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- Peptide(C)TTKINMDDLQPSENEDKS,correspondingtoaminoacidresidues848-865ofratCaV1.2(Accession P22002).IntracellularloopbetweendomainsIIandIII.
- Westernblotanalysisofratbrainmembrane:1. Guineapig Anti-CaV1.2 (CACNA1C) Antibody(#AGP-001),(1:200).
2.GuineapigAnti-CaV1.2(CACNA1C)Antibody,preincubatedwiththenegativecontrolantigen.WesternblotanalysisofCaV1.2-transfected Xenopus oocytes(lane1)andnon-transfectedoocyteslysates(lane2):1. Guineapig Anti-CaV1.2 (CACNA1C) Antibody(#AGP-001),(1:200)in CaV1.2(CACNA1C)ChannelOverexpressedMembraneFractions(LX-104).
2.GuineapigAnti-CaV1.2(CACNA1C)Antibodyinnon-transfectedoocytes.
- Immuno-colocalizationofCaV1.2andGABA(A) α1ReceptorinratcerebellumImmunohistochemicalstainingofratcerebellumusingGuineapig Anti-CaV1.2 (CACNA1C) Antibody(#AGP-001)and Anti-GABA(A) α1Receptor(extracellular)-ATTO-488Antibody (#AGA-001-AG). A.CaV1.2(red)isdetectedmostlyinPurkinjecells(arrow).B.Inthesamesection, GABA(A)α1Receptor(green)isobservedinthegranulelayer.C.MergeofthetwoimagessuggestssomecolocalizationbetweenCaV1.2andGABA(A)α1ReceptorintheratgranulelayerbutonlyCaV1.2appearsinPurkinjecells.ExpressionofCaV1.2inhumanatriaImmunohistochemicalstainingofhumanleftatriumusingGuineapigAnti-CaV1.2 (CACNA1C) Antibody(#AGP-001),(1:100).
ThepicturewaskindlyprovidedbyDr.VanWagoner,D.R.fromtheDepartmentofMolecularCardiology,ClevelandClinic,Cleveland,Ohio,USA.Lovano,B.andPeterson,J.collectedthedata.ExpressionofCaV1.2inratheartImmunohistochemicalstainingofratheartparaffinembeddedsectionsusingGuineapig Anti-CaV1.2 (CACNA1C) Antibody(#AGP-001).A.CaV1.2staining(green)appearsmainlyinthecardiacmuscle,andinalesserintensityinthetunicaintimalayerofthesmoothmuscleofthemusculararteries.B.NuclearstainingusingDAPIasthecounterstain.C.MergedimagesofAandB.ExpressionofCaV1.2inmousehippocampusImmunohistochemicalstainingofmousedentategyrususing Guineapig Anti-CaV1.2 (CACNA1C) Antibody(#AGP-001).A.CaV1.2(green)appearedintheoutermolecularlayerofthedentategyrusandinthegranulelayer.B.CounterstainwithDAPI(blue)outlinesthegranulelayerofthedentategyrus.
- 1.Bauer,C.S.etal.(2010)Curr.Opin.Neurobiol.20,563.
- 2.Arikkath,J.etal.(2003)Curr.Opin.Neurobiol.13,298.
- 3.Catterall,W.A.(2000)Annu.Rev.Cell.Dev.Biol.16,521.
- 4.Davies,A.etal.(2007)TrendsPharmacol.Sci.28,220.
- 5.Dai,S.etal.(2009)Physiol.Rev.89,411.
- 6.Zuccotti,A.etal.(2011)TrendsPharmacol.Sci.32,366.
- 7.Hell,J.W.etal.(1996)Proc.Natl.Acad.Sci.U.S.A.93,3362.
- 8.DeJongh,K.S.etal.(1996)Biochemistry35,10392.
- 9.Gao,T.etal.(2001)J.Biol.Chem.276,21089.
