4000-520-616
欢迎来到免疫在线！(蚂蚁淘生物旗下平台)  请登录 |  免费注册 |  询价篮
产品库 品牌馆 现货促销 技术交流 新闻动态 联系我们
smartox-biotech
主营：主营：动物毒液多肽毒素
咨询热线电话
4000-520-616
公司首页 公司介绍 产品中心 新闻动态 联系方式 在线下单
当前位置： 首页 > 产品中心 > acid_base_buffer_solution > Smartox/电压门控钠通道强效阻断剂/12HTX001-01000/1mg
商品详细Smartox/电压门控钠通道强效阻断剂/12HTX001-01000/1mg
Smartox/电压门控钠通道强效阻断剂/12HTX001-01000/1mg
Smartox/电压门控钠通道强效阻断剂/12HTX001-01000/1mg
商品编号： 12HTX001-01000
品牌： smartox-biotech
市场价： ¥11856.00
美元价： 9120.00
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
电子邮箱： info@ebiomall.com
立即询价
商品介绍

Hainantoxin-IV(HNTX-IV)isapeptidethatwasoriginallyisolatedfromthevenomoftheChinesebirdspiderOrnithoctonushainanaLiang(SelenocosmiahainanaLiang).IthasbeenreportedthatthispeptideisapotentantagoNISToftetrodotoxin-sensitive(TTX-S)voltage-gatedsodiumchannels(VGSCs).Hainantoxin-IVbindstoTTX-SwithanIC50valueof34nMinadultratdorsalrootganglion(DRG)neurons.Tetrodotoxin-resistant(TTX-R)voltage-gatedsodiumchannelsarenotaffectedbyHainantoxin-IV.Itprobablyinteractswiththesite1throughamechanismquitesimilartothatofTTXwithoutaffectingtheactivationandinactivationkinetics.


Description:

Productcode:N/A.Category:Sodiumchannels.Tags:nav,tetrodotoxin,ttx.

AAsequence:Glu-Cys2-Leu-Gly-Phe-Gly-Lys-Gly-Cys9-Asn-Pro-Ser-Asn-Asp-Gln-Cys16-Cys17-Lys-Ser-Ser-Asn-Leu-Val-Cys24-Ser-Arg-Lys-His-Arg-Trp-Cys31-Lys-Tyr-Glu-Ile-NH2
(DisulfidebondsbetweenCys2-Cys17,Cys9-Cys24,andCys16-Cys31)
Length(aa):35
Formula:C166H257N53O50S6
MolecularWeight:3987.6Da
Appearance:Whitelyophilizedsolid
Solubility:waterandsalinebuffer
CASnumber:Notavailable
Source:Synthetic
Purityrate:>97%

Reference:

Apositivelychargedsurfacepatchisimportantforhainantoxin-IVbindingtovoltage-gatedsodiumchannels
Hainantoxin-IV(HNTX-IV),isolatedfromthevenomofthespiderOrnithoctonushainana,isaspecificantagonistoftetrodotoxin-sensitive(TTX-S)voltage-gatedsodiumchannelsinratdorsalrootganglion(DRG)cells.Itadoptsaninhibitorcystineknotmotif,andstructuralanalysisrevealedapositivelychargedpatchconsistingofArg26,Lys27,His28,Arg29andLys32distributedonitsmolecularsurface.OurpreviousstudydemonstratedthatLys27andArg29butnotArg26werecriticalresiduesforHNTX-IVbindingtoTTX-Ssodiumchannels.Inthepresentstudy,weexaminedtherolesofHis28andLys32intheinteractionofHNTX-IVwithitstarget.Twomutants,HNTX-IV-H28DandHNTX-IV-K32A,weregeneratedbysolid-phasechemicalsynthesisandpurifiedbyreverse-phaseHPLCafterrefoldingandoxidation,yieldingtwocompoundsofhighpuritywithmonoisotopicmassesof3962.66and3927.70 Da,respectively,asdeterminedbyMALDI-TOFmassspectrometry.Thisindicatedthepresenceofsixcysteineresiduesformingthreedisulfidebonds.Moreover,circulardichroismspectroscopyanalysisdemonstratedthatthesubstitutionofHis28orLys32didnotaffecttheoverallstructureofHNTX-IV.TheinhibitoryactivityofHNTX-IV-H28DandHNTX-IV-K32AagainstTTX-SsodiumchannelsinratDRGcellswasanalyzedbywhole-cellpatch-clamptechnique.TheIC(50)valuesforthemutantswere0.57and5.80 μM(17-foldand170-foldlowerthantheactivityofthenativetoxin),indicatingthatHis28andLys32maybeimportantfortheinhibitoryactivityofHNTX-IV.Takentogether,ourresultssuggestthatthepositivelychargedpatchmightbethebindingsitefortheinteractionofHNTX-IVwithTTX-Ssodiumchannels.ThesefindingsmightcontributetotheelucidationofthestructureandfunctionrelationshipofHNTX-IV.

