Phospholamban(PLB/PLN)isasmalltransmembraneproteinwhichplaysanimportantroleincontrollingtheactivityofthesarcoplasmicreticulumATPase(SERCA2a)ofcardiacmuscleduringcalciumsequestration.Phospholambanisphosphorylatedonseparateaminoacidresidues(Ser-16,Thr-17,Ser-10)bydifferentkinases.cAMP-dependent,andcGMP-dependentproteinkinasesphosphorylateSer-16.Theresultisanincreasedcalciumpumpactivitywhichreducesthetimecourseofthecalciumtransient,increasesthecalciumloadinthesarcoplasmicreticulum,andconsequently,producesalargercalciumtransientatthenextactionpotential.However,alterationinthishomeostaticinteractionhasbeenshowntoresultinheartfailure,underpinarrhythmiasandprovokesachangeinphenotypeofsmoothmusclecellsinatherosclerosis.
Testedapplications:WesternBlot(1:5000dilution),IHCMicroscopy(1:200dilution).Notyettestedinotherapplications,therefore,optimaldilutions/concentrationsshouldbedeterminedbytheuser.Speciesrecognition:Allmammalianspecies,whenphosphorylatedonSer-16.
Description | LyophilisedaffinitypurifiedRabbitpolyclonalantibody(A010-12AP)specificforSer-16phosphorylatedformsofPLB(Drago&Colyer,1994) |
Immunogen | Phosphopeptidecomprisingresidues9-19-Y(residuesR9SAIRRAS(PO3H2)TIE19Y)conjugatedtoKLH. |
Isotype | IgG |
Purification | ProteinAaffinitypurified |
Speciesreactivity | Theantibodyrecognisesmonoandoligomericphospholambanwhenphosphorylatedonserine-16byPKA.BindingoftheantibodytoitstargetepitopeisblockedinthepresenceofaphosphopeptidecontainingthePLBPhosphoSer-16epitope.AntibodyaffinityisreducedincircumstancesofdualphosphorylationofSer-16andThr-17. |
Testedapplications | WB,IHC |
Recommendeddilution | WB1:5000,IHC1:200 |
Optimization | Optimaldilutionstobedeterminedbyenduser |
Storage | Lyophilisedantibodyisstableat4°Cwhenstoredwithdesiccant.Reconstitutelyophilisedpowderin50µlof18MΩH2O,aliquotandstorefrozenat-80°Cfor1year.Avoidfreeze-thawcycles. |
Storage | Lyophilised:4°C.Reconstituted:-80°C |
Datasheet | A010-12AP |
MSDS | A010-12AP |
Regulatorystatement | Productforresearchuseonly.Notintendedfordiagnosticortherapeuticuse. |
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