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| AlternativeName: | Vasodilatorstimulatedphosphoprotein |
| Host: | Rabbit |
| Immunogen: | Recombinant humanVASP(vasodilatorstimulatedphosphoprotein)fusedtoaHis-tag. |
| UniProtID: | P50552 |
| Speciesreactivity: | Human |
| Specificity: | Recognizesunphosphorylatedaswellasphosphorylated(Ser157)VASP. |
| Crossreactivity: | Doesnotcross-reactwithmouseorratVASP.ForthedetectionofmouseVASPuseProd.No.ALX-210-880. |
| Applications: | IF,WB |
| RecommendedDilutions/Conditions: | Immunofluorescenceofformaldehydefixedcells(1:500-1:1000) WesternBlot(1:1500-1:3000) Suggesteddilutions/conditionsmaynotbeavailableforallapplications. Optimalconditionsmustbedeterminedindividuallyforeachapplication. |
| PositiveControl: | Humanplateletprotein(500µg),suppliedat5mg/mlinSDSsamplebuffer(100mMNaCl,73mMTRIS/HClpH6.7,10mMDTT,8mMEDTA,5%glycerol,2%SDS,10µg/mlBromophenolBluesodiumsalt).Use5µl(25µg)perlaneforWesternblottingoftricinegels(13%acrylamide)or15%Laemmligels. |
| Formulation: | Liquid.Contains0.02%sodiumazide. |
| Handling: | Avoidfreeze/thawcycles. |
| Shipping: | ShippedonBlueIce |
| ShortTermStorage: | +4°C |
| LongTermStorage: | -20°C |
| ScientificBackground: | VASP(vasodilatorstimulatedphosphoprotein)isaproline-richproteinsubstrateofcAMP-andcGMP-dependentproteinkinases.PhosphorylationofVASPatSer-157causesamobilityshiftinSDSgelelectrophoresisfrom46to50kDa,whichhasbeenusedasaconvenientMarkertomonitorcyclicnucleotide-dependentproteinkinaseactivity.VASPisthefoundingmemberoftheEna-VASPproteinfamily,comprisingtheDrosophilaproteinEnabled(Ena),itsmousehomologueMena(mammalianEnabled),andmouseEVL(Ena-VASP-likeprotein).WiththeseproteinsVASPsharesaconservedoveralldomainorganization: a)theconservedN-terminalEna-VASPhomologydomain1(EVH1),whichmediatesbindingtoaproline-richmotif b)amoredivergentproline-richcentraldomain(whichisresponsIBLeforprofilinbinding) c)aconservedC-terminalEVH2domain. VASPisexpressedinavarietyofmammaliancelltypesandtissues.Inculturedcells,VASPisassociatedwithfocaladhesions,cell-cellcontacts,MICROFILaments,andhighlydynamicmembraneregions.FrominvitrobindingdataVASPhasbeensuggestedtolinkprofilintozyxin,vinculin,andtheListeriaspp.surfaceproteinActA,respectively.FunctionalevidenceindicatesthatVASPisacrucialfactorinvolvedintheenhancementofactinfilamentformationandtheactin-dependentmotilityofintracellularbacterialpathogens. |
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