBa2+indicatingthecontributionofanelectrostatic,surfacecharge-likemechanismandsupportingtheideaofamulti-facetedtoxin-channelinteraction.

EdgertonGB.,etal.(2008)EvidenceformultipleeffectsofProTx-IIonactivationgatinginNa(V)1.5,Toxicon.PMID:18657562

ProTx-IandProTx-II:gatingmodifiersofvoltage-gatedsodiumchannels
ThetarantulavenompeptidesProTx-IandProTx-IIinhibitvoltage-gatedsodiumchannelsbyshiftingtheirvoltagedependenceofactivationtoamorepositivepotential,thusactingbyamechanismsimilartothatofpotassiumchannelgatingmodifierssuchashanatoxinandVSTX1.ProTx-IandProTx-IIinhibitallsodiumchannel(Nav1)subtypestestedwithsimilarpotencyandrepresentthefirstpotentpeptidylinhibitorsofTTX-resistantsodiumchannels.Likegatingmodifiersofpotassiumchannels,ProTx-IandProTx-IIconformtotheinhibitorycystineknotmotif,andProTx-IIwasdemonstratedtobindtosodiumchannelsintheclosedstate.Bothtoxinshavebeensynthesizedchemically,andProTx-II,producedbyrecombinantmeans,hasbeenusedtomaptheinteractionsurfaceofthepeptidewiththeNav1.5channel.Incomparison,beta-scorpiontoxinsactivatesodiumchannelsbyshiftingthevoltagedependenceofactivationtomorenegativepotentials,andtogetherthesepeptidesrepresentvaluabletoolsforexploringthegatingmechanismofsodiumchannels.

PriestBT.,etal.(2007)ProTx-IandProTx-II:gatingmodifiersofvoltage-gatedsodiumchannels,Toxicon.PMID:17087985

Differentialphospholipidbindingbysite3andsite4toxins.ImplicationsforstructuralvariABIlitybetweenvoltage-sensitivesodiumchanneldomains
Ithasbeenshownrecentlythatpolypeptidetoxinsthatmodulatethegatingpropertiesofvoltage-sensitivecationchannelsareabletobindtophospholipidmembranes,leADIngtothesuggestionthatthesetoxinsareabletoaccessachannel-bindingsitethatremainsmembrane-restricted(Lee,S.-Y.,andMacKinnon,R.(2004)Nature430,232-235).WethereforeexaminedtheabilityofanthopleurinB(ApB),aseaanemonetoxinthatselectivelymodifiesinactivationkineticsofNa(V)1.xchannels,andProTx-II,aspidertoxinthatmodifiesactivationkineticsofthesamechannels,tobindtoliposomes.WhereasProTx-IIcanbequantitativelydepletedfromsolutionuponincubationwithphosphatidylcholine/phosphatidylserineliposomes,ApBdisplaysnodiscernIBLephospholipidbindingactivity.Wethereforeexaminedtheactivitiesofstructurallyunrelatedsite3andsite4toxinsderivedfromLeiurusandCentruroidesvenoms,respectively,inthesameassay.LikeApB,thesite3toxinLqqVshowsnolipidbindingactivity,whereasthesite4toxinCentruroidestoxinII,likeProTx-II,iscompletelybound.WeconcludethattoxinsthatmodifyinactivationkineticsviabindingtoNa(V)1.xsite3lacktheabilitytobindphospholipids,whereassite4toxins,whichmodifyactivation,havethisactivity.ThisinherentdifferencesuggeststhattheconformationofdomainIImorecloselyresemblesthatoftheK(V)APchannelthandoestheconformationofdomainIV.

SmithJJ.,etal.(2005)Differentialphospholipidbindingbysite3andsite4toxins.Implicationsforstructuralvariabilitybetweenvoltage-sensitivesodiumchanneldomains,JBiolChem.PMID:15632158

Twotarantulapeptidesinhibitactivationofmultiplesodiumchannels
Twopeptides,ProTx-IandProTx-II,fromthevenomofthetarantulaThrixopelmapruriens,havebeenisolatedandcharacterized.Thesepeptideswerepurifiedonthebasisoftheirabilitytoreversiblyinhibitthetetrodotoxin-resistantNachannel,Na(V)1.8,andareshowntobelongtotheinhibitorycystineknot(ICK)familyofpeptidetoxinsinteractingwithvoltage-gatedionchannels.Thefamilyhasseveralhallmarks:cystinebridgeconnectivity,mechanismofchannelinhibition,andpromiscuityacrosschannelswithinandacrosschannelfamilies.ThecystinebridgeconnectivityofProTx-IIisverysimilartothatofothermembersofthisfamily,i.e.,C(2)toC(16),C(9)toC(21),andC(15)toC(25).Thesepeptidesarethefirsthigh-affinityligandsfortetrodotoxin-resistantperipheralnerveNa(V)channels,butalsoinhibitotherNa(V)channels(IC(50)’s<100nM).ProTx-IandProTx-IIshiftthevoltagedependenceofactivationofNa(V)1.5tomorepositivevoltages,similartoothergating-modifierICKfamilymembers.ProTx-IalsoshiftsthevoltagedependenceofactivationofCa(V)3.1(alpha(1G),T-type,IC(50)=50nM)withoutaffectingthevoltagedependenceofinactivation.Toenablefurtherstructuralandfunctionalstudies,syntheticProTx-IIwasmade;itadoptsthesamestructureandhasthesamefunctionalpropertiesasthenativepeptide.SyntheticProTx-Iwasalsomadeandexhibitsthesamepotencyasthenativepeptide.SyntheticProTx-I,butnotProTx-II,alsoinhibitsK(V)2.1channelswith10-foldlesspotencythanitspotencyonNa(V)channels.ThesepeptidesrepresentnoveltoolsforexploringthegatingmechanismsofseveralNa(V)andCa(V)channels.

MiddletonRE.,etal.(2002)Twotarantulapeptidesinhibitactivationofmultiplesodiumchannels,Biochemistry.PMID:12475222

品牌介绍
Smartox Biotechnology 是全球唯一一家专门生产动物毒液多肽毒素，用于细胞离子通道功能研究的生物医药公司。多肽毒素在生物制药领域具有重要的使用价值。Smartox Biotechnology 于 2009 年由来自 Grenoble 神经科学研究所 (Grenoble Institute of Neuroscience) 的 Michel de waard 博士创立, Smartox Biotechnology 专门研究动物毒液，制作合成多种毒液中的多肽成分（常称为毒素）。 De Waard 博士研究离子通道与毒素多肽的关系，尤其是鉴定、开发毒素多肽作为治疗性分子或细胞穿透肽 (cell penetrating peptides, CPP) 。其研究团队在毒液分离，药理性活性肽鉴定、富半胱氨酸肽定性、制作和优化等方面具有独特、丰富的经验。 2010 年， Smartox Biotechnolgy 被法国研究部 (Ministry of Research) 授予“新兴企业 OSEO 奖 (OSEO prize for emerging businesses) ”。 
公司介绍
Smartox Biotechnology 是全球唯一一家专门生产动物毒液多肽毒素，用于细胞离子通道功能研究的生物医药公司。多肽毒素在生物制药领域具有重要的使用价值。Smartox Biotechnology 于 2009 年由来自 Grenoble 神经科学研究所 (Grenoble Institute of Neuroscience) 的 Michel de waard 博士创立, Smart
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其他 Kv1.3通道 GPCR 机械敏感通道 嘌呤受体 hERG/Kv11.1型 内整流钾通道 NMDA受体 高压门控Ca2 +通道
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