- 10.Liao,P.etal.(2010)Pflugers.Arch.460,353.
Voltage-gatedCa2+ channels(CaV),enablethepassageofCa2+ ionsinavoltagedependentmanner.Theseheteromericentitiesareformedinpartbythepore-forming α1subunitwhichdeterminesthebiophysicalandpharmacologicalpropertiesofthechannel1.
L-typeCa2+ channelsmakeuponeofthreevoltage-gatedCa2+ channelfamilies.Fourdifferent α1isoforms(CaV1.1toCaV1.4)belongtotheL-typesubfamily.Structurally,each α1subunithasfourhomologousdomains(I-IV)andeachdomainhasasixtransmembranesection.Likemanyothervoltage-gatedchannels,L-typeCa2+ channelshaveauxiliarysubunitswhichareresponsIBLeformodulatingthesurfaceexpressionandpropertiesofthechannels2-5.
CaV1.1ismostlyexpressedintheskeletalmuscle,whileCaV1.4ismainlydetectedintheretina.TheexpressionofbothCaV1.2and CaV1.3 ismoreextensiveandincludesneurons,heart,smoothmuscle,innerear,retinaandpancreas6.L-typeCa2+ channelsareinvolvedinandmodulateavarietyofphysiologicalfunctionssuchasmusclecontraction,hormonesecretion,neuronalexcitABIlityandgeneexpression5.
CaV1.2undergoesvariouspost-translationalmodifications.Forexample,itcanundergoproteolyticcleavageatitsC-terminal.Thiscleavagehasbeenshowntotakeplaceinneuronsfollowingtheactivationof NMDA receptors5,7 andintheheart5,8,9.Thecleavedmoietycanstillinteractwiththechannelanditsgeneralpurposeistomodulatechannelactivity5.OtherpostranslationmodificationsofthechannelincludephosphorylationofCaV1.2byanumberofkinasessuchasPKA,PKC,SrcandCaMKII5.Inaddition,itisnotsurprisingthatphosphatasesalsoregulatechannelactivity,astheyarerequiredtoantagonizetheactivityofthevariouskinasesknowntophosphorylateCaV1.2 5.
ThefactthatCaV1.2playsaprominentroleinpropercardiacfunctionhaspromptedendlessstudiesregardingitsregulation.Suchstudieshaveconcludedthatdysregulationofthechannelleadstoanomaliesinheartcontractionandthusheartfailure5.Likewise,CaV1.2defectshavebeendetectedinautismandbipolardisorder10.
Immuno-colocalizationofCaV1.2andGABA(A) α1ReceptorinratandmousehippocampusImmunohistochemicalstainingofmouseandrathippocampaldentategyrususingGuineapig Anti-CaV1.2 (CACNA1C) Antibody(#AGP-001)and Anti-GABA(A)α1Receptor(extracellular)-ATTO-488Antibody (#AGA-001-AG)inthesamesection.BothCaV1.2(red)andGABA(A)α1Receptor(green)aredetectedinneuron-shapedcells(arrows).StainingsuggestspartialcolocalizationbetweenCaV1.2andGABA(A)α1Receptorinasub-populationofdentategyrusneurons.A.Mousehippocampus.B.Rathippocampus.
GuineapigAnti-CaV1.2(CACNA1C)Antibody(#AGP-001),raisedinguineapigs,isahighlyspecificantibodydirectedagainstanepitopeoftheratprotein.Theantibodycanbeusedinwesternblotandimmunohistochemistryapplications.ItandhasbeendesignedtorecognizeCaV1.2frommouse,ratandhumansamples.TheantigenusedtoimmunizeguineapigsisthesameasAnti-CaV1.2(CACNA1C)Antibody(#ACC-003)raisedinrabbit.Ourlineofguineapigantibodiesenablesmoreflexibilitywithourproductssuchasimmuno-colocalizationstudies,immunoprecipitation,etc.