ω-conotoxin-GVIA(omegaconotoxinGVIA)isaconotoxinthathhasbeenisolatedfromthevenomoftheconeConusgeographus. ω-conotoxinGVIA actsatpresynapticmembranes.Itbindsandblocksspecifically voltage-dependentN-typeCa2+channels Cav2.2channel withanED50 of68pM.
Description:
AAsequence: H-Cys1-Lys-Ser-Hyp-Gly-Ser-Ser-Cys8-Ser-Hyp-Thr-Ser-Tyr-Asn-Cys15-Cys16-Arg-Ser-Cys19-Asn-Hyp-Tyr-Thr-Lys-Arg-Cys26-Tyr-NH2
Hyp:hydroxyproline
(DisulfidebondsbetweenCys1-Cys16,Cys8-Cys19 andCys15-Cys26)
Length(aa): 27
Formula: C120H182N38O43S6
MolecularWeight: 3036.05Da
Appearance: Whitelyophilizedsolid
Solubility: waterandsalinebuffer
CASnumber: [106375-28-4]Source: Synthetic
Purityrate: >95%
Reference:
Structure-functionrelationshipsofomega-conotoxinGVIA.Synthesis,structure,calciumchannelbinding,andfunctionalassayofalanine-substitutedanalogues
Thestructure-functionrelationshipsoftheN-typecalciumchannelblocker,omega-conotoxinGVIA(GVIA),havebeenelucidatedbystructural,binding&invitro&invivofunctionalstudiesofalanine-substitutedanaloguesofthenativemolecule.Alaninewassubstitutedatallnon-bridgingpositionsinthesequence.Inmostcasesthestructureoftheanaloguesinaqueoussolutionwasshowntobenative-likeby1HNMRspectroscopy.Minorconformationalchangesobservedinsomecaseswerecharacterizedbytwo-dimensionalNMR.ReplacementofLys2&Tyr13withAlacausedreductionsinpotencyofmorethan2ordersofmagnitudeinthreefunctionalassays(sympatheticnervestimulationofratisolatedvasdeferens,rightatrium&mesentericartery)&aratbrainmembranebindingassay.ReplacementofseveralotherresidueswithAla(particularlyArg17,Tyr22&Lys24)resultedinsignificantreductionsinpotency(<100-fold)inthefunctionalassays,butnotthebindingassay.Thepotenciesoftheanalogueswerestronglycorrelatedbetweenthedifferentfunctionalassaysbutnotbetweenthefunctionalassays&thebindingassay.Thus,thephysiologicallyrelevantassaysemployedinthisstudyhaveshownthatthehighaffinityofGVIAfortheN-typecalciumchannelistheresultofinteractionsbetweenthechannelbindingsite&thetoxinatmoresitesthanthepreviouslyidentifiedLys2&Tyr13.
CharacteristicsofOmega-conotoxinGVIAandMVIICBindingtoCav2.1andCav2.2ChannelsCapturedbyAnti-Ca2+ChannelPeptideAntibodies
N-typecalciumchannelblockers:noveltherapeuticsforthetreatmentofpain
ebiomall.com
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常用流动相加酸碱后PH的总结,希望大家能够提供一点自己测过的结果,谢谢先
1.直接用固体磷酸钠配制成50mM的磷酸钠溶液,再调pH到7.4;(我们试着用这个做了下,发现挂不上柱)
2.配置磷酸钠盐缓冲液:按NaH2PO4:Na2HPO4以19:81的摩尔比配制成pH7.4的缓冲液?(附一张百度出来的配方
)
3.如果是磷酸钠盐缓冲液,可以直接将50mM的NaH2PO4的水溶液用NaOH调成pH7.4吗?
再者,2和3这两个方法配制的磷酸钠盐缓冲液有什么区别?最终效果是一样的吗?如果不一样,有什么理论的知识支撑呢?个人感觉是分析化学中酸碱理论中的缓冲液那里的知识。求帮忙解答这些疑问。
另外,我还想问一下,pH对于Ni柱对His-tagged的蛋白的分离纯化影响大吗?是怎么影响的?谢谢大家了!
有了源数据之后把源数据按照大小排列,
选中源数据区域-->ALT+A1-->选中图标区右键-->更改图表类型-->散点图
因为是考察不同PH对药物的影响,样品又不好改变其PH值,这种情况怎么办?希望有经验的高手指教。
我的流动相是甲醇-水(90:10)
谢谢赐教!
请进子版按格式发贴,自行修改,谢谢。
由弱酸及其盐、弱碱及其盐组成的混合溶液,能在一定程度上抵消、减轻外加强酸或强碱对溶液酸碱度的影响,从而保持溶液的pH值相对稳定。这种溶液称为缓冲溶液。
:)
我在做一细菌不同酸碱度生长状况时,发现这些奇怪现象:pH=3的培养基灭菌(TSB液体培养基)灭菌后pH上升到到9.2!而原来pH=9.0的降到8.7(基本没多少变化),请问各位大侠,这是什么原因?
一般做不同酸碱度生长实验时,该如何才能防止pH在湿热灭菌后基本不变化?
是否可以理解为纯化水得PH范围为6.3-7.6?能否直接用pH计测量?谢谢!

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