LiuY,etal.(2012)Apositivelychargedsurfacepatchisimportantforhainantoxin-IVbindingtovoltage-gatedsodiumchannels.JPeptSci.PMID:22927181

Structure--activityrelationshipsofhainantoxin-IVandstructuredeterminationofactiveandinactivesodiumchannelblockers.
Hainantoxin-IV(HNTX-IV)canspecificallyinhibittheneuronaltetrodotoxin-sensitivesodiumchannelsanddefinesanewclassofdepressantspidertoxin.ThesequenceofnativeHNTX-IVisECLGFGKGCNPSNDQCCKSSNLVCSRKHRWCKYEI-NH(2).Inthepresentstudy,toobtainfurtherinsightintotheprimaryandtertiarystructuralrequirementsofneuronalsodiumchannelblockers,wedeterminedthesolutionstructureofHNTX-IVasatypicalinhibitorcystineknotmotifandsynthesizedfourmutantsdesignedbasedonthepredictedsitesfollowedbystructuralelucidationoftwoinactivemutants.PharmacologicalstudiesindicatedthattheS12AandR26AmutantshadactivitiesnearthatofnativeHNTX-IV,whileK27AandR29Ademonstratedactivitiesreducedby2ordersofmagnitude.(1)HMRanalysisshowedthesimilarmolecularconformationsfornativeHNTX-IVandfoursyntheticmutants.FurThermore,inthedeterminedstructuresofK27AandR29A,thesidechainsofresidues27and29werelocatedintheidenticalspatialpositiontothoseofnativeHNTX-IV.TheseresultssuggestedthatresiduesSer(12),Arg(26),Lys(27),andArg(29)werenotresponsIBLeforstABIlizingthedistinctconformationofHNTX-IV,butLys(27)andArg(29)werecriticalforthebioactivities.ThepotencyreductionsproducedbyAlasubstitutionswereprimarilyduetothedirectinteractionoftheessentialresiduesLys(27)andArg(29)withsodiumchannelsratherthantoaconformationalchange.Aftercomparisonofthesestructuresandactivitieswithcorrelatedtoxins,wehypothesizedthatresiduesLys(27),Arg(29),His(28),Lys(32),Phe(5),andTrp(30)clusteredononefaceofHNTX-IVwereresponsibleforligandbinding.

LiD,etal.(2004)Structure–activityrelationshipsofhainantoxin-IVandstructuredeterminationofactiveandinactivesodiumchannelblockers.JBiolChem.PMID:15201273

Isolationandcharacterizationofhainantoxin-IV,anovelantagonistoftetrodotoxin-sensitivesodiumchannelsfromtheChinesebirdspiderSelenocosmiahainana.

Aneurotoxin,namedhainantoxin-IV,waspurifiedfromthevenomofthespiderSelenocosmiahainana.TheaminoacidsequencewasdeterminedbyEdmandegradation,revealingittobea35-residuepolypeptideamidatedatitsCterminalandincludingthreedisulfidebridges:Cys2-Cys17,Cys9-Cys24,andCys16-Cys31assignedbypartialreductionandsequenceanalysis.Hainantoxin-IVshares80%sequenceidentitywithhuwentoxin-IVfromthespiderS.huwena,apotentantagonistthatactsatsite1ontetrodotoxin-sensitive(TTX-S)sodiumchannels,suggestingthathainantoxin-IVadoptsaninhibitorcystineknotstructuralmotiflikehuwentoin-IV.Underwhole-cellvoltage-clampconditions,thistoxinhasnoeffectontetrodotoxin-resistantvoltage-gatedsodiumchannelsinadultratdorsalrootganglionneurons,whileitblocksTTX-Ssodiumchannelsinamannersimilartohuwentoxin-IV,andtheactionsofbothtoxinsonsodiumcurrentsareverysimilartothatoftetrodotoxin.Thus,theydefineanewfamilyofspidertoxinsaffectingsodiumchannels.

LiuZ,etal.(2003)Isolationandcharacterizationofhainantoxin-IV,anovelantagonistoftetrodotoxin-sensitivesodiumchannelsfromtheChinesebirdspiderSelenocosmiahainana.CellMolLifeSci.PMID:12827284

Inhibitionofneuronaltetrodotoxin-sensitiveNa+channelsbytwospidertoxins:hainantoxin-IIIandhainantoxin-IV.

Hainantoxin-IIIandhainantoxin-IV,isolatedfromthevenomoftheChinesebirdspiderSeleconosmiahainana,areneurotoxicpeptidescomposedof33-35residueswiththreedisulfidebonds.Usingwhole-cellpatch-clamptechnique,weinvestigatedtheiractiononionicchannelsofadultratdorsalrootganglionneurons.ItwasfoundthatthetwotoxinsdidnotaffectCa2+channels(bothhighvoltageactivatedandlowvoltageactivatedtypes)nortetrodotoxin-resistantvoltage-gatedNa+channels(VGSCs).However,hainantoxin-IIIandhainantoxin-IVstronglydepressedtheamplitudeoftetrodotoxin-sensitiveNa+currentswithIC50valuesof1.1and44.6nM,respectively.Bothhainantoxin-III(1nM)andhainantoxin-IV(50nM)causedahyperpolarizingshiftofabout10mVinthevoltagemidpointofsteady-stateNa+channelinactivation,buttheyshoweddifferenceinthereprimekineticsofVGSCs:hainantoxin-IIIsignificantlydecreasedtherecoveryratefrominactivationataprepulsepotentialof-80mVwhilehainantoxin-IVdidnotdo.Itisinterestingtonotethatsimilartohuwentoxin-IV,thetwohainantoxinsdidnotaffecttheactivationandinactivationkineticsofNa+currentsandataconcentrationof1microMtheycompletelyinhibitedtheslowinginactivationcurrentsinducedbyBMK-I(toxinIfromthescorpionButhusmartensiKarsch),ascorpionalpha-liketoxin.Theresultsindicatethathainantoxin-IIIandhainantoxin-IVarenovelspidertoxinsandaffectthemammalneuralNa+channelsthroughamechanismquitedifferentfromotherspidertoxinstargetingtheneuralreceptorsite3,suchasdelta-aractoxinsandmu-agatoxins.

XiaoY,etal.(2003)Inhibitionofneuronaltetrodotoxin-sensitiveNa+channelsbytwospidertoxins:hainantoxin-IIIandhainantoxin-IV.EurJPharmacol.PMID:14512091

Determinationofdisulfidebridgesoftwospidertoxins:Hainantoxin-IIIandHainantoxin-IV

Peptidetoxinsareusuallyhighlybridgedproteinswithmultipairsofintrachaindisulfidebonds.Analysisofdisulfideconnectivityisanimportantfacetofproteinstructuredetermination.Inthispaper,wesuccessfullyassignedthedisulfidelinkageoftwonovelpeptidetoxins,calledHNTX-IIIandHNTX-IV,isolatedfromthevenomofOrnithoctonushainanaspider.BothpeptidesareusefulinhibitorsofTTX-sensitivevoltage-gatedsodiumchannelsandarecomposedofsixcysteineresiduesthatformthreedisulfidebonds,respectively.Firstly,thepeptideswerepartiallyreducedbytris(2-carboxyethyl)-phosphine(TCEP)in0.1Mcitratebuffercontaining6Mguanidine-HClat40°Cfortenminutes.Subsequently,thepartiallyreducedintermediatescontainingfreethiolswereseparatedbyreversed-phasehigh-performanceliquidchromatography(RP-HPLC)andalkylatedbyrapidcarboxamidomethylation.Then,thedisulfidebondsoftheintermediateswereanalyzedbyEdmandegradation.Byusingthestrategyabove,disulfidelinkagesofHNTX-IIIandHNTX-IVweredeterminedasI-IV,II-VandIII-VIpattern.Inaddition,thisstudyalsoshowedthatthismethodmayhaveagreatpotentialfordeterminingthedisulfidebondsofspiderpeptidetoxins.

WangW.,etal.(2009)Determinationofdisulfidebridgesoftwospidertoxins:Hainantoxin-IIIandHainantoxin-IV.JVenomAnimToxinsinclTropDis.

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
品牌分类
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
显示分类
联络我们
服务热线：4000-520-616
（限工作日9:00-18:00）
QQ ：1570468124
手机：18915418616
快速导航：
总部地址：
江苏省苏州市工业园区星湖街218号 苏州生物医药产业园一期（生物纳米园）A4-216(邮编：215125)
工作时间：周一至周五9:00~18:00
技术支持：
短信：18915418616
服务热线：
4000-520-616（全国）
☏  0512-67156496（苏州）
版权信息：
©  2015-2022 苏州蚂蚁淘生物科技有限公司 版权所有 中国
网站备案：
友情链接：
免责声明：
本站有部分内容来自互联网，如无意中侵犯了某个媒体 、公司 、企业或个人等的知识产权，请来电或致函告之，
本网站将在规定时间内给予删除等相关处理。
扫描二维码关注官方微信
获取最新促销及产品信息